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  • Phosphorylation  (275)
  • American Association for the Advancement of Science (AAAS)  (275)
  • Blackwell Publishing Ltd
  • 2000-2004  (275)
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  • American Association for the Advancement of Science (AAAS)  (275)
  • Blackwell Publishing Ltd
  • Springer  (2)
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Year
  • 1
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    Genomic instability in mice lacking histone H2AX (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-06
    Description: Higher order chromatin structure presents a barrier to the recognition and repair of DNA damage. Double-strand breaks (DSBs) induce histone H2AX phosphorylation, which is associated with the recruitment of repair factors to damaged DNA. To help clarify the physiological role of H2AX, we targeted H2AX in mice. Although H2AX is not essential for irradiation-induced cell-cycle checkpoints, H2AX-/- mice were radiation sensitive, growth retarded, and immune deficient, and mutant males were infertile. These pleiotropic phenotypes were associated with chromosomal instability, repair defects, and impaired recruitment of Nbs1, 53bp1, and Brca1, but not Rad51, to irradiation-induced foci. Thus, H2AX is critical for facilitating the assembly of specific DNA-repair complexes on damaged DNA.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721576/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721576/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Celeste, Arkady -- Petersen, Simone -- Romanienko, Peter J -- Fernandez-Capetillo, Oscar -- Chen, Hua Tang -- Sedelnikova, Olga A -- Reina-San-Martin, Bernardo -- Coppola, Vincenzo -- Meffre, Eric -- Difilippantonio, Michael J -- Redon, Christophe -- Pilch, Duane R -- Olaru, Alexandru -- Eckhaus, Michael -- Camerini-Otero, R Daniel -- Tessarollo, Lino -- Livak, Ferenc -- Manova, Katia -- Bonner, William M -- Nussenzweig, Michel C -- Nussenzweig, Andre -- Z99 CA999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2002 May 3;296(5569):922-7. Epub 2002 Apr 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, NIH, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11934988" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; B-Lymphocytes/immunology/physiology ; Base Sequence ; Cell Aging ; Cell Cycle ; Cells, Cultured ; *Chromosome Aberrations ; DNA Damage ; *DNA Repair ; Female ; Gene Targeting ; Histones/chemistry/*genetics/*physiology ; Immunoglobulin Class Switching ; Infertility, Male/genetics/physiopathology ; Lymphocyte Count ; Male ; Meiosis ; Mice ; Mice, Knockout ; Molecular Sequence Data ; Mutation ; Phosphorylation ; *Recombination, Genetic ; Spermatocytes/physiology ; T-Lymphocytes/immunology/physiology
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 2
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    Biomedicine. Ataxin-1 regulators in the spotlight (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heintz, Nathaniel -- New York, N.Y. -- Science. 2003 Jul 4;301(5629):59-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, Rockefeller University, New York, NY 10021, USA. heintz@rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12843383" target="_blank"〉PubMed〈/a〉
    Keywords: 14-3-3 Proteins ; Amino Acid Substitution ; Animals ; Ataxin-1 ; Ataxins ; Cell Nucleus/metabolism ; Disease Progression ; Mice ; Mice, Transgenic ; Mutation ; Nerve Tissue Proteins/*chemistry/genetics/*metabolism ; Nuclear Proteins/*chemistry/genetics/*metabolism ; Peptides ; Phosphorylation ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/*metabolism ; Proto-Oncogene Proteins c-akt ; Purkinje Cells/metabolism/ultrastructure ; Signal Transduction ; Spinocerebellar Ataxias/etiology/genetics/pathology/*physiopathology ; *Trinucleotide Repeat Expansion ; Tyrosine 3-Monooxygenase/*metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 3
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    Cell biology. Microtubule asymmetry (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gundersen, Gregg G -- Bretscher, Anthony -- New York, N.Y. -- Science. 2003 Jun 27;300(5628):2040-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Anatomy and Cell Biology and Department of Pathology, Columbia University, New York, NY 10032, USA. ggg1@columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12829769" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; CDC28 Protein Kinase, S cerevisiae/*metabolism ; Cell Cycle Proteins/metabolism ; Cell Division ; Cell Polarity ; Cyclins/metabolism ; Microtubule Proteins/metabolism ; Microtubule-Organizing Center/*metabolism/ultrastructure ; Microtubules/*metabolism/ultrastructure ; Models, Biological ; Mutation ; Myosin Heavy Chains/metabolism ; Myosin Type V/metabolism ; Nuclear Proteins/*metabolism ; Phosphorylation ; Protein Transport ; Saccharomyces cerevisiae/cytology/metabolism/ultrastructure ; Saccharomyces cerevisiae Proteins/metabolism ; Spindle Apparatus/*physiology/ultrastructure
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 4
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    Role of Raf in vascular protection from distinct apoptotic stimuli (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-07-05
    Description: Raf kinases have been linked to endothelial cell survival. Here, we show that basic fibroblast growth factor (bFGF) and vascular endothelial growth factor (VEGF) differentially activate Raf, resulting in protection from distinct pathways of apoptosis in human endothelial cells and chick embryo vasculature. bFGF activated Raf-1 via p21-activated protein kinase-1 (PAK-1) phosphorylation of serines 338 and 339, resulting in Raf-1 mitochondrial translocation and endothelial cell protection from the intrinsic pathway of apoptosis, independent of the mitogen-activated protein kinase kinase-1 (MEK1). In contrast, VEGF activated Raf-1 via Src kinase, leading to phosphorylation of tyrosines 340 and 341 and MEK1-dependent protection from extrinsic-mediated apoptosis. These findings implicate Raf-1 as a pivotal regulator of endothelial cell survival during angiogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Alavi, Alireza -- Hood, John D -- Frausto, Ricardo -- Stupack, Dwayne G -- Cheresh, David A -- CA45726/CA/NCI NIH HHS/ -- CA50286/CA/NCI NIH HHS/ -- CA75924/CA/NCI NIH HHS/ -- P01 CA78045/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2003 Jul 4;301(5629):94-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12843393" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cell Survival ; Cells, Cultured ; Chick Embryo ; Endothelial Growth Factors/pharmacology ; Endothelium, Vascular/*cytology/drug effects ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Fibroblast Growth Factor 2/pharmacology ; Flavonoids/pharmacology ; Humans ; Intercellular Signaling Peptides and Proteins/pharmacology ; Lymphokines/pharmacology ; MAP Kinase Kinase 1 ; Mitochondria/metabolism ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinase Kinases/antagonists & inhibitors/metabolism ; Mitogen-Activated Protein Kinases/metabolism ; Neovascularization, Pathologic ; *Neovascularization, Physiologic/drug effects ; Phosphorylation ; Point Mutation ; Protein Transport ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Proto-Oncogene Proteins B-raf ; Proto-Oncogene Proteins c-raf/chemistry/genetics/*metabolism ; Signal Transduction ; Umbilical Veins ; Vascular Endothelial Growth Factor A ; Vascular Endothelial Growth Factors ; p21-Activated Kinases ; src-Family Kinases/antagonists & inhibitors/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 5
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    Botany. State transitions--a question of balance (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Allen, John F -- New York, N.Y. -- Science. 2003 Mar 7;299(5612):1530-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Plant Biochemistry, Center for Chemistry and Chemical Engineering, Box 124, Lund University, SE-221 00 Lund, Sweden. john.allen@plantbio.lu.se〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12624254" target="_blank"〉PubMed〈/a〉
    Keywords: Algal Proteins/chemistry/genetics/isolation & purification/metabolism ; Animals ; Binding Sites ; Chlamydomonas reinhardtii/*enzymology/genetics/metabolism ; Chlorophyll/metabolism ; Electron Transport ; Fluorescence ; Gene Library ; Light ; Light-Harvesting Protein Complexes ; Models, Biological ; Mutation ; Oxidation-Reduction ; Phosphorylation ; Photosynthesis ; Photosynthetic Reaction Center Complex Proteins/*metabolism ; Plastoquinone/metabolism ; Protein-Serine-Threonine Kinases/chemistry/genetics/*isolation & ; purification/*metabolism ; Signal Transduction ; Thylakoids/*enzymology ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 6
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    Derepression of BDNF transcription involves calcium-dependent phosphorylation of MeCP2 (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-01
    Description: Mutations in MeCP2, which encodes a protein that has been proposed to function as a global transcriptional repressor, are the cause of Rett syndrome (RT T), an X-linked progressive neurological disorder. Although the selective inactivation of MeCP2 in neurons is sufficient to confer a Rett-like phenotype in mice, the specific functions of MeCP2 in postmitotic neurons are not known. We find that MeCP2 binds selectively to BDNF promoter III and functions to repress expression of the BDNF gene. Membrane depolarization triggers the calcium-dependent phosphorylation and release of MeCP2 from BDNF promoter III, thereby facilitating transcription. These studies indicate that MeCP2 plays a key role in the control of neuronal activity-dependent gene regulation and suggest that the deregulation of this process may underlie the pathology of RT T.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, Wen G -- Chang, Qiang -- Lin, Yingxi -- Meissner, Alexander -- West, Anne E -- Griffith, Eric C -- Jaenisch, Rudolf -- Greenberg, Michael E -- HD 18655/HD/NICHD NIH HHS/ -- NS28829/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2003 Oct 31;302(5646):885-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neuroscience, Children's Hospital, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14593183" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain-Derived Neurotrophic Factor/*genetics ; Calcium/*metabolism ; Cell Membrane/physiology ; Cells, Cultured ; *Chromosomal Proteins, Non-Histone ; Cloning, Molecular ; CpG Islands ; DNA Methylation ; DNA-Binding Proteins/*metabolism ; Electrophoretic Mobility Shift Assay ; *Gene Expression Regulation ; Gene Silencing ; Histones/metabolism ; Methyl-CpG-Binding Protein 2 ; Methylation ; Mice ; Mice, Knockout ; Neurons/metabolism/physiology ; Phosphorylation ; Potassium Chloride/pharmacology ; Precipitin Tests ; Promoter Regions, Genetic ; Rats ; *Repressor Proteins ; Rett Syndrome/genetics ; *Transcription, Genetic
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  • 7
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    Diverse psychotomimetics act through a common signaling pathway (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-11-25
    Description: Three distinct classes of drugs: dopaminergic agonists (such as D-amphetamine), serotonergic agonists (such as LSD), and glutamatergic antagonists (such as PCP) all induce psychotomimetic states in experimental animals that closely resemble schizophrenia symptoms in humans. Here we implicate a common signaling pathway in mediating these effects. In this pathway, dopamine- and an adenosine 3',5'-monophosphate (cAMP)-regulated phospho-protein of 32 kilodaltons (DARPP-32) is phosphorylated or dephosphorylated at three sites, in a pattern predicted to cause a synergistic inhibition of protein phosphatase-1 and concomitant regulation of its downstream effector proteins glycogen synthesis kinase-3 (GSK-3), cAMP response element-binding protein (CREB), and c-Fos. In mice with a genetic deletion of DARPP-32 or with point mutations in phosphorylation sites of DARPP-32, the effects of D-amphetamine, LSD, and PCP on two behavioral parameters-sensorimotor gating and repetitive movements-were strongly attenuated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Svenningsson, Per -- Tzavara, Eleni T -- Carruthers, Robert -- Rachleff, Ilan -- Wattler, Sigrid -- Nehls, Michael -- McKinzie, David L -- Fienberg, Allen A -- Nomikos, George G -- Greengard, Paul -- DA10044/DA/NIDA NIH HHS/ -- MH40899/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2003 Nov 21;302(5649):1412-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/14631045" target="_blank"〉PubMed〈/a〉
    Keywords: 1-Methyl-4-phenyl-1,2,3,6-tetrahydropyridine/pharmacology ; Animals ; Brain/drug effects/*metabolism ; Central Nervous System Agents/*pharmacology ; Corpus Striatum/drug effects/metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Dextroamphetamine/pharmacology ; Dopamine/metabolism ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Frontal Lobe/drug effects/metabolism ; Genes, fos ; Glycogen Synthase Kinase 3/metabolism ; Lysergic Acid Diethylamide/pharmacology ; Male ; Mice ; Mice, Knockout ; Motor Activity/drug effects ; Nerve Tissue Proteins/metabolism ; Phencyclidine/pharmacology ; Phosphoprotein Phosphatases/antagonists & inhibitors ; Phosphoproteins/*metabolism ; Phosphorylation ; Protein Phosphatase 1 ; RNA, Messenger/genetics/metabolism ; Receptors, Dopamine D1/genetics/metabolism ; Reflex, Startle/drug effects ; *Signal Transduction ; Synaptic Transmission
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 8
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    Disruption of transforming growth factor-beta signaling in ELF beta-spectrin-deficient mice (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-01-25
    Description: Disruption of the adaptor protein ELF, a beta-spectrin, leads to disruption of transforming growth factor-beta (TGF-beta) signaling by Smad proteins in mice. Elf-/- mice exhibit a phenotype similar to smad2+/-/smad3+/- mutant mice of midgestational death due to gastrointestinal, liver, neural, and heart defects. We show that TGF-beta triggers phosphorylation and association of ELF with Smad3 and Smad4, followed by nuclear translocation. ELF deficiency results in mislocalization of Smad3 and Smad4 and loss of the TGF-beta-dependent transcriptional response, which could be rescued by overexpression of the COOH-terminal region of ELF. This study reveals an unexpected molecular link between a major dynamic scaffolding protein and a key signaling pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tang, Yi -- Katuri, Varalakshmi -- Dillner, Allan -- Mishra, Bibhuti -- Deng, Chu-Xia -- Mishra, Lopa -- R01 DK56111/DK/NIDDK NIH HHS/ -- R01 DK58637/DK/NIDDK NIH HHS/ -- R03 DK53861/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2003 Jan 24;299(5606):574-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Biology, Department of Medicine, Georgetown University, Washington, DC 20007, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12543979" target="_blank"〉PubMed〈/a〉
    Keywords: Abnormalities, Multiple ; Animals ; Carrier Proteins/metabolism ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; Contractile Proteins/metabolism ; DNA-Binding Proteins/metabolism ; Embryonic and Fetal Development ; Filamins ; Gene Targeting ; Genes, fos ; Liver/abnormalities/embryology/*metabolism ; Mice ; Mice, Knockout ; Microfilament Proteins/metabolism ; Microscopy, Confocal ; Mutation ; Phenotype ; Phosphorylation ; Platelet-Derived Growth Factor/pharmacology ; *Signal Transduction ; Smad2 Protein ; Smad3 Protein ; Smad4 Protein ; Spectrin/genetics/*metabolism ; Trans-Activators/metabolism ; Transcriptional Activation ; Transforming Growth Factor beta/*metabolism/pharmacology ; Tumor Cells, Cultured
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 9
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    Activation of the DNA replication checkpoint through RNA synthesis by primase (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-23
    Description: When DNA replication is inhibited during the synthesis (S) phase of the cell cycle, a signaling pathway (checkpoint) is activated that serves to prevent mitosis from initiating before completion of replication. This replication checkpoint acts by down-regulating the activity of the mitotic inducer cdc2-cyclin B. Here, we report the relation between chromatin structure and induction of the replication checkpoint. Chromatin was competent to initiate a checkpoint response only after the DNA was unwound and DNA polymerase alpha had been loaded. Checkpoint induction did not require new DNA synthesis on the unwound template strand but did require RNA primer synthesis by primase. These findings identify the RNA portion of the primer as an important component of the signal that activates the replication checkpoint.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Michael, W M -- Ott, R -- Fanning, E -- Newport, J -- 52948/PHS HHS/ -- R01GM33523-16/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2133-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biology, University of California, San Diego, La Jolla, CA 92093-0349, USA. matt@mcb.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11000117" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aphidicolin/pharmacology ; *CDC2-CDC28 Kinases ; Carrier Proteins/metabolism ; Chromatin/*metabolism ; Cyclin E/metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/metabolism ; DNA Helicases/metabolism ; DNA Polymerase I/antagonists & inhibitors/metabolism ; DNA Primase/*metabolism ; *DNA Replication/drug effects ; DNA, Single-Stranded/metabolism ; DNA-Binding Proteins/metabolism ; Mitosis ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; RNA/*biosynthesis ; Recombinant Proteins/metabolism ; S Phase ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Xenopus ; Xenopus Proteins
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 10
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    Two-amino acid molecular switch in an epithelial morphogen that regulates binding to two distinct receptors (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-20
    Description: Ectodysplasin, a member of the tumor necrosis factor family, is encoded by the anhidrotic ectodermal dysplasia (EDA) gene. Mutations in EDA give rise to a clinical syndrome characterized by loss of hair, sweat glands, and teeth. EDA-A1 and EDA-A2 are two isoforms of ectodysplasin that differ only by an insertion of two amino acids. This insertion functions to determine receptor binding specificity, such that EDA-A1 binds only the receptor EDAR, whereas EDA-A2 binds only the related, but distinct, X-linked ectodysplasin-A2 receptor (XEDAR). In situ binding and organ culture studies indicate that EDA-A1 and EDA-A2 are differentially expressed and play a role in epidermal morphogenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yan, M -- Wang, L C -- Hymowitz, S G -- Schilbach, S -- Lee, J -- Goddard, A -- de Vos, A M -- Gao, W Q -- Dixit, V M -- New York, N.Y. -- Science. 2000 Oct 20;290(5491):523-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Oncology, Genentech, 1 DNA Way, South San Francisco, CA 94080, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11039935" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Binding Sites ; Cell Line ; DNA-Binding Proteins/metabolism ; Ectodermal Dysplasia/genetics ; Ectodysplasins ; Epidermis/embryology/*metabolism ; Humans ; *I-kappa B Proteins ; In Situ Hybridization ; Ligands ; Membrane Proteins/*chemistry/*metabolism ; Mice ; Models, Molecular ; Molecular Sequence Data ; Morphogenesis ; NF-kappa B/metabolism ; Phosphorylation ; Point Mutation ; Protein Conformation ; Proteins/metabolism ; Receptors, Cell Surface/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; TNF Receptor-Associated Factor 6 ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 11
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    Prokaryotic regulation of epithelial responses by inhibition of IkappaB-alpha ubiquitination (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-01
    Description: Epithelia of the vertebrate intestinal tract characteristically maintain an inflammatory hyporesponsiveness toward the lumenal prokaryotic microflora. We report the identification of enteric organisms (nonvirulent Salmonella strains) whose direct interaction with model human epithelia attenuate synthesis of inflammatory effector molecules elicited by diverse proinflammatory stimuli. This immunosuppressive effect involves inhibition of the inhibitor kappaB/nuclear factor kappaB (IkappaB/NF-kappaB) pathway by blockade of IkappaB-alpha degradation, which prevents subsequent nuclear translocation of active NF-kappaB dimer. Although phosphorylation of IkappaB-alpha occurs, subsequent polyubiquitination necessary for regulated IkappaB-alpha degradation is completely abrogated. These data suggest that prokaryotic determinants could be responsible for the unique tolerance of the gastrointestinal mucosa to proinflammatory stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neish, A S -- Gewirtz, A T -- Zeng, H -- Young, A N -- Hobert, M E -- Karmali, V -- Rao, A S -- Madara, J L -- DK-35932/DK/NIDDK NIH HHS/ -- DK-47662/DK/NIDDK NIH HHS/ -- DK09800/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Sep 1;289(5484):1560-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Epithelial Pathobiology Unit, Department of Pathology and Laboratory Medicine, Emory University School of Medicine, Atlanta, GA 30322, USA. aneish@emory.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10968793" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/metabolism ; Cysteine Proteinase Inhibitors/pharmacology ; Cytoskeletal Proteins/metabolism ; DNA-Binding Proteins/*metabolism ; Dimerization ; Humans ; *I-kappa B Proteins ; Inflammation Mediators/pharmacology ; Interleukin-8/genetics/metabolism ; Intestinal Mucosa/*metabolism/*microbiology ; Leupeptins/pharmacology ; Ligases/metabolism ; NF-kappa B/genetics/*metabolism ; Phosphorylation ; Salmonella/pathogenicity/*physiology ; Salmonella typhimurium/pathogenicity/physiology ; *Trans-Activators ; Transcription Factor RelA ; Tumor Cells, Cultured ; Tumor Necrosis Factor-alpha/pharmacology ; Ubiquitin-Protein Ligases ; Ubiquitins/metabolism ; beta Catenin
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  • 12
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    Structural mechanism for STI-571 inhibition of abelson tyrosine kinase (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-09-16
    Description: The inadvertent activation of the Abelson tyrosine kinase (Abl) causes chronic myelogenous leukemia (CML). A small-molecule inhibitor of Abl (STI-571) is effective in the treatment of CML. We report the crystal structure of the catalytic domain of Abl, complexed to a variant of STI-571. Critical to the binding of STI-571 is the adoption by the kinase of an inactive conformation, in which a centrally located "activation loop" is not phosphorylated. The conformation of this loop is distinct from that in active protein kinases, as well as in the inactive form of the closely related Src kinases. These results suggest that compounds that exploit the distinctive inactivation mechanisms of individual protein kinases can achieve both high affinity and high specificity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Schindler, T -- Bornmann, W -- Pellicena, P -- Miller, W T -- Clarkson, B -- Kuriyan, J -- GM29362/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 15;289(5486):1938-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratories of Molecular Biophysics and Howard Hughes Medical Institute, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10988075" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antineoplastic Agents/chemistry/*pharmacology ; Benzamides ; Catalytic Domain ; Crystallography, X-Ray ; Enzyme Activation ; Enzyme Inhibitors/chemistry/*pharmacology ; Humans ; Imatinib Mesylate ; Mice ; Models, Molecular ; Phosphorylation ; *Piperazines ; Protein Conformation ; Proto-Oncogene Proteins c-abl/*antagonists & inhibitors/chemistry/metabolism ; Pyrimidines/chemistry/*pharmacology ; Recombinant Fusion Proteins ; Structure-Activity Relationship
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  • 13
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    Rapid destruction of human Cdc25A in response to DNA damage (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-29
    Description: To protect genome integrity and ensure survival, eukaryotic cells exposed to genotoxic stress cease proliferating to provide time for DNA repair. Human cells responded to ultraviolet light or ionizing radiation by rapid, ubiquitin- and proteasome-dependent protein degradation of Cdc25A, a phosphatase that is required for progression from G1 to S phase of the cell cycle. This response involved activated Chk1 protein kinase but not the p53 pathway, and the persisting inhibitory tyrosine phosphorylation of Cdk2 blocked entry into S phase and DNA replication. Overexpression of Cdc25A bypassed this mechanism, leading to enhanced DNA damage and decreased cell survival. These results identify specific degradation of Cdc25A as part of the DNA damage checkpoint mechanism and suggest how Cdc25A overexpression in human cancers might contribute to tumorigenesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mailand, N -- Falck, J -- Lukas, C -- Syljuasen, R G -- Welcker, M -- Bartek, J -- Lukas, J -- New York, N.Y. -- Science. 2000 May 26;288(5470):1425-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cancer Biology, Danish Cancer Society, Strandboulevarden 49, DK-2100 Copenhagen, Denmark.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10827953" target="_blank"〉PubMed〈/a〉
    Keywords: *CDC2-CDC28 Kinases ; Cell Line ; Cell Survival ; Cyclin E/metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/antagonists & inhibitors/metabolism ; Cysteine Endopeptidases/metabolism ; *DNA Damage ; DNA Repair ; DNA Replication ; G1 Phase ; Humans ; Multienzyme Complexes/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Proteasome Endopeptidase Complex ; Protein Kinase Inhibitors ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; Recombinant Fusion Proteins/metabolism ; S Phase ; Transfection ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/metabolism ; Ultraviolet Rays ; cdc25 Phosphatases/genetics/*metabolism
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  • 14
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    Quantitative imaging of lateral ErbB1 receptor signal propagation in the plasma membrane (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-11-25
    Description: Evidence for a new signaling mechanism consisting of ligand-independent lateral propagation of receptor activation in the plasma membrane is presented. We visualized the phosphorylation of green fluorescent protein (GFP)-tagged ErbB1 (ErbB1-GFP) receptors in cells focally stimulated with epidermal growth factor (EGF) covalently attached to beads. This was achieved by quantitative imaging of protein reaction states in cells by fluorescence resonance energy transfer (FRET) with global analysis of fluorescence lifetime imaging microscopy (FLIM) data. The rapid and extensive propagation of receptor phosphorylation over the entire cell after focal stimulation demonstrates a signaling wave at the plasma membrane resulting in full activation of all receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Verveer, P J -- Wouters, F S -- Reynolds, A R -- Bastiaens, P I -- New York, N.Y. -- Science. 2000 Nov 24;290(5496):1567-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cell Biology and Cell Biophysics Program, European Molecular Biology Laboratory, Meyerhofstrasse 1, 69117 Heidelberg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11090353" target="_blank"〉PubMed〈/a〉
    Keywords: Arsenicals/pharmacology ; Carbocyanines ; Cell Membrane/*metabolism ; Diffusion ; Dimerization ; Endocytosis ; Energy Transfer ; Enzyme Inhibitors/pharmacology ; Epidermal Growth Factor/*metabolism/pharmacology ; Fluorescence ; Fluorescent Dyes ; Green Fluorescent Proteins ; Humans ; Immunoglobulin Fab Fragments ; Ligands ; Luminescent Proteins ; Microscopy, Confocal ; Microscopy, Fluorescence ; Microspheres ; Phosphorylation ; Phosphotyrosine/immunology ; Protein Tyrosine Phosphatases/antagonists & inhibitors/metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; *Signal Transduction ; Tumor Cells, Cultured
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  • 15
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    Requirement for DARPP-32 in progesterone-facilitated sexual receptivity in female rats and mice (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-02-11
    Description: DARPP-32, a dopamine- and adenosine 3',5'-monophosphate (cAMP)-regulated phosphoprotein (32 kilodaltons in size), is an obligate intermediate in progesterone (P)-facilitated sexual receptivity in female rats and mice. The facilitative effect of P on sexual receptivity in female rats was blocked by antisense oligonucleotides to DARPP-32. Homozygous mice carrying a null mutation for the DARPP-32 gene exhibited minimal levels of P-facilitated sexual receptivity when compared to their wild-type littermates. P significantly increased hypothalamic cAMP levels and cAMP-dependent protein kinase activity. These increases were not inhibited by a D1 subclass dopamine receptor antagonist. P also enhanced phosphorylation of DARPP-32 on threonine 34 in the hypothalamus of mice. DARPP-32 activation is thus an obligatory step in progestin receptor regulation of sexual receptivity in rats and mice.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mani, S K -- Fienberg, A A -- O'Callaghan, J P -- Snyder, G L -- Allen, P B -- Dash, P K -- Moore, A N -- Mitchell, A J -- Bibb, J -- Greengard, P -- O'Malley, B W -- MH49662/MH/NIMH NIH HHS/ -- MH57442/MH/NIMH NIH HHS/ -- NS 35457/NS/NINDS NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1053-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Baylor College of Medicine, Houston, TX 77030, USA. smani@bcm.tmc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669419" target="_blank"〉PubMed〈/a〉
    Keywords: 2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-benzazepine/pharmacology ; Animals ; Cyclic AMP/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Dopamine/pharmacology ; Dopamine Agonists/pharmacology ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Female ; Hypothalamus/metabolism ; Injections, Intraventricular ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; *Nerve Tissue Proteins ; Oligonucleotides, Antisense/pharmacology ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; Posture ; Progesterone/*pharmacology ; Proteins/genetics/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, Progesterone/metabolism ; Serotonin/pharmacology ; Sexual Behavior, Animal/*drug effects ; Signal Transduction
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    Receptor-mediated activation of heterotrimeric G-proteins in living cells (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-03-27
    Description: Receptor-mediated activation of heterotrimeric GTP-binding proteins (G-proteins) was visualized in living Dictyostelium discoideum cells by monitoring fluorescence resonance energy transfer (FRET) between alpha- and beta- subunits fused to cyan and yellow fluorescent proteins. The G-protein heterotrimer rapidly dissociated and reassociated upon addition and removal of chemoattractant. During continuous stimulation, G-protein activation reached a dose-dependent steady-state level. Even though physiological responses subsided, the activation did not decline. Thus, adaptation occurs at another point in the signaling pathway, and occupied receptors, whether or not they are phosphorylated, catalyze the G-protein cycle. Construction of similar energy-transfer pairs of mammalian G-proteins should enable direct in situ mechanistic studies and applications such as drug screening and identifying ligands of newly found G-protein-coupled receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Janetopoulos, C -- Jin, T -- Devreotes, P -- GM28007/GM/NIGMS NIH HHS/ -- GM34933/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2408-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins Medical Institutions, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11264536" target="_blank"〉PubMed〈/a〉
    Keywords: 8-Bromo Cyclic Adenosine Monophosphate/pharmacology ; Animals ; Bacterial Proteins ; Cyclic AMP/metabolism/*pharmacology ; Deoxyadenine Nucleotides/pharmacology ; Dictyostelium/*metabolism ; Energy Transfer ; Fluorescence ; Guanosine 5'-O-(3-Thiotriphosphate)/pharmacology ; Heterotrimeric GTP-Binding Proteins/*metabolism ; Kinetics ; Ligands ; Luminescent Proteins ; Microscopy, Fluorescence ; Phosphorylation ; Receptors, Cyclic AMP/*metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Spectrometry, Fluorescence ; Transformation, Genetic
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  • 17
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    Interaction of the response regulator ARR4 with phytochrome B in modulating red light signaling (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-11-03
    Description: The Arabidopsis thaliana response regulator 4, expressed in response to phytochrome B action, specifically interacts with the extreme amino-terminus of the photoreceptor. The response regulator 4 stabilizes the active Pfr form of phytochrome B in yeast and in planta, thus elevates the level of the active photoreceptor in vivo. Accordingly, transgenic Arabidopsis plants overexpressing the response regulator 4 display hypersensitivity to red light but not to light of other wavelengths. We propose that the response regulator 4 acts as an output element of a two-component system that modulates red light signaling on the level of the phytochrome B photoreceptor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sweere, U -- Eichenberg, K -- Lohrmann, J -- Mira-Rodado, V -- Baurle, I -- Kudla, J -- Nagy, F -- Schafer, E -- Harter, K -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1108-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut fur Biologie II / Botanik, Universitat Freiburg, Schanzlestrasse 1, 79104 Freiburg, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691995" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/*metabolism/radiation effects ; Arabidopsis Proteins/genetics/*metabolism ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; Darkness ; Genes, Plant ; *Light ; Phenotype ; Phosphorylation ; *Photoreceptor Cells ; Phytochrome/chemistry/*metabolism ; Phytochrome B ; Plants, Genetically Modified ; Protein Conformation ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; *Transcription Factors ; Two-Hybrid System Techniques ; Yeasts/genetics/metabolism
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    Translating the histone code (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-08-11
    Description: Chromatin, the physiological template of all eukaryotic genetic information, is subject to a diverse array of posttranslational modifications that largely impinge on histone amino termini, thereby regulating access to the underlying DNA. Distinct histone amino-terminal modifications can generate synergistic or antagonistic interaction affinities for chromatin-associated proteins, which in turn dictate dynamic transitions between transcriptionally active or transcriptionally silent chromatin states. The combinatorial nature of histone amino-terminal modifications thus reveals a "histone code" that considerably extends the information potential of the genetic code. We propose that this epigenetic marking system represents a fundamental regulatory mechanism that has an impact on most, if not all, chromatin-templated processes, with far-reaching consequences for cell fate decisions and both normal and pathological development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Jenuwein, T -- Allis, C D -- GM53512/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 10;293(5532):1074-80.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Research Institute of Molecular Pathology (IMP) at the Vienna Biocenter, Dr. Bohrgasse 7, A-1030 Vienna, Austria. jenuwein@nt.imp.univie.ac.at〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11498575" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Amino Acid Sequence ; Animals ; Chromatin/chemistry/metabolism/ultrastructure ; *Gene Expression Regulation ; *Gene Silencing ; Genomic Imprinting ; Histones/chemistry/genetics/*metabolism ; Methylation ; Molecular Sequence Data ; Phosphorylation ; Protein Structure, Tertiary ; Transcription, Genetic ; Transcriptional Activation
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    Taking cell-matrix adhesions to the third dimension (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-11-27
    Description: Adhesions between fibroblastic cells and extracellular matrix have been studied extensively in vitro, but little is known about their in vivo counterparts. Here, we characterized the composition and function of adhesions in three-dimensional (3D) matrices derived from tissues or cell culture. "3D-matrix adhesions" differ from focal and fibrillar adhesions characterized on 2D substrates in their content of alpha5beta1 and alphavbeta3 integrins, paxillin, other cytoskeletal components, and tyrosine phosphorylation of focal adhesion kinase (FAK). Relative to 2D substrates, 3D-matrix interactions also display enhanced cell biological activities and narrowed integrin usage. These distinctive in vivo 3D-matrix adhesions differ in structure, localization, and function from classically described in vitro adhesions, and as such they may be more biologically relevant to living organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cukierman, E -- Pankov, R -- Stevens, D R -- Yamada, K M -- New York, N.Y. -- Science. 2001 Nov 23;294(5547):1708-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Craniofacial Developmental Biology and Regeneration Branch, National Institute of Dental and Craniofacial Research, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11721053" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Animals ; *Cell Adhesion/drug effects ; Cell Culture Techniques/methods ; Cell Division ; Cell Movement ; Cell Size ; Cells, Cultured ; Culture Techniques/methods ; Cycloheximide/pharmacology ; Cytoskeletal Proteins/metabolism ; Extracellular Matrix/chemistry/metabolism ; Fibroblasts/chemistry/*cytology/*metabolism ; Fibronectins/metabolism ; Fluorescent Antibody Technique, Indirect ; Focal Adhesion Kinase 1 ; Focal Adhesion Protein-Tyrosine Kinases ; Focal Adhesions/chemistry/metabolism ; Glutaral/metabolism ; Humans ; Imaging, Three-Dimensional/*methods ; Integrins/metabolism ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Molecular Conformation ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Time Factors
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    Virology. HIV--breaking the rules for nuclear entry (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-11-03
    Description: How does human immunodeficiency virus (HIV) gain access to the carefully guarded nucleus of the host cell? In a Perspective, Segura-Totten and Wilson elaborate on new findings (de Noronha et al.) showing that the HIV protein Vpr is crucial for causing transient herniations in the host cell nuclear envelope. These ruptures are sufficient to enable the preintegration complexes of invading virions to enter the nucleus and to integrate with host cell DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Segura-Totten, M -- Wilson, K L -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1016-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691977" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Nucleus/*metabolism/*virology ; Chromatin/metabolism ; DNA-Binding Proteins/metabolism ; G2 Phase ; Gene Products, vpr/genetics/*metabolism ; HIV/*physiology ; HeLa Cells ; Humans ; Lamins ; Membrane Proteins/metabolism ; Mutation ; Nuclear Envelope/*metabolism/ultrastructure ; Nuclear Proteins/metabolism ; Phosphorylation ; Thymopoietins/metabolism ; *Virus Integration ; vpr Gene Products, Human Immunodeficiency Virus
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  • 21
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    Requirement for the SLP-76 adaptor GADS in T cell development (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-03-10
    Description: GADS is an adaptor protein implicated in CD3 signaling because of its ability to link SLP-76 to LAT. A GADS-deficient mouse was generated by gene targeting, and the function of GADS in T cell development and activation was examined. GADS- CD4-CD8- thymocytes exhibited a severe block in proliferation but still differentiated into mature T cells. GADS- thymocytes failed to respond to CD3 cross-linking in vivo and were impaired in positive and negative selection. Immunoprecipitation experiments revealed that the association between SLP-76 and LAT was uncoupled in GADS- thymocytes. These observations indicate that GADS is a critical adaptor for CD3 signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoder, J -- Pham, C -- Iizuka, Y M -- Kanagawa, O -- Liu, S K -- McGlade, J -- Cheng, A M -- New York, N.Y. -- Science. 2001 Mar 9;291(5510):1987-91.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Medical Scientist Training Program, Washington University School of Medicine, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11239162" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antigens, CD3/metabolism ; Carrier Proteins/*metabolism ; Cell Differentiation ; Cell Division ; Cell Lineage ; Cell Size ; Female ; Gene Targeting ; Lymphocyte Activation ; Male ; *Membrane Proteins ; Mice ; Mice, Transgenic ; Phosphoproteins/*metabolism ; Phosphorylation ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; Spleen/cytology/immunology ; T-Lymphocytes/*cytology/immunology ; Thymus Gland/cytology/immunology ; src Homology Domains
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    Clinical resistance to STI-571 cancer therapy caused by BCR-ABL gene mutation or amplification (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-06-26
    Description: Clinical studies with the Abl tyrosine kinase inhibitor STI-571 in chronic myeloid leukemia demonstrate that many patients with advanced stage disease respond initially but then relapse. Through biochemical and molecular analysis of clinical material, we find that drug resistance is associated with the reactivation of BCR-ABL signal transduction in all cases examined. In six of nine patients, resistance was associated with a single amino acid substitution in a threonine residue of the Abl kinase domain known to form a critical hydrogen bond with the drug. This substitution of threonine with isoleucine was sufficient to confer STI-571 resistance in a reconstitution experiment. In three patients, resistance was associated with progressive BCR-ABL gene amplification. These studies provide evidence that genetically complex cancers retain dependence on an initial oncogenic event and suggest a strategy for identifying inhibitors of STI-571 resistance.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gorre, M E -- Mohammed, M -- Ellwood, K -- Hsu, N -- Paquette, R -- Rao, P N -- Sawyers, C L -- GM07185/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 3;293(5531):876-80. Epub 2001 Jun 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, Molecular Biology Institute, University of California, Los Angeles, CA 90095, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423618" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Antineoplastic Agents/metabolism/pharmacology/therapeutic use ; Base Sequence ; Benzamides ; Blast Crisis/genetics ; Cell Line ; Drug Resistance, Neoplasm/genetics ; Fusion Proteins, bcr-abl/*metabolism ; Gene Amplification ; *Genes, abl ; Humans ; Hydrogen Bonding ; Imatinib Mesylate ; Leukemia, Myelogenous, Chronic, BCR-ABL Positive/*drug therapy/*genetics ; Molecular Sequence Data ; Philadelphia Chromosome ; Phosphorylation ; Piperazines/metabolism/*pharmacology/therapeutic use ; Point Mutation ; Protein Structure, Tertiary ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-abl/antagonists & ; inhibitors/chemistry/*genetics/metabolism ; Proto-Oncogene Proteins c-crk ; Pyrimidines/metabolism/*pharmacology/therapeutic use ; Recurrence ; Signal Transduction
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    Molecular biology. Getting p53 out of the nucleus (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-09
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gottifredi, V -- Prives, C -- New York, N.Y. -- Science. 2001 Jun 8;292(5523):1851-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Sciences, Columbia University, New York, NY 10027, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11397937" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Cell Cycle ; Cell Line ; Cell Nucleus/*metabolism ; Cysteine Endopeptidases/metabolism ; Cytoplasm/metabolism ; DNA Damage ; Humans ; Multienzyme Complexes/metabolism ; Nuclear Localization Signals ; Nuclear Pore/metabolism ; *Nuclear Proteins ; Phosphorylation ; Proteasome Endopeptidase Complex ; *Protein Sorting Signals ; Proto-Oncogene Proteins/chemistry/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Recombinant Fusion Proteins/metabolism ; Tumor Suppressor Protein p53/chemistry/*metabolism ; Ubiquitins/metabolism ; Ultraviolet Rays
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  • 24
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    Formation of neurofibrillary tangles in P301l tau transgenic mice induced by Abeta 42 fibrils (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-25
    Description: beta-Amyloid plaques and neurofibrillary tangles (NFTs) are the defining neuropathological hallmarks of Alzheimer's disease, but their pathophysiological relation is unclear. Injection of beta-amyloid Abeta42 fibrils into the brains of P301L mutant tau transgenic mice caused fivefold increases in the numbers of NFTs in cell bodies within the amygdala from where neurons project to the injection sites. Gallyas silver impregnation identified NFTs that contained tau phosphorylated at serine 212/threonine 214 and serine 422. NFTs were composed of twisted filaments and occurred in 6-month-old mice as early as 18 days after Abeta42 injections. Our data support the hypothesis that Abeta42 fibrils can accelerate NFT formation in vivo.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gotz, J -- Chen, F -- van Dorpe, J -- Nitsch, R M -- New York, N.Y. -- Science. 2001 Aug 24;293(5534):1491-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Psychiatry Research, University of Zurich, August Forel Strasse 1, 8008 Zurich, Switzerland. goetz@bli.unizh.ch〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11520988" target="_blank"〉PubMed〈/a〉
    Keywords: Aged ; Aged, 80 and over ; Alzheimer Disease/metabolism/*pathology ; Amygdala/*pathology ; Amyloid beta-Peptides/administration & dosage/*metabolism ; Animals ; Brain/*pathology ; Epitopes ; Female ; Fluorescent Antibody Technique ; Humans ; Male ; Mice ; Mice, Transgenic ; Microscopy, Immunoelectron ; Mutation ; Neurofibrillary Tangles/*metabolism/pathology ; Peptide Fragments/administration & dosage/*metabolism ; Phosphorylation ; Plaque, Amyloid/*metabolism/pathology ; Protein Conformation ; Protein Isoforms ; Sex Characteristics ; tau Proteins/chemistry/genetics/immunology/*metabolism
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    Reversal of obesity- and diet-induced insulin resistance with salicylates or targeted disruption of Ikkbeta (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-05
    Description: We show that high doses of salicylates reverse hyperglycemia, hyperinsulinemia, and dyslipidemia in obese rodents by sensitizing insulin signaling. Activation or overexpression of the IkappaB kinase beta (IKKbeta) attenuated insulin signaling in cultured cells, whereas IKKbeta inhibition reversed insulin resistance. Thus, IKKbeta, rather than the cyclooxygenases, appears to be the relevant molecular target. Heterozygous deletion (Ikkbeta+/-) protected against the development of insulin resistance during high-fat feeding and in obese Lep(ob/ob) mice. These findings implicate an inflammatory process in the pathogenesis of insulin resistance in obesity and type 2 diabetes mellitus and identify the IKKbeta pathway as a target for insulin sensitization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yuan, M -- Konstantopoulos, N -- Lee, J -- Hansen, L -- Li, Z W -- Karin, M -- Shoelson, S E -- AI43477/AI/NIAID NIH HHS/ -- DK45493/DK/NIDDK NIH HHS/ -- DK51729/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 31;293(5535):1673-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Joslin Diabetes Center and Department of Medicine, Harvard Medical School, Boston, MA 02215, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11533494" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Anti-Inflammatory Agents, Non-Steroidal/pharmacology ; Aspirin/administration & dosage/*pharmacology ; Blood Glucose/metabolism ; Cell Line ; Dietary Fats/*administration & dosage ; Gene Deletion ; Gene Targeting ; Glucose Tolerance Test ; I-kappa B Kinase ; Insulin/administration & dosage/blood/*metabolism/pharmacology ; *Insulin Resistance ; Lipids/blood ; Liver/metabolism ; Male ; Mice ; Mice, Obese ; Muscles/metabolism ; Obesity/metabolism/*physiopathology ; Phosphorylation ; Prostaglandin-Endoperoxide Synthases/genetics/metabolism ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/genetics/*metabolism ; Rats ; Rats, Zucker ; Receptor, Insulin/metabolism ; Signal Transduction ; Sodium Salicylate/administration & dosage/*pharmacology ; Tumor Necrosis Factor-alpha/pharmacology
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    A p53 amino-terminal nuclear export signal inhibited by DNA damage-induced phosphorylation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-09
    Description: The p53 protein is present in low amounts in normally growing cells and is activated in response to physiological insults. MDM2 regulates p53 either through inhibiting p53's transactivating function in the nucleus or by targeting p53 degradation in the cytoplasm. We identified a previously unknown nuclear export signal (NES) in the amino terminus of p53, spanning residues 11 to 27 and containing two serine residues phosphorylated after DNA damage, which was required for p53 nuclear export in colloboration with the carboxyl-terminal NES. Serine-15-phosphorylated p53 induced by ultraviolet irradiation was not exported. Thus, DNA damage-induced phosphorylation may achieve optimal p53 activation by inhibiting both MDM2 binding to, and the nuclear export of, p53.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Zhang, Y -- Xiong, Y -- CA65572/CA/NCI NIH HHS/ -- K01 CA087580/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 8;292(5523):1910-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Lineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, and Program in Molecular Biology and Biotechnology, University of North Carolina at Chapel Hill, NC 27599-7295, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11397945" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Amino Acid Sequence ; Animals ; Cell Fusion ; Cell Line ; Cell Nucleus/*metabolism ; Cells, Cultured ; Cytoplasm/metabolism ; *DNA Damage ; Mice ; Molecular Sequence Data ; Mutation ; *Nuclear Proteins ; Phosphorylation ; Phosphoserine/metabolism ; *Protein Sorting Signals ; Protein Structure, Tertiary ; Proteins/genetics/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Recombinant Fusion Proteins/metabolism ; Transfection ; Tumor Suppressor Protein p14ARF ; Tumor Suppressor Protein p53/*chemistry/genetics/*metabolism ; Ubiquitins/metabolism ; Ultraviolet Rays
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    Cell cycle research. DNA: once copied, thrice blocked (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davenport, R J -- New York, N.Y. -- Science. 2001 Jun 29;292(5526):2415-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11431544" target="_blank"〉PubMed〈/a〉
    Keywords: CDC28 Protein Kinase, S cerevisiae/*metabolism ; Cell Cycle Proteins/metabolism ; *Cell Division ; Cell Nucleus/metabolism ; *DNA Replication ; DNA, Fungal/*biosynthesis ; Fungal Proteins/metabolism ; Genes, Fungal ; Phosphorylation ; Replication Origin ; *Saccharomyces cerevisiae Proteins ; Yeasts/cytology/genetics/*metabolism
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    Prevention of chemotherapy-induced alopecia in rats by CDK inhibitors (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-01-06
    Description: Most traditional cytotoxic anticancer agents ablate the rapidly dividing epithelium of the hair follicle and induce alopecia (hair loss). Inhibition of cyclin-dependent kinase 2 (CDK2), a positive regulator of eukaryotic cell cycle progression, may represent a therapeutic strategy for prevention of chemotherapy-induced alopecia (CIA) by arresting the cell cycle and reducing the sensitivity of the epithelium to many cell cycle-active antitumor agents. Potent small-molecule inhibitors of CDK2 were developed using structure-based methods. Topical application of these compounds in a neonatal rat model of CIA reduced hair loss at the site of application in 33 to 50% of the animals. Thus, inhibition of CDK2 represents a potentially useful approach for the prevention of CIA in cancer patients.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S T -- Benson, B G -- Bramson, H N -- Chapman, D E -- Dickerson, S H -- Dold, K M -- Eberwein, D J -- Edelstein, M -- Frye, S V -- Gampe Jr, R T -- Griffin, R J -- Harris, P A -- Hassell, A M -- Holmes, W D -- Hunter, R N -- Knick, V B -- Lackey, K -- Lovejoy, B -- Luzzio, M J -- Murray, D -- Parker, P -- Rocque, W J -- Shewchuk, L -- Veal, J M -- Walker, D H -- Kuyper, L F -- New York, N.Y. -- Science. 2001 Jan 5;291(5501):134-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cancer Biology, Glaxo Wellcome Research and Development, Research Triangle Park, NC 27709, USA. std41085@glaxowellcome.com〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11141566" target="_blank"〉PubMed〈/a〉
    Keywords: Alopecia/*chemically induced/*prevention & control ; Animals ; Animals, Newborn ; Antineoplastic Agents/*toxicity ; Antineoplastic Combined Chemotherapy Protocols/toxicity ; Apoptosis/drug effects ; *CDC2-CDC28 Kinases ; Cell Cycle/drug effects ; Cell Line ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/*antagonists & inhibitors/metabolism ; Cyclophosphamide/toxicity ; Cytoprotection/drug effects ; DNA/biosynthesis ; Doxorubicin/toxicity ; Drug Design ; Enzyme Inhibitors/chemical synthesis/chemistry/*pharmacology ; Epithelium/drug effects ; Etoposide/toxicity ; Hair Follicle/cytology/*drug effects ; Humans ; Indoles/chemical synthesis/chemistry/*pharmacology ; Mice ; Mice, SCID ; Phosphorylation ; Protein-Serine-Threonine Kinases/*antagonists & inhibitors/metabolism ; Rats ; Retinoblastoma Protein/metabolism ; Scalp/transplantation ; Sulfonamides/chemical synthesis/chemistry/*pharmacology ; Transplantation, Heterologous
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    The neurobiology of slow synaptic transmission (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-11-03
    Description: Nerve cells communicate with each other through two mechanisms, referred to as fast and slow synaptic transmission. Fast-acting neurotransmitters, e.g., glutamate (excitatory) and gamma-aminobutyric acid (GABA) (inhibitory), achieve effects on their target cells within one millisecond by virtue of opening ligand-operated ion channels. In contrast, all of the effects of the biogenic amine and peptide neurotransmitters, as well as many of the effects of glutamate and GABA, are achieved over hundreds of milliseconds to minutes by slow synaptic transmission. This latter process is mediated through an enormously more complicated sequence of biochemical steps, involving second messengers, protein kinases, and protein phosphatases. Slow-acting neurotransmitters control the efficacy of fast synaptic transmission by regulating the efficiency of neurotransmitter release from presynaptic terminals and by regulating the efficiency with which fast-acting neurotransmitters produce their effects on postsynaptic receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Greengard, P -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1024-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular and Cellular Neuroscience, The Rockefeller University, 1230 York Avenue, New York, NY 10021, USA. greengd@mail.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691979" target="_blank"〉PubMed〈/a〉
    Keywords: Adenylyl Cyclases/metabolism ; Animals ; Brain/*physiology ; Dopamine/physiology ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Glutamic Acid/physiology ; Humans ; *Nerve Tissue Proteins ; Neurons/*physiology ; Neurotransmitter Agents/*physiology ; Phosphoprotein Phosphatases/metabolism ; Phosphoproteins/physiology ; Phosphorylation ; Presynaptic Terminals/physiology ; Protein Kinases/metabolism ; Receptors, Neurotransmitter/physiology ; Second Messenger Systems/physiology ; Signal Transduction ; *Synaptic Transmission
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    Neuroscience. A kinase to dampen the effects of cocaine? (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gupta, A -- Tsai, L H -- New York, N.Y. -- Science. 2001 Apr 13;292(5515):236-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Harvard Medical School and Howard Hughes Medical Institute, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11305318" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cocaine/*pharmacology ; Corpus Striatum/*drug effects/metabolism ; Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors/metabolism ; Cyclin-Dependent Kinase 5 ; Cyclin-Dependent Kinases/antagonists & inhibitors/genetics/*metabolism ; Dopamine/metabolism ; Dopamine Uptake Inhibitors/*pharmacology ; Dopamine and cAMP-Regulated Phosphoprotein 32 ; Mice ; Mice, Knockout ; Motor Activity/drug effects ; Nerve Tissue Proteins/metabolism ; Neurons/metabolism ; Phosphoprotein Phosphatases/antagonists & inhibitors/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Proto-Oncogene Proteins c-fos/metabolism ; Rats ; Signal Transduction
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    Mammalian TOR: a homeostatic ATP sensor (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-03
    Description: The bacterial macrolide rapamycin is an efficacious anticancer agent against solid tumors. In a hypoxic environment, the increase in mass of solid tumors is dependent on the recruitment of mitogens and nutrients. When nutrient concentrations change, particularly those of essential amino acids, the mammalian Target of Rapamycin (mTOR) functions in regulatory pathways that control ribosome biogenesis and cell growth. In bacteria, ribosome biogenesis is independently regulated by amino acids and adenosine triphosphate (ATP). Here we demonstrate that the mTOR pathway is influenced by the intracellular concentration of ATP, independent of the abundance of amino acids, and that mTOR itself is an ATP sensor.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dennis, P B -- Jaeschke, A -- Saitoh, M -- Fowler, B -- Kozma, S C -- Thomas, G -- New York, N.Y. -- Science. 2001 Nov 2;294(5544):1102-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Friedrich Miescher Institute for Biomedical Research, Maulbeerstrasse 66, CH-4058, Basel, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11691993" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Adenosine Triphosphate/*metabolism ; Amino Acids/metabolism ; Androstadienes/pharmacology ; Carrier Proteins/metabolism ; Cell Line ; Deoxyglucose/pharmacology ; Enzyme Activation ; Homeostasis ; Humans ; Insulin/pharmacology ; Kinetics ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; RNA, Transfer, Amino Acyl/metabolism ; Recombinant Fusion Proteins/metabolism ; Ribosomal Protein S6 Kinases/antagonists & inhibitors/metabolism ; Ribosomes/metabolism ; Rotenone/pharmacology ; Signal Transduction ; Sirolimus/pharmacology ; TOR Serine-Threonine Kinases
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    Two-state allosteric behavior in a single-domain signaling protein (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-03-27
    Description: Protein actions are usually discussed in terms of static structures, but function requires motion. We find a strong correlation between phosphorylation-driven activation of the signaling protein NtrC and microsecond time-scale backbone dynamics. Using nuclear magnetic resonance relaxation, we characterized the motions of NtrC in three functional states: unphosphorylated (inactive), phosphorylated (active), and a partially active mutant. These dynamics are indicative of exchange between inactive and active conformations. Both states are populated in unphosphorylated NtrC, and phosphorylation shifts the equilibrium toward the active species. These results support a dynamic population shift between two preexisting conformations as the underlying mechanism of activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Volkman, B F -- Lipson, D -- Wemmer, D E -- Kern, D -- GM62117/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2429-33.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Magnetic Resonance Facility at Madison (NMRFAM), Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11264542" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; *Bacterial Proteins ; Binding Sites ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Models, Molecular ; Motion ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; *Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Signal Transduction ; Time ; *Trans-Activators ; *Transcription Factors
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    Protein synthesis. The perks of balancing glucose (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-08-04
    Description: What do the regulation of translation initiation and glucose metabolism have to do with each other? Quite a lot, it seems, according to Sonenberg and Newgard in their Perspective. They discuss new findings that identify the kinase responsible for inactivating eIF2--a factor that is required for translation initiation (and hence protein synthesis)--when the endoplasmic reticulum is under stress. Loss of this kinase results in destruction of insulin-producing b cells in the pancreas and dysregulation of glucose homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sonenberg, N -- Newgard, C B -- New York, N.Y. -- Science. 2001 Aug 3;293(5531):818-9.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11486079" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Blood Glucose/metabolism ; Endoplasmic Reticulum/*metabolism ; Eukaryotic Initiation Factor-2/*metabolism ; Gluconeogenesis ; Glucose/*metabolism ; Homeostasis ; Hyperglycemia/etiology ; Hypoglycemia/etiology ; Islets of Langerhans/enzymology/metabolism ; Liver/metabolism ; Mice ; Mutation ; Phosphorylation ; *Protein Biosynthesis ; Protein Folding ; eIF-2 Kinase/*metabolism
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    Transcription. Switching partners in a regulatory tango (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nishioka, K -- Reinberg, D -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2497-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Biochemistry, Robert Wood Johnson Medical School, Piscataway, NJ 08854, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752565" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/metabolism ; *Gene Expression Regulation ; Histone Acetyltransferases ; Methylation ; Nuclear Proteins/*metabolism ; Phosphorylation ; Promoter Regions, Genetic ; Protein Structure, Tertiary ; Protein-Arginine N-Methyltransferases/*metabolism ; Receptors, Cytoplasmic and Nuclear/metabolism ; *Saccharomyces cerevisiae Proteins ; Signal Transduction ; Trans-Activators/*metabolism ; Transcription Factors/metabolism ; *Transcription, Genetic
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    On the dynamic origins of allosteric activation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wand, A J -- New York, N.Y. -- Science. 2001 Aug 24;293(5534):1395.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉The Johnson Research Foundation and Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia, PA 19104-6059, USA. wand@mail.med.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11520951" target="_blank"〉PubMed〈/a〉
    Keywords: Allosteric Regulation ; *Bacterial Proteins ; Calcium/metabolism ; Calmodulin/chemistry/metabolism ; DNA-Binding Proteins/*chemistry/genetics/*metabolism ; Motion ; Mutation ; Nuclear Magnetic Resonance, Biomolecular ; PII Nitrogen Regulatory Proteins ; Phosphorylation ; Protein Conformation ; Thermodynamics ; *Trans-Activators ; *Transcription Factors
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Phosphorylation-dependent ubiquitination of cyclin E by the SCFFbw7 ubiquitin ligase (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-05
    Description: Cyclin E binds and activates the cyclin-dependent kinase Cdk2 and catalyzes the transition from the G1 phase to the S phase of the cell cycle. The amount of cyclin E protein present in the cell is tightly controlled by ubiquitin-mediated proteolysis. Here we identify the ubiquitin ligase responsible for cyclin E ubiquitination as SCFFbw7 and demonstrate that it is functionally conserved in yeast, flies, and mammals. Fbw7 associates specifically with phosphorylated cyclin E, and SCFFbw7 catalyzes cyclin E ubiquitination in vitro. Depletion of Fbw7 leads to accumulation and stabilization of cyclin E in vivo in human and Drosophila melanogaster cells. Multiple F-box proteins contribute to cyclin E stability in yeast, suggesting an overlap in SCF E3 ligase specificity that allows combinatorial control of cyclin E degradation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Koepp, D M -- Schaefer, L K -- Ye, X -- Keyomarsi, K -- Chu, C -- Harper, J W -- Elledge, S J -- R01 AG011085/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2001 Oct 5;294(5540):173-7. Epub 2001 Aug 30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Baylor College of Medicine, Houston, TX, 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11533444" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Breast Neoplasms/genetics/metabolism ; *CDC2-CDC28 Kinases ; *Cell Cycle ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; Cell Line ; Cyclin E/*metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/metabolism ; Drosophila Proteins ; Drosophila melanogaster ; *F-Box Proteins ; Humans ; Mice ; Molecular Sequence Data ; Peptide Synthases/chemistry/genetics/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Double-Stranded ; Recombinant Fusion Proteins/metabolism ; SKP Cullin F-Box Protein Ligases ; Saccharomyces cerevisiae/genetics/metabolism ; Saccharomyces cerevisiae Proteins ; Sequence Alignment ; Transfection ; Tumor Cells, Cultured ; *Ubiquitin-Protein Ligases ; Ubiquitins/*metabolism
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    Cell biology. A switch to release the motor (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cheney, R E -- Rodriguez, O C -- R29 DC003299/DC/NIDCD NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 17;293(5533):1263-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Molecular Physiology, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA. cheneyr@med.unc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509712" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/metabolism ; Animals ; Biological Transport ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Calmodulin-Binding Proteins/chemistry/*metabolism ; Cell Cycle ; Humans ; Intermediate Filament Proteins/metabolism ; Melanosomes/*metabolism ; Molecular Motor Proteins/*metabolism ; *Myosin Heavy Chains ; *Myosin Type V ; Nerve Tissue Proteins/chemistry/*metabolism ; Organelles/metabolism ; Phosphorylation ; Protein Structure, Tertiary ; Xenopus ; rab GTP-Binding Proteins/metabolism
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    Development. Staying a boy forever (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-12-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wasserman, S A -- DiNardo, S -- New York, N.Y. -- Science. 2001 Dec 21;294(5551):2495-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Molecular Genetics, Section of Cell and Developmental Biology, University of California, San Diego, La Jolla, CA 92093-0634, USA. stevenw@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11752564" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Aging ; Cell Division ; Cell Nucleus/metabolism ; Drosophila/cytology/embryology/physiology ; Drosophila Proteins/*metabolism ; Germ Cells/cytology/metabolism/*physiology ; Glycoproteins/*metabolism ; Ligands ; Male ; Phosphorylation ; Protein-Tyrosine Kinases/*metabolism ; Signal Transduction ; Spermatids/cytology/physiology ; Spermatogenesis ; Stem Cells/cytology/metabolism/*physiology ; Testis/cytology ; Transcription Factors/*metabolism
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    Integrin connections map: to infinity and beyond (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-01
    Description: Integrins are transmembrane proteins that serve as primary sensors of the extracellular matrix (ECM) environment. In response to interactions with the ECM, integrins initiate signaling pathways that regulate cell migration, growth, and survival. Advances in imaging have contributed to the understanding of the dynamic nature of these cell-ECM interactions and the complexes that form at these sites and have provided insights into their regulation and signal organizing functions.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Martin, Karen H -- Slack, Jill K -- Boerner, Scott A -- Martin, Clifford C -- Parsons, J Thomas -- New York, N.Y. -- Science. 2002 May 31;296(5573):1652-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology, University of Virginia Health System, Box 800734, Charlottesville, VA 22908-0734, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12040184" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/metabolism ; Animals ; Cell Adhesion ; Cell Survival ; Extracellular Matrix/metabolism ; Focal Adhesions/metabolism ; Humans ; Integrins/*metabolism ; Phosphorylation ; *Signal Transduction ; ras Proteins/metabolism ; rho GTP-Binding Proteins/metabolism
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    TRP-PLIK, a bifunctional protein with kinase and ion channel activities (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-13
    Description: We cloned and characterized a protein kinase and ion channel, TRP-PLIK. As part of the long transient receptor potential channel subfamily implicated in control of cell division, it is a protein that is both an ion channel and a protein kinase. TRP-PLIK phosphorylated itself, displayed a wide tissue distribution, and, when expressed in CHO-K1 cells, constituted a nonselective, calcium-permeant, 105-picosiemen, steeply outwardly rectifying conductance. The zinc finger containing alpha-kinase domain was functional. Inactivation of the kinase activity by site-directed mutagenesis and the channel's dependence on intracellular adenosine triphosphate (ATP) demonstrated that the channel's kinase activity is essential for channel function.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Runnels, L W -- Yue, L -- Clapham, D E -- New York, N.Y. -- Science. 2001 Feb 9;291(5506):1043-7. Epub 2001 Jan 18.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Cardiology, Department of Neurobiology, Harvard Medical School, 1309 Enders Building, 320 Longwood Avenue, Children's Hospital, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11161216" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; CHO Cells ; Calcium/metabolism ; Catalytic Domain ; Cations/metabolism ; Cell Line ; Cricetinae ; DNA, Complementary ; Electric Conductivity ; Humans ; Ion Channels/chemistry/*genetics/*metabolism ; *Membrane Proteins ; Mice ; Molecular Sequence Data ; Mutation ; Myelin Basic Protein/metabolism ; Patch-Clamp Techniques ; Phosphorylation ; Protein Kinases/chemistry/*genetics/*metabolism ; Protein-Serine-Threonine Kinases ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; TRPM Cation Channels ; Transfection ; Two-Hybrid System Techniques ; Type C Phospholipases/metabolism
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    Circadian rhythms. Mutant gene speeds up the human clock (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-17
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chicurel, M -- New York, N.Y. -- Science. 2001 Jan 12;291(5502):226-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11253206" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biological Clocks/*genetics ; Casein Kinases ; Chromosomes, Human, Pair 2/genetics ; Circadian Rhythm/*genetics ; Humans ; Mutation ; Nuclear Proteins ; Period Circadian Proteins ; Phosphorylation ; Protein Kinases/metabolism ; Proteins/*genetics/metabolism ; Sleep Disorders, Circadian Rhythm/*genetics/metabolism ; Transcription Factors
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    MAP kinase phosphatase as a locus of flexibility in a mitogen-activated protein kinase signaling network (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-08-10
    Description: Intracellular signaling networks receive and process information to control cellular machines. The mitogen-activated protein kinase (MAPK) 1,2/protein kinase C (PKC) system is one such network that regulates many cellular machines, including the cell cycle machinery and autocrine/paracrine factor synthesizing machinery. We used a combination of computational analysis and experiments in mouse NIH-3T3 fibroblasts to understand the design principles of this controller network. We find that the growth factor-stimulated signaling network containing MAPK 1, 2/PKC can operate with one (monostable) or two (bistable) stable states. At low concentrations of MAPK phosphatase, the system exhibits bistable behavior, such that brief stimulus results in sustained MAPK activation. The MAPK-induced increase in the amounts of MAPK phosphatase eliminates the prolonged response capability and moves the network to a monostable state, in which it behaves as a proportional response system responding acutely to stimulus. Thus, the MAPK 1, 2/PKC controller network is flexibly designed, and MAPK phosphatase may be critical for this flexible response.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhalla, Upinder S -- Ram, Prahlad T -- Iyengar, Ravi -- CA-79134/CA/NCI NIH HHS/ -- CA-81050/CA/NCI NIH HHS/ -- GM-54508/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Aug 9;297(5583):1018-23.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉National Center for Biological Sciences, Bangalore 560065 India. bhalla@ncbs.res.in〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12169734" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adaptation, Physiological ; Animals ; *Cell Cycle Proteins ; Computer Simulation ; Dose-Response Relationship, Drug ; Dual Specificity Phosphatase 1 ; *Feedback, Physiological ; Immediate-Early Proteins/*metabolism ; *MAP Kinase Signaling System ; Mathematics ; Mice ; Mitogen-Activated Protein Kinase 1/*metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/*metabolism ; Models, Biological ; Phospholipases A/antagonists & inhibitors/metabolism ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Protein Kinase C/metabolism ; Protein Phosphatase 1 ; Protein Tyrosine Phosphatases/*metabolism
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    A pit stop at the ER (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: Although ligand activation of receptor signaling is well understood, less is known about how a cell switches off signaling by the activated receptor. In his Perspective, Gill discusses new work (Haj et al.) that visualizes one step in the process of deactivating a ligand-activated receptor tyrosine kinase--the dephosphorylation of the internalized receptor by a phosphatase in the endoplasmic reticulum.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gill, Gordon N -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1654-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉University of California, San Diego, La Jolla, CA 92093-0650, USA. ggill@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872824" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/enzymology ; Endocytosis ; Endoplasmic Reticulum/*enzymology ; Endosomes/enzymology/metabolism ; Energy Transfer ; Fluorescence ; Ligands ; Lysosomes/metabolism ; Mice ; Phosphatidylinositol 3-Kinases/metabolism ; Phosphorylation ; Protein Transport ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 ; Protein Tyrosine Phosphatases/chemistry/genetics/*metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-cbl ; Receptor Protein-Tyrosine Kinases/chemistry/*metabolism ; Receptor, Epidermal Growth Factor/chemistry/*metabolism ; Receptors, Platelet-Derived Growth Factor/chemistry/*metabolism ; Ubiquitin/metabolism ; *Ubiquitin-Protein Ligases
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    Calcium, calmodulin, and CaMKII requirement for initiation of centrosome duplication in Xenopus egg extracts (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Aberrant centrosome duplication is observed in many tumor cells and may contribute to genomic instability through the formation of multipolar mitotic spindles. Cyclin-dependent kinase 2 (Cdk2) is required for multiple rounds of centrosome duplication in Xenopus egg extracts but not for the initial round of replication. Egg extracts undergo periodic oscillations in the level of free calcium. We show here that chelation of calcium in egg extracts or specific inactivation of calcium/calmodulin-dependent protein kinase II (CaMKII) blocks even initial centrosome duplication, whereas inactivation of Cdk2 does not. Duplication can be restored to inhibited extracts by addition of CaMKII and calmodulin. These results indicate that calcium, calmodulin, and CaMKII are required for an essential step in initiation of centrosome duplication. Our data suggest that calcium oscillations in the cell cycle may be linked to centrosome duplication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Matsumoto, Yutaka -- Maller, James L -- CA46934/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):499-502.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Pharmacology, University of Colorado School of Medicine, Denver, CO 80262, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799245" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *CDC2-CDC28 Kinases ; Calcium/*metabolism ; *Calcium Signaling ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Calmodulin/*metabolism/pharmacology ; Cell Extracts ; Centrosome/*metabolism ; Chelating Agents/pharmacology ; Cyclin E ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/antagonists & inhibitors/metabolism ; Egtazic Acid/*analogs & derivatives/pharmacology ; Embryo, Nonmammalian/cytology/metabolism ; Enzyme Inhibitors/pharmacology ; Fluorescent Antibody Technique ; Heparin/pharmacology ; Microtubules/metabolism/ultrastructure ; Ovum/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/antagonists & inhibitors/metabolism ; *S Phase ; Xenopus ; Xenopus Proteins/metabolism
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    Local actin polymerization and dynamin recruitment in SV40-induced internalization of caveolae (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-04-20
    Description: Simian virus 40 (SV40) utilizes endocytosis through caveolae for infectious entry into host cells. We found that after binding to caveolae, virus particles induced transient breakdown of actin stress fibers. Actin was then recruited to virus-loaded caveolae as actin patches that served as sites for actin "tail" formation. Dynamin II was also transiently recruited. These events depended on the presence of cholesterol and on the activation of tyrosine kinases that phosphorylated proteins in caveolae. They were necessary for formation of caveolae-derived endocytic vesicles and for infection of the cell. Thus, caveolar endocytosis is ligand-triggered and involves extensive rearrangement of the actin cytoskeleton.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pelkmans, Lucas -- Puntener, Daniel -- Helenius, Ari -- New York, N.Y. -- Science. 2002 Apr 19;296(5567):535-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Swiss Federal Institute of Technology Zurich (ETHZ), HPM1 Building, ETH Honggerberg, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11964480" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/*physiology/ultrastructure ; Actins/*metabolism ; Animals ; Bicyclo Compounds, Heterocyclic/pharmacology ; Caveolae/*metabolism/ultrastructure/virology ; Caveolin 1 ; Caveolins/metabolism ; Cell Line ; Cholesterol/physiology ; *Depsipeptides ; Dynamins ; *Endocytosis ; GTP Phosphohydrolases/genetics/*metabolism ; Haplorhini ; Peptides, Cyclic/pharmacology ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Recombinant Fusion Proteins/metabolism ; Simian virus 40/*physiology ; Stress Fibers/metabolism ; Thiazoles/pharmacology ; Thiazolidines ; Transport Vesicles/metabolism
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    Signal transduction and the control of gene expression (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-02
    Description: More than 2000 transcription factors are encoded in the human genome. Such proteins have often been classified according to common structural elements. But because transcription factors evolved in the service of biologic function, we propose an alternative grouping of eukaryotic transcription factors on the basis of characteristics that describe their roles within cellular regulatory circuits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brivanlou, Ali H -- Darnell, James E Jr -- 1RO1EY12370-03/EY/NEI NIH HHS/ -- 2RO1HD/GM32105-06A1/HD/NICHD NIH HHS/ -- AI32489/AI/NIAID NIH HHS/ -- AI34420/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 1;295(5556):813-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Vertebrate Embryology, Rockefeller University, 1230 York Avenue, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11823631" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; DNA/metabolism ; DNA-Binding Proteins/metabolism ; *Gene Expression Regulation ; Phosphorylation ; Phosphoserine/metabolism ; Receptors, Cell Surface/metabolism ; Second Messenger Systems ; *Signal Transduction ; Transcription Factors/chemistry/*classification/*metabolism ; *Transcription, Genetic
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  • 47
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    Imaging sites of receptor dephosphorylation by PTP1B on the surface of the endoplasmic reticulum (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: When bound by extracellular ligands, receptor tyrosine kinases (RTKs) on the cell surface transmit critical signals to the cell interior. Although signal termination is less well understood, protein tyrosine phosphatase-1B (PTP1B) is implicated in the dephosphorylation and inactivation of several RTKs. However, PTP1B resides on the cytoplasmic surface of the endoplasmic reticulum (ER), so how and when it accesses RTKs has been unclear. Using fluorescence resonance energy transfer (FRET) methods, we monitored interactions between the epidermal- and platelet-derived growth factor receptors and PTP1B. PTP1B-catalyzed dephosphorylation required endocytosis of the receptors and occurred at specific sites on the surface of the ER. Most of the RTKs activated at the cell surface showed interaction with PTP1B after internalization, establishing that RTK activation and inactivation are spatially and temporally partitioned within cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haj, Fawaz G -- Verveer, Peter J -- Squire, Anthony -- Neel, Benjamin G -- Bastiaens, Philippe I H -- R01 CA49152/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1708-11.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Biology Program, Division of Hematology-Oncology, Department of Medicine, Beth Israel-Deaconess Medical Center, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872838" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; Catalytic Domain ; Cell Membrane/enzymology ; Cells, Cultured ; *Endocytosis ; Endoplasmic Reticulum/*enzymology ; Energy Transfer ; Epidermal Growth Factor/metabolism/pharmacology ; Fluorescence ; Mice ; Microscopy, Confocal ; Microscopy, Fluorescence ; Phosphorylation ; Platelet-Derived Growth Factor/metabolism/pharmacology ; Protein Transport ; Protein Tyrosine Phosphatase, Non-Receptor Type 1 ; Protein Tyrosine Phosphatases/chemistry/genetics/*metabolism ; Receptor, Epidermal Growth Factor/*metabolism ; Receptors, Platelet-Derived Growth Factor/*metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction
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    Cooperation of GGAs and AP-1 in packaging MPRs at the trans-Golgi network (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-07
    Description: The Golgi-localized, gamma-ear-containing, adenosine diphosphate ribosylation factor-binding proteins (GGAs) are multidomain proteins that bind mannose 6-phosphate receptors (MPRs) in the Golgi and have an essential role in lysosomal enzyme sorting. Here the GGAs and the coat protein adaptor protein-1 (AP-1) were shown to colocalize in clathrin-coated buds of the trans-Golgi networks of mouse L cells and human HeLa cells. Binding studies revealed a direct interaction between the hinge domains of the GGAs and the gamma-ear domain of AP-1. Further, AP-1 contained bound casein kinase-2 that phosphorylated GGA1 and GGA3, thereby causing autoinhibition. This could induce the directed transfer of the MPRs from GGAs to AP-1. MPRs that are defective in binding to GGAs are poorly incorporated into AP-1-containing clathrin-coated vesicles. Thus, the GGAs and AP-1 interact to package MPRs into AP-1-containing coated vesicles.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doray, Balraj -- Ghosh, Pradipta -- Griffith, Janice -- Geuze, Hans J -- Kornfeld, Stuart -- R01 CA-08759/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2002 Sep 6;297(5587):1700-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Internal Medicine, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12215646" target="_blank"〉PubMed〈/a〉
    Keywords: ADP-Ribosylation Factors/*metabolism ; Adaptor Proteins, Vesicular Transport ; Animals ; Biological Transport ; Carrier Proteins/*metabolism ; Cattle ; Cell Line ; Clathrin-Coated Vesicles/metabolism ; HeLa Cells ; Humans ; L Cells (Cell Line) ; Membrane Proteins/*metabolism ; Mice ; Mutation ; Phosphorylation ; Protein Binding ; Receptor, IGF Type 2/genetics/*metabolism ; Recombinant Proteins/metabolism ; trans-Golgi Network/*metabolism
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    A distinct signaling pathway used by the IgG-containing B cell antigen receptor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-12-21
    Description: The immunoglobulin G (IgG)-containing B lymphocyte antigen receptor (IgG-BCR) transmits a signal distinct from that of IgM-BCR or IgD-BCR, although all three use the same signal-transducing component, Igalpha/Igbeta. Here we demonstrate that the inhibitory coreceptor CD22 down-modulates signaling through IgM-BCR and IgD-BCR, but not that through IgG-BCR, because of the IgG cytoplasmic tail, which prevents CD22 phosphorylation. These results suggest that the cytoplasmic tail of IgG specifically enhances IgG-BCR signaling by preventing CD22-mediated signal inhibition. Enhanced signaling through IgG-BCR may be involved in efficient IgG production, which is crucial for immunity to pathogens.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wakabayashi, Chisato -- Adachi, Takahiro -- Wienands, Jurgen -- Tsubata, Takeshi -- New York, N.Y. -- Science. 2002 Dec 20;298(5602):2392-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Medical Research Institute, Tokyo Medical and Dental University, 113-8510 Tokyo, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12493916" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD/metabolism ; Antigens, Differentiation, B-Lymphocyte/metabolism ; B-Lymphocytes/immunology/metabolism ; Calcium/metabolism ; Calcium Signaling ; *Cell Adhesion Molecules ; Cells, Cultured ; Immunoglobulin D/immunology/metabolism ; Immunoglobulin G/chemistry/immunology/*metabolism ; Intracellular Signaling Peptides and Proteins ; Lectins/metabolism ; Mice ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinases/metabolism ; Phosphorylation ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Receptors, Antigen, B-Cell/chemistry/immunology/*metabolism ; Sialic Acid Binding Ig-like Lectin 2 ; *Signal Transduction ; Transfection ; Tumor Cells, Cultured
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    Fork reversal and ssDNA accumulation at stalled replication forks owing to checkpoint defects (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-07-27
    Description: Checkpoint-mediated control of replicating chromosomes is essential for preventing cancer. In yeast, Rad53 kinase protects stalled replication forks from pathological rearrangements. To characterize the mechanisms controlling fork integrity, we analyzed replication intermediates formed in response to replication blocks using electron microscopy. At the forks, wild-type cells accumulate short single-stranded regions, which likely causes checkpoint activation, whereas rad53 mutants exhibit extensive single-stranded gaps and hemi-replicated intermediates, consistent with a lagging-strand synthesis defect. Further, rad53 cells accumulate Holliday junctions through fork reversal. We speculate that, in checkpoint mutants, abnormal replication intermediates begin to form because of uncoordinated replication and are further processed by unscheduled recombination pathways, causing genome instability.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sogo, Jose M -- Lopes, Massimo -- Foiani, Marco -- New York, N.Y. -- Science. 2002 Jul 26;297(5581):599-602.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cell Biology, ETH Honggerberg, CH-8093 Zurich, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12142537" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Cycle Proteins ; Checkpoint Kinase 2 ; Cross-Linking Reagents/pharmacology ; *DNA Replication ; DNA, Fungal/biosynthesis/chemistry/*metabolism ; DNA, Single-Stranded/chemistry/*metabolism ; Furocoumarins/pharmacology ; Hydroxyurea/pharmacology ; Microscopy, Electron ; Mutation ; Nucleic Acid Conformation ; Nucleosomes/metabolism/ultrastructure ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/metabolism ; *Recombination, Genetic ; Saccharomyces cerevisiae/*genetics/*metabolism ; *Saccharomyces cerevisiae Proteins
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    Enhanced morphine analgesia in mice lacking beta-arrestin 2 (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: The ability of morphine to alleviate pain is mediated through a heterotrimeric guanine nucleotide binding protein (G protein)-coupled heptahelical receptor (GPCR), the mu opioid receptor (muOR). The efficiency of GPCR signaling is tightly regulated and ultimately limited by the coordinated phosphorylation of the receptors by specific GPCR kinases and the subsequent interaction of the phosphorylated receptors with beta-arrestin 1 and beta-arrestin 2. Functional deletion of the beta-arrestin 2 gene in mice resulted in remarkable potentiation and prolongation of the analgesic effect of morphine, suggesting that muOR desensitization was impaired. These results provide evidence in vivo for the physiological importance of beta-arrestin 2 in regulating the function of a specific GPCR, the muOR. Moreover, they suggest that inhibition of beta-arrestin 2 function might lead to enhanced analgesic effectiveness of morphine and provide potential new avenues for the study and treatment of pain, narcotic tolerance, and dependence.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bohn, L M -- Lefkowitz, R J -- Gainetdinov, R R -- Peppel, K -- Caron, M G -- Lin, F T -- F32 DA006023/DA/NIDA NIH HHS/ -- HL16037/HL/NHLBI NIH HHS/ -- NS 19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2495-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute Laboratories, Departments of Cell Biology and Medicine, Duke University Medical Center, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617462" target="_blank"〉PubMed〈/a〉
    Keywords: Analgesia ; Analgesics, Opioid/administration & dosage/metabolism/*pharmacology ; Animals ; Arrestins/genetics/*physiology ; Binding Sites ; Body Temperature/drug effects ; Brain/metabolism ; Enkephalin, Ala(2)-MePhe(4)-Gly(5)-/pharmacology ; GTP-Binding Proteins/metabolism ; Guanosine 5'-O-(3-Thiotriphosphate)/metabolism ; Mice ; Mice, Inbred C57BL ; Mice, Knockout ; Morphine/administration & dosage/metabolism/*pharmacology ; Naloxone/metabolism/pharmacology ; Narcotic Antagonists/metabolism/pharmacology ; Pain Measurement ; Pain Threshold ; Phosphorylation ; Receptors, Opioid, mu/*metabolism ; Signal Transduction
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    Structural assets of a tumor suppressor (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-05
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tonks, N K -- Myers, M P -- New York, N.Y. -- Science. 1999 Dec 10;286(5447):2096-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA. tonks@cshl.org〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10617421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Binding Sites ; Cell Membrane/metabolism ; Crystallography, X-Ray ; *Genes, Tumor Suppressor ; Humans ; Hydrogen Bonding ; Membrane Lipids/metabolism ; Models, Biological ; Mutation ; Neoplasms/*etiology/genetics ; PTEN Phosphohydrolase ; Phosphatidylinositol 3-Kinases/chemistry/metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phosphoric Monoester Hydrolases/*chemistry/genetics/*metabolism ; Phosphorylation ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Signal Transduction ; *Tumor Suppressor Proteins
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    Checkpoint gene linked to human cancer (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hagmann, M -- New York, N.Y. -- Science. 1999 Dec 24;286(5449):2433-4.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10636795" target="_blank"〉PubMed〈/a〉
    Keywords: *Cell Cycle ; Checkpoint Kinase 2 ; Genes, Tumor Suppressor ; Genes, p53 ; Humans ; Li-Fraumeni Syndrome/enzymology/*genetics/pathology ; Mutation ; Phosphorylation ; *Protein Kinases ; Protein-Serine-Threonine Kinases/*genetics/metabolism ; Signal Transduction ; Tumor Cells, Cultured ; Tumor Suppressor Protein p53/genetics/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 54
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    From marrow to brain: expression of neuronal phenotypes in adult mice (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-02
    Description: After intravascular delivery of genetically marked adult mouse bone marrow into lethally irradiated normal adult hosts, donor-derived cells expressing neuronal proteins (neuronal phenotypes) developed in the central nervous system. Flow cytometry revealed a population of donor-derived cells in the brain with characteristics distinct from bone marrow. Confocal microscopy of individual cells showed that hundreds of marrow-derived cells in brain sections expressed gene products typical of neurons (NeuN, 200-kilodalton neurofilament, and class III beta-tubulin) and were able to activate the transcription factor cAMP response element-binding protein (CREB). The generation of neuronal phenotypes in the adult brain 1 to 6 months after an adult bone marrow transplant demonstrates a remarkable plasticity of adult tissues with potential clinical applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Brazelton, T R -- Rossi, F M -- Keshet, G I -- Blau, H M -- AG09521/AG/NIA NIH HHS/ -- CA59717/CA/NCI NIH HHS/ -- HD18179/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 1;290(5497):1775-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Pharmacology, CCSR 4215, 269 Campus Drive, Stanford University, Stanford, CA 94305-5175, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11099418" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Biomarkers/analysis ; Bone Marrow Cells/*cytology ; *Bone Marrow Transplantation ; Brain/*cytology ; Cell Differentiation ; Cell Size ; Cyclic AMP Response Element-Binding Protein/metabolism ; Flow Cytometry ; Gene Expression ; Green Fluorescent Proteins ; Luminescent Proteins/analysis ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Transgenic ; Microscopy, Confocal ; Nerve Tissue Proteins/analysis/genetics ; Neurons/chemistry/*cytology/metabolism ; Olfactory Bulb/cytology ; Phenotype ; Phosphorylation
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    Cancer. Nota bene: The killer instinct of a p53 target (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, O -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):67.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11183152" target="_blank"〉PubMed〈/a〉
    Keywords: *Apoptosis ; DNA Damage ; DNA Repair ; Gamma Rays ; Gene Expression ; Humans ; Membrane Potentials ; Mitochondria/physiology ; Phosphorylation ; Phosphoserine/metabolism ; Promoter Regions, Genetic ; Tumor Suppressor Protein p53/*metabolism ; Ultraviolet Rays
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    Nota bene. Awakening aurora (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-15
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Smith, O -- New York, N.Y. -- Science. 2000 Apr 7;288(5463):69.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10766638" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Aurora Kinases ; Cell Cycle Proteins ; Genes, mos ; MAP Kinase Signaling System ; *Meiosis ; Oocytes/*cytology/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Poly A/metabolism ; Progesterone/*metabolism ; Protein Biosynthesis ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins c-mos/genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; RNA-Binding Proteins/metabolism ; Receptors, Progesterone/metabolism ; Transcription Factors/metabolism ; Xenopus ; *Xenopus Proteins ; *mRNA Cleavage and Polyadenylation Factors
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    Differential clustering of CD4 and CD3zeta during T cell recognition (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-08-26
    Description: Whereas T helper cells recognize peptide-major histocompatibility complex (MHC) class II complexes through their T cell receptors (TCRs), CD4 binds to an antigen-independent region of the MHC. Using green fluorescent protein-tagged chimeras and three-dimensional video microscopy, we show that CD4 and TCR-associated CD3zeta cluster in the interface coincident with increases in intracellular calcium. Signaling-, costimulation-, and cytoskeleton-dependent processes then stabilize CD3zeta in a single cluster at the center of the interface, while CD4 moves to the periphery. Thus, the CD4 coreceptor may serve primarily to "boost" recognition of ligand by the TCR and may not be required once activation has been initiated.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krummel, M F -- Sjaastad, M D -- Wulfing, C -- Davis, M M -- New York, N.Y. -- Science. 2000 Aug 25;289(5483):1349-52.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Immunology, Stanford University School of Medicine, and the Howard Hughes Medical Institute, Stanford, CA 94305, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10958781" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigen-Presenting Cells/immunology ; Antigens, CD3/*metabolism ; Antigens, CD4/*metabolism ; Calcium Signaling ; Cell Line ; Cytoskeleton/physiology ; Histocompatibility Antigens Class II/immunology/metabolism ; Ligands ; *Lymphocyte Activation ; Microscopy, Video ; Phosphorylation ; Receptors, Antigen, T-Cell/immunology/metabolism ; Recombinant Fusion Proteins/metabolism ; T-Lymphocytes, Helper-Inducer/*immunology/metabolism ; Transfection
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    Response of Schwann cells to action potentials in development (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-24
    Description: Sensory axons become functional late in development when Schwann cells (SC) stop proliferating and differentiate into distinct phenotypes. We report that impulse activity in premyelinated axons can inhibit proliferation and differentiation of SCs. This neuron-glial signaling is mediated by adenosine triphosphate acting through P2 receptors on SCs and intracellular signaling pathways involving Ca2+, Ca2+/calmodulin kinase, mitogen-activated protein kinase, cyclic adenosine 3',5'-monophosphate response element binding protein, and expression of c-fos and Krox-24. Adenosine triphosphate arrests maturation of SCs in an immature morphological stage and prevents expression of O4, myelin basic protein, and the formation of myelin. Through this mechanism, functional activity in the developing nervous system could delay terminal differentiation of SCs until exposure to appropriate axon-derived signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stevens, B -- Fields, R D -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2267-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Developmental Neurobiology, National Institutes of Health, National Institute of Child Health and Human Development, Building 49, Room 5A38, 49 Convent Drive, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10731149" target="_blank"〉PubMed〈/a〉
    Keywords: Action Potentials ; Adenosine Triphosphate/metabolism ; Animals ; Axons/*physiology ; Calcium/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Cell Differentiation ; Cell Division ; Cells, Cultured ; Coculture Techniques ; Cyclic AMP Response Element-Binding Protein/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Early Growth Response Protein 1 ; Electric Stimulation ; Ganglia, Spinal/physiology ; Gene Expression Regulation, Developmental ; Genes, fos ; *Immediate-Early Proteins ; Mice ; Microscopy, Confocal ; Myelin Sheath/metabolism ; Neurons, Afferent/*physiology ; Phosphorylation ; Proto-Oncogene Proteins c-fos/metabolism ; Receptors, Purinergic P2/metabolism ; Schwann Cells/*cytology/*physiology ; Signal Transduction ; Transcription Factors/genetics/metabolism
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    Failure to regulate TNF-induced NF-kappaB and cell death responses in A20-deficient mice (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-09-29
    Description: A20 is a cytoplasmic zinc finger protein that inhibits nuclear factor kappaB (NF-kappaB) activity and tumor necrosis factor (TNF)-mediated programmed cell death (PCD). TNF dramatically increases A20 messenger RNA expression in all tissues. Mice deficient for A20 develop severe inflammation and cachexia, are hypersensitive to both lipopolysaccharide and TNF, and die prematurely. A20-deficient cells fail to terminate TNF-induced NF-kappaB responses. These cells are also more susceptible than control cells to undergo TNF-mediated PCD. Thus, A20 is critical for limiting inflammation by terminating TNF-induced NF-kappaB responses in vivo.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3582399/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3582399/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, E G -- Boone, D L -- Chai, S -- Libby, S L -- Chien, M -- Lodolce, J P -- Ma, A -- 5T32GM07183/GM/NIGMS NIH HHS/ -- R01 DK052751/DK/NIDDK NIH HHS/ -- T32GM07839/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2350-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, The University of Chicago, 5841 South Maryland Avenue, MC 6084, Chicago, IL 60637, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11009421" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Cachexia/pathology/physiopathology ; Cells, Cultured ; Cysteine Endopeptidases ; DNA/metabolism ; DNA-Binding Proteins/genetics/metabolism ; Fibroblasts/metabolism ; Gene Targeting ; *I-kappa B Proteins ; Inflammation/pathology/*physiopathology ; Interleukin-1/pharmacology ; Intestines/pathology ; Intracellular Signaling Peptides and Proteins ; Kidney/pathology ; Lipopolysaccharides/immunology ; Liver/pathology ; Mice ; NF-kappa B/*metabolism ; Nuclear Proteins ; Phosphorylation ; Proteins/genetics/*physiology ; Skin/pathology ; T-Lymphocytes/cytology/metabolism ; Tumor Necrosis Factor-alpha/*pharmacology ; Zinc Fingers
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    Regulation of STAT3 by direct binding to the Rac1 GTPase (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-10-06
    Description: The signal transducers and activators of transcription (STAT) transcription factors become phosphorylated on tyrosine and translocate to the nucleus after stimulation of cells with growth factors or cytokines. We show that the Rac1 guanosine triphosphatase can bind to and regulate STAT3 activity. Dominant negative Rac1 inhibited STAT3 activation by growth factors, whereas activated Rac1 stimulated STAT3 phosphorylation on both tyrosine and serine residues. Moreover, activated Rac1 formed a complex with STAT3 in mammalian cells. Yeast two-hybrid analysis indicated that STAT3 binds directly to active but not inactive Rac1 and that the interaction occurs via the effector domain. Rac1 may serve as an alternate mechanism for targeting STAT3 to tyrosine kinase signaling complexes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Simon, A R -- Vikis, H G -- Stewart, S -- Fanburg, B L -- Cochran, B H -- Guan, K L -- GM-54304/GM/NIGMS NIH HHS/ -- K08-HL-03547/HL/NHLBI NIH HHS/ -- P30-DK34928/DK/NIDDK NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):144-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Pulmonary and Critical Care Division, Tupper Research Institute, New England Medical Center, Boston, MA 02111, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021801" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Animals ; COS Cells ; Cell Line ; Cercopithecus aethiops ; DNA-Binding Proteins/genetics/*metabolism ; Enzyme Activation ; Epidermal Growth Factor/pharmacology ; Gene Expression Regulation ; Genes, Reporter ; Genetic Vectors ; Guanine Nucleotide Exchange Factors/genetics/metabolism ; Humans ; Janus Kinase 2 ; Mutation ; Neoplasm Proteins ; Phosphorylation ; Phosphoserine/metabolism ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/genetics/metabolism ; *Proto-Oncogene Proteins ; Rats ; STAT3 Transcription Factor ; Signal Transduction ; Trans-Activators/genetics/*metabolism ; Transfection ; Two-Hybrid System Techniques ; rac1 GTP-Binding Protein/genetics/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Transcription. New insights into an old modification (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mizzen, C A -- Allis, C D -- New York, N.Y. -- Science. 2000 Sep 29;289(5488):2290-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Genetics, University of Virginia Health System, Charlottesville, VA 22908, USA. cam8y@virginia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11041795" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyltransferases/metabolism ; Animals ; Cell Cycle ; Chromatin/*metabolism ; DNA/metabolism ; DNA-Binding Proteins/genetics/*metabolism ; Drosophila/genetics ; Gene Expression Regulation ; Histone Acetyltransferases ; Histone Deacetylases/metabolism ; Histones/*metabolism ; Nuclear Proteins/genetics/*metabolism ; Nucleosomes/metabolism ; Phosphorylation ; Promoter Regions, Genetic ; *Saccharomyces cerevisiae Proteins ; TATA Box ; *TATA-Binding Protein Associated Factors ; Trans-Activators/*metabolism ; Transcription Factor TFIID ; Transcription Factors, TFII/metabolism ; *Transcriptional Activation ; Ubiquitins/metabolism
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    Biochemistry. Ubiquitination--more than two to tango (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-14
    Description: The ubiquitin pathway in the cell is an elegant system for targeting unwanted proteins for degradation. Three enzymes, E1, E2, and E3, are responsible for attaching the ubiquitin tag to proteins destined to be chopped up. In their Perspective, Joazeiro and Hunter discuss new structural findings that reveal the part played by an E3 called c-Cbl in this ubiquitinating process.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Joazeiro, C A -- Hunter, T -- New York, N.Y. -- Science. 2000 Sep 22;289(5487):2061-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Biology and Virology Laboratory, Salk Institute, La Jolla, CA 92037, USA. cjoazeiro@aim.salk.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11032556" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; Binding Sites ; Ligases/chemistry/*metabolism ; Models, Molecular ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein Conformation ; Protein Folding ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Proteins/*metabolism ; Proto-Oncogene Proteins/*chemistry/*metabolism ; Proto-Oncogene Proteins c-cbl ; Receptor Protein-Tyrosine Kinases/metabolism ; Substrate Specificity ; *Ubiquitin-Conjugating Enzymes ; Ubiquitin-Protein Ligases ; Ubiquitins/*metabolism ; src Homology Domains
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    Response to RAG-mediated VDJ cleavage by NBS1 and gamma-H2AX (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-09
    Description: Genetic disorders affecting cellular responses to DNA damage are characterized by high rates of translocations involving antigen receptor loci and increased susceptibility to lymphoid malignancies. We report that the Nijmegen breakage syndrome protein (NBS1) and histone gamma-H2AX, which associate with irradiation-induced DNA double-strand breaks (DSBs), are also found at sites of VDJ (variable, diversity, joining) recombination-induced DSBs. In developing thymocytes, NBS1 and gamma-H2AX form nuclear foci that colocalize with the T cell receptor alpha locus in response to recombination activating gene (RAG) protein-mediated VDJ cleavage. Our results suggest that surveillance of T cell receptor recombination intermediates by NBS1 and gamma-H2AX may be important for preventing oncogenic translocations.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721589/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4721589/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Chen, H T -- Bhandoola, A -- Difilippantonio, M J -- Zhu, J -- Brown, M J -- Tai, X -- Rogakou, E P -- Brotz, T M -- Bonner, W M -- Ried, T -- Nussenzweig, A -- Z99 CA999999/Intramural NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 8;290(5498):1962-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Experimental Immunology Branch, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11110662" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Nucleus/metabolism ; DNA Damage ; DNA-Binding Proteins/metabolism ; Fluorescent Antibody Technique ; *Gene Rearrangement, alpha-Chain T-Cell Antigen Receptor ; *Genes, T-Cell Receptor alpha ; Histones/*metabolism ; Homeodomain Proteins/metabolism ; Mice ; Mice, Transgenic ; Microscopy, Confocal ; Molecular Sequence Data ; Nuclear Proteins/*metabolism ; Phosphorylation ; *Recombination, Genetic ; T-Lymphocytes/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Roles of PLC-beta2 and -beta3 and PI3Kgamma in chemoattractant-mediated signal transduction (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-11
    Description: The roles of phosphoinositide 3-kinase (PI3K) and phospholipase C (PLC) in chemoattractant-elicited responses were studied in mice lacking these key enzymes. PI3Kgamma was required for chemoattractant-induced production of phosphatidylinositol 3,4,5-trisphosphate [PtdIns (3,4,5)P3] and has an important role in chemoattractant-induced superoxide production and chemotaxis in mouse neutrophils and in production of T cell-independent antigen-specific antibodies composed of the immunoglobulin lambda light chain (TI-IglambdaL). The study of the mice lacking PLC-beta2 and -beta3 revealed that the PLC pathways have an important role in chemoattractant-mediated production of superoxide and regulation of protein kinases, but not chemotaxis. The PLC pathways also appear to inhibit the chemotactic activity induced by certain chemoattractants and to suppress TI-IglambdaL production.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Li, Z -- Jiang, H -- Xie, W -- Zhang, Z -- Smrcka, A V -- Wu, D -- New York, N.Y. -- Science. 2000 Feb 11;287(5455):1046-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Rochester, Rochester, NY 14642, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10669417" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; B-Lymphocytes/immunology ; Chemokine CCL4 ; Chemotactic Factors/*pharmacology ; Chemotaxis, Leukocyte/*physiology ; Immunoglobulin lambda-Chains/biosynthesis ; Isoenzymes/*metabolism ; Macrophage Inflammatory Proteins/pharmacology ; Mice ; N-Formylmethionine Leucyl-Phenylalanine/pharmacology ; Neutrophil Infiltration ; Neutrophils/metabolism/*physiology ; Peritonitis/immunology ; Phosphatidylinositol 3-Kinases/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase C beta ; Phosphorylation ; *Signal Transduction ; Skin Ulcer/pathology ; Superoxides/metabolism ; Type C Phospholipases/*metabolism
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    Cross talk between interferon-gamma and -alpha/beta signaling components in caveolar membrane domains (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-07-06
    Description: Definition of cellular responses to cytokines often involves cross-communication through their respective receptors. Here, signaling by interferon-gamma (IFN-gamma) is shown to depend on the IFN-alpha/beta receptor components. Although these IFNs transmit signals through distinct receptor complexes, the IFN-alpha/beta receptor component, IFNAR1, facilitates efficient assembly of IFN-gamma-activated transcription factors. This cross talk is contingent on a constitutive subthreshold IFN-alpha/beta signaling and the association between the two nonligand-binding receptor components, IFNAR1 and IFNGR2, in the caveolar membrane domains. This aspect of signaling cross talk by IFNs may apply to other cytokines.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Takaoka, A -- Mitani, Y -- Suemori, H -- Sato, M -- Yokochi, T -- Noguchi, S -- Tanaka, N -- Taniguchi, T -- New York, N.Y. -- Science. 2000 Jun 30;288(5475):2357-60.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, Graduate School of Medicine and Faculty of Medicine, University of Tokyo, Hongo 7-3-1, Bunkyo-ku, Tokyo 113-0033, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10875919" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Membrane/*metabolism ; Cells, Cultured ; Cytopathogenic Effect, Viral ; DNA-Binding Proteins/metabolism ; Dimerization ; Encephalomyocarditis virus/drug effects/physiology ; Interferon Type I/*metabolism ; Interferon-alpha/genetics/metabolism/pharmacology ; Interferon-beta/genetics/metabolism/pharmacology ; Interferon-gamma/*metabolism/pharmacology ; Janus Kinase 1 ; Janus Kinase 2 ; Membrane Proteins ; Mice ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; *Receptor Cross-Talk ; Receptor, Interferon alpha-beta ; Receptors, Interferon/genetics/*metabolism ; Recombinant Proteins ; STAT1 Transcription Factor ; *Signal Transduction ; Trans-Activators/metabolism
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    Regulation of JNK by Src during Drosophila development (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-01-15
    Description: In Drosophila, the Jun amino-terminal kinase (JNK) homolog Basket (Bsk) is required for epidermal closure. Mutants for Src42A, a Drosophila c-src protooncogene homolog, are described. Src42A functions in epidermal closure during both embryogenesis and metamorphosis. The severity of the epidermal closure defect in the Src42A mutant depended on the amount of Bsk activity, and the amount of Bsk activity depended on the amount of Src42A. Thus, activation of the Bsk pathway is required downstream of Src42A in epidermal closure. This work confirms mammalian studies that demonstrated a physiological link between Src and JNK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Tateno, M -- Nishida, Y -- Adachi-Yamada, T -- New York, N.Y. -- Science. 2000 Jan 14;287(5451):324-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Biological Science, Graduate School of Science, Nagoya University, Chikusa-ku, Nagoya 464-8602, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10634792" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Animals ; Drosophila/embryology/genetics/*growth & development/metabolism ; *Drosophila Proteins ; Enzyme Activation ; Epidermis/embryology ; Genes, Insect ; Insect Proteins/genetics/metabolism ; JNK Mitogen-Activated Protein Kinases ; Metamorphosis, Biological ; Mitogen-Activated Protein Kinases/*metabolism ; Phenotype ; Phosphoprotein Phosphatases/genetics/metabolism ; Phosphorylation ; Phosphotyrosine/metabolism ; Point Mutation ; Protein-Tyrosine Kinases/genetics/*metabolism ; Proto-Oncogene Proteins/genetics/*metabolism ; Signal Transduction
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    Designing small-molecule switches for protein-protein interactions (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-06-17
    Description: Mutations introduced into human growth hormone (hGH) (Thr175 --〉 Gly-hGH) and the extracellular domain of the hGH receptor (Trp104 --〉 Gly-hGHbp) created a cavity at the protein-protein interface that resulted in binding affinity being reduced by a factor of 10(6). A small library of indole analogs was screened for small molecules that bind the cavity created by the mutations and restore binding affinity. The ligand 5-chloro-2-trichloromethylimidazole was found to increase the affinity of the mutant hormone for its receptor more than 1000-fold. Cell proliferation and JAK2 phosphorylation assays showed that the mutant hGH activates growth hormone signaling in the presence of added ligand. This approach may allow other protein-protein and protein-nucleic acid interactions to be switched on or off by the addition or depletion of exogenous small molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guo, Z -- Zhou, D -- Schultz, P G -- New York, N.Y. -- Science. 2000 Jun 16;288(5473):2042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Chemistry and the Skaggs Institute for Chemical Biology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10856217" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Binding Sites ; Cell Division ; Cell Line ; Human Growth Hormone/chemistry/genetics/*metabolism ; Imidazoles/*chemistry/metabolism ; Janus Kinase 2 ; Ligands ; Mice ; Molecular Sequence Data ; Peptide Library ; Phosphorylation ; Protein Binding ; Protein-Tyrosine Kinases/metabolism ; *Proto-Oncogene Proteins ; Receptors, Somatotropin/chemistry/genetics/*metabolism ; Signal Transduction ; Structure-Activity Relationship ; Transfection
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    Translocation of Helicobacter pylori CagA into gastric epithelial cells by type IV secretion (2000)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2000-02-26
    Description: The Gram-negative bacterium Helicobacter pylori is a causative agent of gastritis and peptic ulcer disease in humans. Strains producing the CagA antigen (cagA(+)) induce strong gastric inflammation and are strongly associated with gastric adenocarcinoma and MALT lymphoma. We show here that such strains translocate the bacterial protein CagA into gastric epithelial cells by a type IV secretion system, encoded by the cag pathogenicity island. CagA is tyrosine-phosphorylated and induces changes in the tyrosine phosphorylation state of distinct cellular proteins. Modulation of host cells by bacterial protein translocation adds a new dimension to the chronic Helicobacter infection with yet unknown consequences.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Odenbreit, S -- Puls, J -- Sedlmaier, B -- Gerland, E -- Fischer, W -- Haas, R -- New York, N.Y. -- Science. 2000 Feb 25;287(5457):1497-500.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max von Pettenkofer Institute for Hygiene and Medical Microbiology, Ludwig-Maximilians University Munich, D-80336 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10688800" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Motifs ; *Antigens, Bacterial ; Bacterial Proteins/genetics/*metabolism ; Biological Transport ; Enzyme Inhibitors/pharmacology ; Epithelial Cells/metabolism/microbiology ; Fluorescent Antibody Technique ; Gastric Mucosa/*metabolism/*microbiology ; Genes, Bacterial ; Genetic Complementation Test ; Genistein/pharmacology ; Helicobacter pylori/genetics/*metabolism/pathogenicity ; Humans ; Mutation ; Phosphorylation ; Phosphotyrosine/metabolism ; Protein-Tyrosine Kinases/antagonists & inhibitors/metabolism ; Staurosporine/pharmacology ; Tumor Cells, Cultured ; Virulence
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    Quinones as the redox signal for the arc two-component system of bacteria (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-06-26
    Description: The Arc two-component signal transduction system mediates adaptive responses of Escherichia coli to changing respiratory conditions of growth. Under anaerobic conditions, the ArcB sensor kinase autophosphorylates and then transphosphorylates ArcA, a global transcriptional regulator that controls the expression of numerous operons involved in respiratory or fermentative metabolism. We show that oxidized forms of quinone electron carriers act as direct negative signals that inhibit autophosphorylation of ArcB during aerobiosis. Thus, the Arc signal transduction system provides a link between the electron transport chain and gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Georgellis, D -- Kwon, O -- Lin, E C -- GM40993/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Jun 22;292(5525):2314-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Microbiology and Molecular Genetics, Harvard Medical School, 200 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11423658" target="_blank"〉PubMed〈/a〉
    Keywords: Aerobiosis ; Bacterial Outer Membrane Proteins/*metabolism ; Electron Transport ; Escherichia coli/genetics/*metabolism ; *Escherichia coli Proteins ; Gene Expression Regulation, Bacterial ; Membrane Proteins/*metabolism ; Mutation ; Oxidation-Reduction ; Phosphorylation ; Protein Kinases/*metabolism ; Quinones/*metabolism ; *Repressor Proteins ; *Signal Transduction ; Ubiquinone/metabolism ; Vitamin K/*analogs & derivatives/metabolism ; *Vitamin K 2/*analogs & derivatives
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    A circadian output in Drosophila mediated by neurofibromatosis-1 and Ras/MAPK (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-09-22
    Description: Output from the circadian clock controls rhythmic behavior through poorly understood mechanisms. In Drosophila, null mutations of the neurofibromatosis-1 (Nf1) gene produce abnormalities of circadian rhythms in locomotor activity. Mutant flies show normal oscillations of the clock genes period (per) and timeless (tim) and of their corresponding proteins, but altered oscillations and levels of a clock-controlled reporter. Mitogen-activated protein kinase (MAPK) activity is increased in Nf1 mutants, and the circadian phenotype is rescued by loss-of-function mutations in the Ras/MAPK pathway. Thus, Nf1 signals through Ras/MAPK in Drosophila. Immunohistochemical staining revealed a circadian oscillation of phospho-MAPK in the vicinity of nerve terminals containing pigment-dispersing factor (PDF), a secreted output from clock cells, suggesting a coupling of PDF to Ras/MAPK signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Williams, J A -- Su, H S -- Bernards, A -- Field, J -- Sehgal, A -- New York, N.Y. -- Science. 2001 Sep 21;293(5538):2251-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Center for Sleep and Respiratory Neurobiology, Department of Pharmacology, University of Pennsylvania School of Medicine, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11567138" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Animals ; Biological Clocks ; Brain/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/genetics/*metabolism ; *Circadian Rhythm ; Cyclic AMP Response Element-Binding Protein/genetics/metabolism ; Cyclic AMP-Dependent Protein Kinases/metabolism ; Drosophila/genetics/*physiology ; *Drosophila Proteins ; *Extracellular Signal-Regulated MAP Kinases ; Genes, Insect ; Genes, Neurofibromatosis 1 ; Insect Proteins/*genetics/metabolism/*physiology ; MAP Kinase Signaling System ; Male ; Motor Activity ; Mutation ; Nerve Endings/metabolism ; Nerve Tissue Proteins/*genetics/*physiology ; Neuropeptides/genetics/metabolism ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; Phosphorylation ; Signal Transduction ; Transgenes ; *ras GTPase-Activating Proteins ; ras Proteins/metabolism
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    Tauopathy in Drosophila: neurodegeneration without neurofibrillary tangles (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-06-16
    Description: The microtubule-binding protein tau has been implicated in the pathogenesis of Alzheimer's disease and related disorders. However, the mechanisms underlying tau-mediated neurotoxicity remain unclear. We created a genetic model of tau-related neurodegenerative disease by expressing wild-type and mutant forms of human tau in the fruit fly Drosophila melanogaster. Transgenic flies showed key features of the human disorders: adult onset, progressive neurodegeneration, early death, enhanced toxicity of mutant tau, accumulation of abnormal tau, and relative anatomic selectivity. However, neurodegeneration occurred without the neurofibrillary tangle formation that is seen in human disease and some rodent tauopathy models. This fly model may allow a genetic analysis of the cellular mechanisms underlying tau neurotoxicity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wittmann, C W -- Wszolek, M F -- Shulman, J M -- Salvaterra, P M -- Lewis, J -- Hutton, M -- Feany, M B -- New York, N.Y. -- Science. 2001 Jul 27;293(5530):711-4. Epub 2001 Jun 14.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Division of Neuropathology, Brigham and Women's Hospital and Harvard Medical School, 221 Longwood Avenue, Room 514, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11408621" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylcholine/metabolism ; Aging ; Animals ; Animals, Genetically Modified ; Brain/pathology/ultrastructure ; *Disease Models, Animal ; *Drosophila melanogaster/genetics ; Humans ; Mutation ; Nerve Degeneration ; Nerve Endings/metabolism/ultrastructure ; Neurodegenerative Diseases/metabolism/*pathology ; Neurofibrillary Tangles/ultrastructure ; Neurons/metabolism/*ultrastructure ; Neuropil/ultrastructure ; Phosphorylation ; Vacuoles/ultrastructure ; tau Proteins/chemistry/genetics/*metabolism
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    Cell cycle. Order from destruction (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-10-06
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartek, J -- Lukas, J -- New York, N.Y. -- Science. 2001 Oct 5;294(5540):66-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cancer Biology, Danish Cancer Society, DK-2100 Copenhagen, Denmark. bartek@biobase.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11588240" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/genetics ; *CDC2-CDC28 Kinases ; *Cell Cycle ; Cell Cycle Proteins/genetics/*metabolism ; Cell Membrane/metabolism ; Cell Nucleus/metabolism ; Cyclin E/genetics/*metabolism ; Cyclin-Dependent Kinase 2 ; Cyclin-Dependent Kinases/*metabolism ; Cysteine Endopeptidases/metabolism ; *F-Box Proteins ; Female ; Gene Expression ; Humans ; Multienzyme Complexes/metabolism ; Mutation ; Neoplasms/etiology ; Ovarian Neoplasms/genetics ; Peptide Synthases/*metabolism ; Phosphorylation ; Proteasome Endopeptidase Complex ; Protein-Serine-Threonine Kinases/*metabolism ; SKP Cullin F-Box Protein Ligases ; *Ubiquitin-Protein Ligases ; Ubiquitins/*metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular biology. The histone modification circus (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-04-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Berger, S L -- New York, N.Y. -- Science. 2001 Apr 6;292(5514):64-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Molecular Genetics Program, The Wistar Institute, Philadelphia, PA 19104, USA. berger@wistar.upenn.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11294220" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Cell Cycle Proteins/genetics/metabolism ; Centromere/metabolism ; Chromatin/metabolism ; Fungal Proteins/chemistry/metabolism ; *Gene Expression Regulation, Fungal ; *Gene Silencing ; Heterochromatin/metabolism ; Histone Deacetylases/metabolism ; *Histone-Lysine N-Methyltransferase ; Histones/*metabolism ; Lysine/metabolism ; Methylation ; Methyltransferases/metabolism ; Phosphorylation ; Protein Binding ; Protein Methyltransferases ; Protein Structure, Tertiary ; *Saccharomyces cerevisiae Proteins ; Schizosaccharomyces/*genetics/metabolism ; *Schizosaccharomyces pombe Proteins ; Serine/metabolism ; Transcription Factors/chemistry/metabolism
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    Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-18
    Description: Organelle transport by myosin-V is down-regulated during mitosis, presumably by myosin-V phosphorylation. We used mass spectrometry phosphopeptide mapping to show that the tail of myosin-V was phosphorylated in mitotic Xenopus egg extract on a single serine residue localized in the carboxyl-terminal organelle-binding domain. Phosphorylation resulted in the release of the motor from the organelle. The phosphorylation site matched the consensus sequence of calcium/calmodulin-dependent protein kinase II (CaMKII), and inhibitors of CaMKII prevented myosin-V release. The modulation of cargo binding by phosphorylation is likely to represent a general mechanism regulating organelle transport by myosin-V.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karcher, R L -- Roland, J T -- Zappacosta, F -- Huddleston, M J -- Annan, R S -- Carr, S A -- Gelfand, V I -- GM-52111/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 17;293(5533):1317-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509731" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Biological Transport ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Calmodulin-Binding Proteins/chemistry/genetics/*metabolism ; Cell Extracts ; Egtazic Acid/analogs & derivatives/pharmacology ; Enzyme Inhibitors/pharmacology ; Interphase ; Mass Spectrometry ; Melanophores/metabolism/ultrastructure ; Melanosomes/*metabolism ; *Mitosis ; Molecular Motor Proteins/*metabolism ; Molecular Sequence Data ; Mutation ; *Myosin Type V ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Ovum ; Peptides/pharmacology ; Phosphopeptides/analysis/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection ; Xenopus
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    Induction of apoptosis by a secreted lipocalin that is transcriptionally regulated by IL-3 deprivation (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-04
    Description: Many hematopoietic cells undergo apoptosis when deprived of specific cytokines, and this process requires de novo RNA/protein synthesis. Using DNA microarrays to analyze interleukin-3 (IL-3)-dependent murine FL5.12 pro-B cells, we found that the gene undergoing maximal transcriptional induction after cytokine withdrawal is 24p3, which encodes a secreted lipocalin. Conditioned medium from IL-3-deprived FL5.12 cells contained 24p3 and induced apoptosis in naive FL5.12 cells even when IL-3 was present. 24p3 also induced apoptosis in a wide variety of leukocytes but not other cell types. Apoptotic sensitivity correlated with the presence of a putative 24p3 cell surface receptor. We conclude that IL-3 deprivation activates 24p3 transcription, leading to synthesis and secretion of 24p3, which induces apoptosis through an autocrine pathway.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Devireddy, L R -- Teodoro, J G -- Richard, F A -- Green, M R -- New York, N.Y. -- Science. 2001 Aug 3;293(5531):829-34.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Program in Gene Function and Expression and Program in Molecular Medicine, University of Massachusetts Medical School, 373 Plantation Street, Worcester, MA 01605, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11486081" target="_blank"〉PubMed〈/a〉
    Keywords: Acute-Phase Proteins/*genetics/*metabolism ; Animals ; *Apoptosis/drug effects ; Autocrine Communication ; Carrier Proteins/metabolism ; Cell Line ; Cells, Cultured ; Culture Media, Conditioned ; Dexamethasone/pharmacology ; *Gene Expression Regulation ; Humans ; Insulin-Like Growth Factor I/pharmacology ; Interleukin-3/*metabolism ; Interleukins/metabolism ; Leukocytes/cytology/*physiology ; Lipocalins ; Mice ; Oligonucleotide Array Sequence Analysis ; Oncogene Proteins/*genetics/*metabolism ; Phosphorylation ; Proto-Oncogene Proteins ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Receptors, Cell Surface/metabolism ; Recombinant Fusion Proteins/metabolism ; Transcription, Genetic ; Tumor Cells, Cultured ; bcl-Associated Death Protein ; bcl-X Protein
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    Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-10-06
    Description: Although trafficking and degradation of several membrane proteins are regulated by ubiquitination catalyzed by E3 ubiquitin ligases, there has been little evidence connecting ubiquitination with regulation of mammalian G protein (heterotrimeric guanine nucleotide-binding protein)-coupled receptor (GPCR) function. Agonist stimulation of endogenous or transfected beta2-adrenergic receptors (beta2ARs) led to rapid ubiquitination of both the receptors and the receptor regulatory protein, beta-arrestin. Moreover, proteasome inhibitors reduced receptor internalization and degradation, thus implicating a role for the ubiquitination machinery in the trafficking of the beta2AR. Receptor ubiquitination required beta-arrestin, which bound to the E3 ubiquitin ligase Mdm2. Abrogation of beta-arrestin ubiquitination, either by expression in Mdm2-null cells or by dominant-negative forms of Mdm2 lacking E3 ligase activity, inhibited receptor internalization with marginal effects on receptor degradation. However, a beta2AR mutant lacking lysine residues, which was not ubiquitinated, was internalized normally but was degraded ineffectively. These findings delineate an adapter role of beta-arrestin in mediating the ubiquitination of the beta2AR and indicate that ubiquitination of the receptor and of beta-arrestin have distinct and obligatory roles in the trafficking and degradation of this prototypic GPCR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shenoy, S K -- McDonald, P H -- Kohout, T A -- Lefkowitz, R J -- HL16037/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2001 Nov 9;294(5545):1307-13. Epub 2001 Oct 4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Department of Medicine, Duke University Medical Center, Box 3821, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11588219" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/*metabolism ; COS Cells ; Catalysis ; Cell Line ; Cricetinae ; Cricetulus ; Cysteine Endopeptidases/metabolism ; Humans ; Isoproterenol/pharmacology ; Ligases/metabolism ; Multienzyme Complexes/antagonists & inhibitors/metabolism ; Mutation ; *Nuclear Proteins ; Phosphorylation ; Proteasome Endopeptidase Complex ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-mdm2 ; Receptors, Adrenergic, beta-2/genetics/*metabolism ; Recombinant Proteins/metabolism ; Transfection ; Ubiquitin/*metabolism ; Ubiquitin-Protein Ligases
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    Role of the sphingosine-1-phosphate receptor EDG-1 in PDGF-induced cell motility (2001)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2001-03-07
    Description: EDG-1 is a heterotrimeric guanine nucleotide binding protein-coupled receptor (GPCR) for sphingosine-1-phosphate (SPP). Cell migration toward platelet-derived growth factor (PDGF), which stimulates sphingosine kinase and increases intracellular SPP, was dependent on expression of EDG-1. Deletion of edg-1 or inhibition of sphingosine kinase suppressed chemotaxis toward PDGF and also activation of the small guanosine triphosphatase Rac, which is essential for protrusion of lamellipodia and forward movement. Moreover, PDGF activated EDG-1, as measured by translocation of beta-arrestin and phosphorylation of EDG-1. Our results reveal a role for receptor cross-communication in which activation of a GPCR by a receptor tyrosine kinase is critical for cell motility.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hobson, J P -- Rosenfeldt, H M -- Barak, L S -- Olivera, A -- Poulton, S -- Caron, M G -- Milstien, S -- Spiegel, S -- CA61774/CA/NCI NIH HHS/ -- GM43880/GM/NIGMS NIH HHS/ -- HL-61365/HL/NHLBI NIH HHS/ -- NS19576/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2001 Mar 2;291(5509):1800-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Georgetown University Medical Center, Washington, DC 20007, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11230698" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestins/metabolism ; Cell Line ; Cell Membrane/metabolism ; Cells, Cultured ; *Chemotaxis/drug effects ; Gene Deletion ; Humans ; Immediate-Early Proteins/genetics/*metabolism ; *Lysophospholipids ; Mice ; Muscle, Smooth, Vascular/cytology/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/antagonists & inhibitors/metabolism ; Platelet-Derived Growth Factor/metabolism/*pharmacology ; Proto-Oncogene Proteins c-sis ; Receptor Cross-Talk ; *Receptors, Cell Surface ; *Receptors, G-Protein-Coupled ; Receptors, Lysophospholipid ; Receptors, Platelet-Derived Growth Factor/metabolism ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Sphingosine/*analogs & derivatives/*metabolism/pharmacology ; Transfection
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    Transcription. Translocating tubby (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-06-16
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cantley, L C -- New York, N.Y. -- Science. 2001 Jun 15;292(5524):2019-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School and Division of Signal Transduction, Beth Israel Deaconess Medical Center, Boston, MA 02115, USA. cantley@helix.mgh.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11408644" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Adaptor Proteins, Signal Transducing ; Animals ; Calcium/metabolism ; Cell Membrane/*metabolism ; Cell Nucleus/*metabolism ; GTP-Binding Protein alpha Subunits, Gq-G11 ; Heterotrimeric GTP-Binding Proteins/metabolism ; Hydrolysis ; Isoenzymes/*metabolism ; Membrane Lipids/metabolism ; Mice ; Obesity/genetics/metabolism ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase C beta ; Phosphorylation ; Protein Structure, Tertiary ; Proteins/chemistry/genetics/*metabolism ; Receptor, Serotonin, 5-HT2C ; Receptors, Serotonin/metabolism ; Signal Transduction ; Transcription Factors/chemistry/genetics/*metabolism ; Type C Phospholipases/*metabolism
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    MAPKK-independent activation of p38alpha mediated by TAB1-dependent autophosphorylation of p38alpha (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-02-16
    Description: Phosphorylation of mitogen-activated protein kinases (MAPKs) on specific tyrosine and threonine sites by MAP kinase kinases (MAPKKs) is thought to be the sole activation mechanism. Here, we report an unexpected activation mechanism for p38alpha MAPK that does not involve the prototypic kinase cascade. Rather it depends on interaction of p38alpha with TAB1 [transforming growth factor-beta-activated protein kinase 1 (TAK1)-binding protein 1] leading to autophosphorylation and activation of p38alpha. We detected formation of a TRAF6-TAB1-p38alpha complex and showed stimulus-specific TAB1-dependent and TAB1-independent p38alpha activation. These findings suggest that alternative activation pathways contribute to the biological responses of p38alpha to various stimuli.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ge, Baoxue -- Gram, Hermann -- Di Padova, Franco -- Huang, Betty -- New, Liguo -- Ulevitch, Richard J -- Luo, Ying -- Han, Jiahuai -- AI41637/AI/NIAID NIH HHS/ -- HL07195/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 15;295(5558):1291-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Immunology, The Scripps Research Institute, 10550 North Torrey Pines Road, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11847341" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Binding Sites ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Line ; *Drosophila Proteins ; Enzyme Activation ; Enzyme Inhibitors/pharmacology ; Humans ; Imidazoles/pharmacology ; *Intracellular Signaling Peptides and Proteins ; MAP Kinase Kinase 6 ; *MAP Kinase Signaling System ; Membrane Glycoproteins/metabolism ; Mitogen-Activated Protein Kinase 14 ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Mitogen-Activated Protein Kinases/antagonists & ; inhibitors/chemistry/genetics/*metabolism ; Mutation ; Peptide Mapping ; Peroxynitrous Acid/pharmacology ; Phosphorylation ; Proteins/metabolism ; Pyridines/pharmacology ; Receptors, Cell Surface/metabolism ; Recombinant Fusion Proteins/metabolism ; TNF Receptor-Associated Factor 6 ; Toll-Like Receptors ; Tumor Necrosis Factor-alpha/pharmacology ; Two-Hybrid System Techniques ; p38 Mitogen-Activated Protein Kinases
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    Neurobiology. Learning more about NMDA receptor regulation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ghosh, Anirvan -- New York, N.Y. -- Science. 2002 Jan 18;295(5554):449-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neuroscience, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA. aghosh@jhmi.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799227" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/*metabolism ; Cyclic AMP Response Element-Binding Protein/metabolism ; Ephrin-B2 ; Glutamic Acid/metabolism ; Hippocampus/metabolism/physiology ; Ligands ; Membrane Proteins/*metabolism/pharmacology ; Mice ; *Neuronal Plasticity ; Neurons/metabolism/physiology ; Phosphorylation ; Protein Structure, Tertiary ; Receptor Protein-Tyrosine Kinases/chemistry/genetics/*metabolism ; Receptor, EphB4 ; Receptors, Eph Family ; Receptors, N-Methyl-D-Aspartate/chemistry/*metabolism ; Signal Transduction ; Synapses/*metabolism ; Synaptic Membranes/metabolism ; src-Family Kinases/metabolism
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    Mitogen-activated protein kinase pathways mediated by ERK, JNK, and p38 protein kinases (2002)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2002-12-10
    Description: Multicellular organisms have three well-characterized subfamilies of mitogen-activated protein kinases (MAPKs) that control a vast array of physiological processes. These enzymes are regulated by a characteristic phosphorelay system in which a series of three protein kinases phosphorylate and activate one another. The extracellular signal-regulated kinases (ERKs) function in the control of cell division, and inhibitors of these enzymes are being explored as anticancer agents. The c-Jun amino-terminal kinases (JNKs) are critical regulators of transcription, and JNK inhibitors may be effective in control of rheumatoid arthritis. The p38 MAPKs are activated by inflammatory cytokines and environmental stresses and may contribute to diseases like asthma and autoimmunity.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Johnson, Gary L -- Lapadat, Razvan -- New York, N.Y. -- Science. 2002 Dec 6;298(5600):1911-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Colorado Health Sciences Center, Denver, CO 80262, USA. gary.johnson@uchsc.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12471242" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Cell Division ; Cytokines/metabolism ; Enzyme Activation ; Gene Expression Regulation ; Humans ; MAP Kinase Kinase Kinases/metabolism ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase 1/metabolism ; Mitogen-Activated Protein Kinase 10 ; Mitogen-Activated Protein Kinase 3 ; Mitogen-Activated Protein Kinase 8 ; Mitogen-Activated Protein Kinase 9 ; Mitogen-Activated Protein Kinases/*metabolism ; Neoplasms/enzymology/pathology ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Transcription, Genetic ; p38 Mitogen-Activated Protein Kinases
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    Retrograde support of neuronal survival without retrograde transport of nerve growth factor (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-01-19
    Description: Application of nerve growth factor (NGF) covalently cross-linked to beads increased the phosphorylation of TrkA and Akt, but not of mitogen-activated protein kinase, in cultured rat sympathetic neurons. NGF beads or iodine-125-labeled NGF beads supplied to distal axons resulted in the survival of over 80% of the neurons for 30 hours, with little or no retrograde transport of iodine-125-labeled NGF; whereas application of free iodine-125-labeled NGF (0.5 nanograms per milliliter) produced 20-fold more retrograde transport, but only 29% of the neurons survived. Thus, in contrast to widely accepted theory, a neuronal survival signal can reach the cell bodies unaccompanied by the NGF that initiated it.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacInnis, Bronwyn L -- Campenot, Robert B -- New York, N.Y. -- Science. 2002 Feb 22;295(5559):1536-9. Epub 2002 Jan 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, 6-14 Medical Sciences Building, University of Alberta, Edmonton, Alberta, Canada, T6G 2H7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11799202" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Axons/*metabolism ; Cell Survival/drug effects ; Cells, Cultured ; Chromones/pharmacology ; Cross-Linking Reagents ; Enzyme Inhibitors/pharmacology ; Iodine Radioisotopes ; Microspheres ; Mitogen-Activated Protein Kinases/metabolism ; Morpholines/pharmacology ; Nerve Growth Factor/*metabolism/pharmacology ; Neurons/metabolism/*physiology ; Phosphatidylinositol 3-Kinases/antagonists & inhibitors/metabolism ; Phosphorylation ; Protein Transport ; *Protein-Serine-Threonine Kinases ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins c-akt ; Rats ; Rats, Sprague-Dawley ; Receptor, trkA/metabolism ; Signal Transduction ; Superior Cervical Ganglion
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    Hijacking of host cell IKK signalosomes by the transforming parasite Theileria (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-11-02
    Description: Parasites have evolved a plethora of mechanisms to ensure their propagation and evade antagonistic host responses. The intracellular protozoan parasite Theileria is the only eukaryote known to induce uncontrolled host cell proliferation. Survival of Theileria-transformed leukocytes depends strictly on constitutive nuclear factor kappa B (NF-kappaB) activity. We found that this was mediated by recruitment of the multisubunit IkappaB kinase (IKK) into large, activated foci on the parasite surface. IKK signalosome assembly was specific for the transforming schizont stage of the parasite and was down-regulated upon differentiation into the nontransforming merozoite stage. Our findings provide insights into IKK activation and how pathogens subvert host-cell signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Heussler, Volker T -- Rottenberg, Sven -- Schwab, Rebekka -- Kuenzi, Peter -- Fernandez, Paula C -- McKellar, Susan -- Shiels, Brian -- Chen, Zhijian J -- Orth, Kim -- Wallach, David -- Dobbelaere, Dirk A E -- GM63692/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Nov 1;298(5595):1033-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Pathology, Institute of Animal Pathology, University of Bern, CH-3012 Bern, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12411708" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Animals ; Antiprotozoal Agents/pharmacology ; Apoptosis ; Cattle ; Cell Cycle ; Cell Division ; Cell Line, Transformed ; Cell Nucleus/metabolism ; Down-Regulation ; I-kappa B Kinase ; I-kappa B Proteins/metabolism ; Leukocytes/enzymology/*parasitology/physiology ; Microscopy, Confocal ; NF-kappa B/metabolism ; Naphthoquinones/pharmacology ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Signal Transduction ; Theileria/growth & development/metabolism/*pathogenicity
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  • 84
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    A LAT mutation that inhibits T cell development yet induces lymphoproliferation (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-06-18
    Description: Mice homozygous for a single tyrosine mutation in LAT (linker for activation of T cells) exhibited an early block in T cell maturation but later developed a polyclonal lymphoproliferative disorder and signs of autoimmune disease. T cell antigen receptor (TCR)-induced activation of phospholipase C-gamma1 (PLC-gamma1) and of nuclear factor of activated T cells, calcium influx, interleukin-2 production, and cell death were reduced or abrogated in T cells from LAT mutant mice. In contrast, TCR-induced Erk activation was intact. These results identify a critical role for integrated PLC-gamma1 and Ras-Erk signaling through LAT in T cell development and homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sommers, Connie L -- Park, Cheung-Seog -- Lee, Jan -- Feng, Chiguang -- Fuller, Claudette L -- Grinberg, Alexander -- Hildebrand, Jay A -- Lacana, Emanuela -- Menon, Rashmi K -- Shores, Elizabeth W -- Samelson, Lawrence E -- Love, Paul E -- New York, N.Y. -- Science. 2002 Jun 14;296(5575):2040-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Cellular and Molecular Biology, Center for Cancer Research, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12065840" target="_blank"〉PubMed〈/a〉
    Keywords: *Adaptor Proteins, Signal Transducing ; Animals ; Antibodies, Antinuclear/blood ; Antigens, CD5/analysis ; Autoimmune Diseases/immunology ; CD4-Positive T-Lymphocytes/immunology/physiology ; Calcium/metabolism ; Calcium Signaling ; Carrier Proteins/*genetics/*physiology ; Cell Division ; Interleukin-2/biosynthesis ; Isoenzymes/*metabolism ; Lymphocyte Activation ; Lymphoproliferative Disorders/*etiology/immunology/pathology ; MAP Kinase Signaling System ; *Membrane Proteins ; Mice ; Mice, Inbred C57BL ; Mitogen-Activated Protein Kinases/metabolism ; Phenotype ; Phospholipase C gamma ; Phosphoproteins/*genetics/*physiology ; Phosphorylation ; *Point Mutation ; Receptors, Antigen, T-Cell/immunology/metabolism ; Signal Transduction ; T-Lymphocyte Subsets/immunology/physiology ; T-Lymphocytes/*immunology/physiology ; Thymus Gland/cytology/immunology/pathology ; Transcription Factors/metabolism ; Type C Phospholipases/*metabolism ; ras Proteins/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 85
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    Tech.Sight. Molecular biology. Making catalytic DNAs (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Breaker, R R -- New York, N.Y. -- Science. 2000 Dec 15;290(5499):2095-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular, Cellular, and Developmental Biology, Yale University, New Haven, CT 06520-8103, USA. ronald.breaker@yale.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11187837" target="_blank"〉PubMed〈/a〉
    Keywords: Binding Sites ; Catalysis ; Catalytic Domain ; DNA/*metabolism ; DNA, Catalytic/*chemistry/*metabolism ; Nucleic Acid Conformation ; Oxidation-Reduction ; Phosphorylation ; RNA/*metabolism
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  • 86
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    Efficient initiation of HCV RNA replication in cell culture (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-12-09
    Description: Hepatitis C virus (HCV) infection is a global health problem affecting an estimated 170 million individuals worldwide. We report the identification of multiple independent adaptive mutations that cluster in the HCV nonstructural protein NS5A and confer increased replicative ability in vitro. Among these adaptive mutations were a single amino acid substitution that allowed HCV RNA replication in 10% of transfected hepatoma cells and a deletion of 47 amino acids encompassing the interferon (IFN) sensitivity determining region (ISDR). Independent of the ISDR, IFN-alpha rapidly inhibited HCV RNA replication in vitro. This work establishes a robust, cell-based system for genetic and functional analyses of HCV replication.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Blight, K J -- Kolykhalov, A A -- Rice, C M -- AI40034/AI/NIAID NIH HHS/ -- CA57973/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2000 Dec 8;290(5498):1972-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Washington University School of Medicine, 660 South Euclid Avenue, St. Louis, MO 63110-1093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11110665" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Substitution ; Hepacivirus/drug effects/genetics/*physiology ; Humans ; Interferon-alpha/pharmacology ; Mutation ; Phosphorylation ; Point Mutation ; RNA Replicase/genetics/metabolism ; RNA, Viral/*biosynthesis ; *Replicon ; Sequence Deletion ; Transfection ; Tumor Cells, Cultured ; Viral Nonstructural Proteins/*genetics/*metabolism ; Virus Replication
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 87
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    Cell cycle. Piecing together the p53 puzzle (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-02-07
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Carr, A M -- New York, N.Y. -- Science. 2000 Mar 10;287(5459):1765-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉MRC Cell Mutation Unit, Sussex University, Falmer, Brighton BN1 9RR, UK. a.m.carr@sussex.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10755928" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins ; Checkpoint Kinase 2 ; *DNA Damage ; DNA-Binding Proteins ; G1 Phase ; G2 Phase ; Genes, Tumor Suppressor ; Humans ; *Interphase ; Mice ; Neoplasms/etiology ; Phosphorylation ; Phosphoserine/metabolism ; *Protein Kinases ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Signal Transduction ; Transcription, Genetic ; Tumor Suppressor Protein p53/*metabolism ; Tumor Suppressor Proteins
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 88
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    Interconnected feedback loops in the Neurospora circadian system (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-07-07
    Description: In Neurospora crassa, white collar 1 (WC-1), a transcriptional activator and positive clock element, is rhythmically expressed from a nonrhythmic steady-state pool of wc-1 transcript, consistent with posttranscriptional regulation of rhythmicity. Mutations in frq influence both the level and periodicity of WC-1 expression, and driven FRQ expression not only depresses its own endogenous levels, but positively regulates WC-1 synthesis with a lag of about 8 hours, a delay similar to that seen in the wild-type clock. FRQ thus plays dual roles in the Neurospora clock and thereby, with WC-1, forms a second feedback loop that would promote robustness and stability in this circadian system. The existence also of interlocked loops in Drosophila melanogaster and mouse clocks suggests that such interlocked loops may be a conserved aspect of circadian timing systems.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lee, K -- Loros, J J -- Dunlap, J C -- MH44651/MH/NIMH NIH HHS/ -- R37-GM 34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2000 Jul 7;289(5476):107-10.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Dartmouth Medical School, Hanover, NH 03755-3844, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10884222" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; *Circadian Rhythm ; DNA-Binding Proteins/biosynthesis/chemistry/genetics/*metabolism ; Darkness ; Feedback ; Fungal Proteins/genetics/*metabolism ; Gene Expression Regulation, Fungal ; Humans ; Kinetics ; Light ; Molecular Sequence Data ; Mutation ; Neurospora crassa/genetics/metabolism/*physiology ; Phosphorylation ; RNA, Fungal/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Sequence Alignment ; Signal Transduction ; Transcription Factors/biosynthesis/chemistry/genetics/*metabolism
    Print ISSN: 0036-8075
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  • 89
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    Hepatitis C virus, the E2 envelope protein, and alpha-interferon resistance (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-25
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Abid, K -- Quadri, R -- Negro, F -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1555.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Gastroenterology and Hepatology, University of Geneva Medical School, Geneva, Switzerland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10733410" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Drug Resistance, Microbial ; Eukaryotic Initiation Factor-2/chemistry/metabolism ; Genotype ; Hepacivirus/*drug effects/genetics ; Hepatitis C/virology ; Humans ; Interferon-alpha/*pharmacology ; Phosphorylation ; Viral Envelope Proteins/*chemistry/*physiology ; eIF-2 Kinase/*antagonists & inhibitors/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 90
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    Circadian rhythms. Marking time for a kingdom (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-05-08
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Young, M W -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):451-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Genetics and National Science Foundation Center for Biological Timing, The Rockefeller University, New York, NY 10021. young@rockvax.rockefeller.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10798982" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Biological Clocks/genetics ; *Casein Kinase Iepsilon ; Casein Kinases ; Cell Cycle Proteins ; *Circadian Rhythm/genetics ; Cloning, Molecular ; Cricetinae ; Drosophila/genetics ; *Drosophila Proteins ; Genes, Insect ; Humans ; Intracellular Signaling Peptides and Proteins ; Mesocricetus ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; Phosphorylation ; Point Mutation ; Protein Kinases/chemistry/*genetics/*metabolism ; Transcription Factors/genetics/metabolism
    Print ISSN: 0036-8075
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 91
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    An ultrasensitive bacterial motor revealed by monitoring signaling proteins in single cells (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-04
    Description: Understanding biology at the single-cell level requires simultaneous measurements of biochemical parameters and behavioral characteristics in individual cells. Here, the output of individual flagellar motors in Escherichia coli was measured as a function of the intracellular concentration of the chemotactic signaling protein. The concentration of this molecule, fused to green fluorescent protein, was monitored with fluorescence correlation spectroscopy. Motors from different bacteria exhibited an identical steep input-output relation, suggesting that they actively contribute to signal amplification in chemotaxis. This experimental approach can be extended to quantitative in vivo studies of other biochemical networks.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cluzel, P -- Surette, M -- Leibler, S -- New York, N.Y. -- Science. 2000 Mar 3;287(5458):1652-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physics, Princeton University, Princeton, NJ 08544, USA. phcluzel@phoenix.princeton.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10698740" target="_blank"〉PubMed〈/a〉
    Keywords: *Bacterial Proteins ; Chemotaxis/*physiology ; Escherichia coli/genetics/*physiology ; Flagella/*physiology ; Green Fluorescent Proteins ; Luminescent Proteins ; Membrane Proteins/genetics/*metabolism ; Molecular Motor Proteins/*physiology ; Movement ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Spectrometry, Fluorescence ; Transformation, Bacterial ; Video Recording
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 92
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    Eta-1 (osteopontin): an early component of type-1 (cell-mediated) immunity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-02-05
    Description: Cell-mediated (type-1) immunity is necessary for immune protection against most intracellular pathogens and, when excessive, can mediate organ-specific autoimmune destruction. Mice deficient in Eta-1 (also called osteopontin) gene expression have severely impaired type-1 immunity to viral infection [herpes simplex virus-type 1 (KOS strain)] and bacterial infection (Listeria monocytogenes) and do not develop sarcoid-type granulomas. Interleukin-12 (IL-12) and interferon-gamma production is diminished, and IL-10 production is increased. A phosphorylation-dependent interaction between the amino-terminal portion of Eta-1 and its integrin receptor stimulated IL-12 expression, whereas a phosphorylation-independent interaction with CD44 inhibited IL-10 expression. These findings identify Eta-1 as a key cytokine that sets the stage for efficient type-1 immune responses through differential regulation of macrophage IL-12 and IL-10 cytokine expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ashkar, S -- Weber, G F -- Panoutsakopoulou, V -- Sanchirico, M E -- Jansson, M -- Zawaideh, S -- Rittling, S R -- Denhardt, D T -- Glimcher, M J -- Cantor, H -- AI12184/AI/NIAID NIH HHS/ -- AI37833/AI/NIAID NIH HHS/ -- CA76176/CA/NCI NIH HHS/ -- etc. -- New York, N.Y. -- Science. 2000 Feb 4;287(5454):860-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory for Skeletal Disorders and Rehabilitation, Department of Orthopedic Surgery, Children's Hospital, Harvard Medical School, 300 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10657301" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD44/metabolism ; Granuloma/immunology ; Herpes Simplex/immunology ; Herpesvirus 1, Human/immunology ; Hypersensitivity, Delayed ; Interferon-gamma/biosynthesis ; Interleukin-10/*biosynthesis ; Interleukin-12/*biosynthesis ; Keratitis, Herpetic/immunology ; Listeriosis/immunology ; Lymphocyte Activation ; Macrophages/*immunology ; Mice ; Mice, Inbred C3H ; Mice, Inbred C57BL ; Mice, Nude ; Osteopontin ; Phosphorylation ; Receptors, Vitronectin/metabolism ; Sialoglycoproteins/*immunology/metabolism/pharmacology ; T-Lymphocytes/*immunology/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 93
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    Positional syntenic cloning and functional characterization of the mammalian circadian mutation tau (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-04-25
    Description: The tau mutation is a semidominant autosomal allele that dramatically shortens period length of circadian rhythms in Syrian hamsters. We report the molecular identification of the tau locus using genetically directed representational difference analysis to define a region of conserved synteny in hamsters with both the mouse and human genomes. The tau locus is encoded by casein kinase I epsilon (CKIepsilon), a homolog of the Drosophila circadian gene double-time. In vitro expression and functional studies of wild-type and tau mutant CKIepsilon enzyme reveal that the mutant enzyme has a markedly reduced maximal velocity and autophosphorylation state. In addition, in vitro CKIepsilon can interact with mammalian PERIOD proteins, and the mutant enzyme is deficient in its ability to phosphorylate PERIOD. We conclude that tau is an allele of hamster CKIepsilon and propose a mechanism by which the mutation leads to the observed aberrant circadian phenotype in mutant animals.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3869379/" target="_blank"〉〈img src="https://static.pubmed.gov/portal/portal3rc.fcgi/4089621/img/3977009" border="0"〉〈/a〉   〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3869379/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lowrey, P L -- Shimomura, K -- Antoch, M P -- Yamazaki, S -- Zemenides, P D -- Ralph, M R -- Menaker, M -- Takahashi, J S -- R01MH56647/MH/NIMH NIH HHS/ -- R37MH39592/MH/NIMH NIH HHS/ -- Howard Hughes Medical Institute/ -- New York, N.Y. -- Science. 2000 Apr 21;288(5465):483-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology and Physiology, Howard Hughes Medical Institute, Northwestern University, Evanston, IL 60208, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10775102" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Casein Kinases ; Cell Cycle Proteins ; Chromosome Mapping ; *Circadian Rhythm/genetics ; Cloning, Molecular ; Cricetinae ; Female ; Heterozygote ; Humans ; Male ; Mesocricetus ; Mice ; Microsatellite Repeats ; Molecular Sequence Data ; Nuclear Proteins/genetics/metabolism ; Period Circadian Proteins ; Phenotype ; Phosphorylation ; *Point Mutation ; Polymerase Chain Reaction ; Polymorphism, Genetic ; Protein Kinases/chemistry/*genetics/*metabolism ; RNA, Messenger/genetics/metabolism ; Recombinant Fusion Proteins/chemistry/metabolism ; Suprachiasmatic Nucleus/metabolism
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    Printing proteins as microarrays for high-throughput function determination (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-09-08
    Description: Systematic efforts are currently under way to construct defined sets of cloned genes for high-throughput expression and purification of recombinant proteins. To facilitate subsequent studies of protein function, we have developed miniaturized assays that accommodate extremely low sample volumes and enable the rapid, simultaneous processing of thousands of proteins. A high-precision robot designed to manufacture complementary DNA microarrays was used to spot proteins onto chemically derivatized glass slides at extremely high spatial densities. The proteins attached covalently to the slide surface yet retained their ability to interact specifically with other proteins, or with small molecules, in solution. Three applications for protein microarrays were demonstrated: screening for protein-protein interactions, identifying the substrates of protein kinases, and identifying the protein targets of small molecules.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉MacBeath, G -- Schreiber, S L -- New York, N.Y. -- Science. 2000 Sep 8;289(5485):1760-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Genomics Research, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA. gavin_macbeath@harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10976071" target="_blank"〉PubMed〈/a〉
    Keywords: Biochemistry/*methods ; Biotin/metabolism ; Digoxigenin/metabolism ; Fluorescence ; Fluorescent Dyes ; Ligands ; *Molecular Probe Techniques ; Phosphorylation ; Piperazines/pharmacology ; *Protein Binding ; Protein Folding ; Protein Kinases/*metabolism ; Proteins/*chemistry/*metabolism ; Robotics ; Serum Albumin, Bovine
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  • 95
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    A role for nuclear inositol 1,4,5-trisphosphate kinase in transcriptional control (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-17
    Description: Phospholipase C and two inositol polyphosphate (IP) kinases constitute a signaling pathway that regulates nuclear messenger RNA export through production of inositol hexakisphosphate (IP6). The inositol 1,4,5-trisphosphate kinase of this pathway in Saccharomyces cerevisiae, designated Ipk2, was found to be identical to Arg82, a regulator of the transcriptional complex ArgR-Mcm1. Synthesis of inositol 1,4,5,6-tetrakisphosphate, but not IP6, was required for gene regulation through ArgR-Mcm1. Thus, the phospholipase C pathway produces multiple IP messengers that modulate distinct nuclear processes. The results reveal a direct mechanism by which activation of IP signaling may control gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Odom, A R -- Stahlberg, A -- Wente, S R -- York, J D -- New York, N.Y. -- Science. 2000 Mar 17;287(5460):2026-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departments of Pharmacology and Cancer Biology and of Biochemistry, Duke University Medical Center, DUMC 3813, Durham, NC 27710, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10720331" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arginine/metabolism ; Cell Nucleus/enzymology/*metabolism ; DNA-Binding Proteins/metabolism ; *Gene Expression Regulation, Fungal ; Inositol 1,4,5-Trisphosphate/metabolism ; Inositol Phosphates/*metabolism ; Minichromosome Maintenance 1 Protein ; Molecular Sequence Data ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylation ; Phosphotransferases (Alcohol Group Acceptor)/chemistry/*metabolism ; Phytic Acid/metabolism ; Saccharomyces cerevisiae/enzymology/*genetics ; Signal Transduction ; Transcription Factors/metabolism ; *Transcription, Genetic ; Type C Phospholipases/metabolism
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  • 96
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    Long-term survival but impaired homeostatic proliferation of Naive T cells in the absence of p56lck (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-10-06
    Description: Interactions between the T cell receptor (TCR) and major histocompatibility complex antigens are essential for the survival and homeostasis of peripheral T lymphocytes. However, little is known about the TCR signaling events that result from these interactions. The peripheral T cell pool of p56lck (lck)-deficient mice was reconstituted by the expression of an inducible lck transgene. Continued survival of peripheral naive T cells was observed for long periods after switching off the transgene. Adoptive transfer of T cells from these mice into T lymphopoienic hosts confirmed that T cell survival was independent of lck but revealed its essential role in TCR-driven homeostatic proliferation of naive T cells in response to the T cell-deficient host environment. These data suggest that survival and homeostatic expansion depend on different signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Seddon, B -- Legname, G -- Tomlinson, P -- Zamoyska, R -- New York, N.Y. -- Science. 2000 Oct 6;290(5489):127-31.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Molecular Immunology, National Institute for Medical Research, The Ridgeway, Mill Hill, London NW7 1AA, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11021796" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, CD3/metabolism ; CD4-Positive T-Lymphocytes/immunology/physiology ; CD8-Positive T-Lymphocytes/immunology/physiology ; Cell Division ; Cell Survival ; Doxycycline/pharmacology ; Gene Expression ; Homeostasis ; Lymphocyte Activation ; Lymphocyte Count ; Lymphocyte Specific Protein Tyrosine Kinase p56(lck)/genetics/*physiology ; Lymphocyte Transfusion ; Lymphoid Tissue/cytology/immunology ; Mice ; Mice, Knockout ; Mice, Transgenic ; Phosphorylation ; Proto-Oncogene Proteins c-bcl-2/genetics/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocyte Subsets/immunology/physiology ; T-Lymphocytes/immunology/*physiology/transplantation ; Thymus Gland/cytology/immunology ; Transgenes
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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  • 97
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    A PEST-like sequence in listeriolysin O essential for Listeria monocytogenes pathogenicity (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-04
    Description: Establishment and maintenance of an intracellular niche are critical to the success of an intracellular pathogen. Here, the pore-forming protein listeriolysin O (LLO), secreted by Listeria monocytogenes, was shown to contain a PEST-like sequence (P, Pro; E, Glu; S, Ser; T, Thr) that is essential for the virulence and intracellular compartmentalization of this pathogen. Mutants lacking the PEST-like sequence entered the host cytosol but subsequently permeabilized and killed the host cell. LLO lacking the PEST-like sequence accumulated in the host-cell cytosol, suggesting that this sequence targets LLO for degradation. Transfer of the sequence to perfringolysin O transformed this toxic cytolysin into a nontoxic derivative that facilitated intracellular growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Decatur, A L -- Portnoy, D A -- AI10283/AI/NIAID NIH HHS/ -- AI27655/AI/NIAID NIH HHS/ -- R01 AI027655/AI/NIAID NIH HHS/ -- R37 AI029619/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2000 Nov 3;290(5493):992-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cell Biology, Division of Infectious Diseases, School of Public Health, University of California, Berkeley, CA 94720, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11062133" target="_blank"〉PubMed〈/a〉
    Keywords: Alleles ; Amino Acid Sequence ; Animals ; Bacterial Toxins/chemistry ; Cell Line ; Cytosol/metabolism ; Heat-Shock Proteins/*chemistry/genetics/*metabolism/toxicity ; Hemolysin Proteins ; L-Lactate Dehydrogenase/metabolism ; Listeria monocytogenes/genetics/metabolism/*pathogenicity ; Listeriosis/microbiology ; Macrophages/microbiology ; Mice ; Mice, Inbred BALB C ; Molecular Sequence Data ; Mutation ; Phagosomes/microbiology ; Phosphorylation ; Sequence Deletion ; Virulence
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 98
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    Driving AMPA receptors into synapses by LTP and CaMKII: requirement for GluR1 and PDZ domain interaction (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-03-24
    Description: To elucidate mechanisms that control and execute activity-dependent synaptic plasticity, alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate receptors (AMPA-Rs) with an electrophysiological tag were expressed in rat hippocampal neurons. Long-term potentiation (LTP) or increased activity of the calcium/calmodulin-dependent protein kinase II (CaMKII) induced delivery of tagged AMPA-Rs into synapses. This effect was not diminished by mutating the CaMKII phosphorylation site on the GluR1 AMPA-R subunit, but was blocked by mutating a predicted PDZ domain interaction site. These results show that LTP and CaMKII activity drive AMPA-Rs to synapses by a mechanism that requires the association between GluR1 and a PDZ domain protein.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hayashi, Y -- Shi, S H -- Esteban, J A -- Piccini, A -- Poncer, J C -- Malinow, R -- New York, N.Y. -- Science. 2000 Mar 24;287(5461):2262-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cold Spring Harbor Laboratory, Cold Spring Harbor, NY 11724, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/10731148" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/*metabolism ; Catalytic Domain ; Cell Line ; Hippocampus/cytology/metabolism ; Humans ; *Long-Term Potentiation ; Membrane Potentials ; Mutation ; Organ Culture Techniques ; Patch-Clamp Techniques ; Phosphorylation ; Protein Structure, Tertiary ; Proteins/*metabolism ; Pyramidal Cells/metabolism/*physiology ; Rats ; Receptors, AMPA/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Synapses/*metabolism ; Synaptic Transmission
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 99
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    Development. The path to the heart and the road not taken (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-03-28
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Olson, E N -- New York, N.Y. -- Science. 2001 Mar 23;291(5512):2327-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA. eolson@hamon.swmed.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11269304" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Blood Cells ; Bone Morphogenetic Proteins/metabolism ; Calcium-Calmodulin-Dependent Protein Kinases/metabolism ; Central Nervous System/embryology/metabolism ; Cytoskeletal Proteins/metabolism ; Drosophila/embryology/metabolism ; *Drosophila Proteins ; *Embryonic Induction ; Endoderm/physiology ; Gene Expression Regulation, Developmental ; Glycogen Synthase Kinase 3 ; Heart/*embryology ; Hematopoiesis ; Insect Proteins/metabolism ; Intercellular Signaling Peptides and Proteins ; Mesoderm/cytology/physiology ; Notochord/metabolism ; Phosphorylation ; Proteins/*metabolism ; Signal Transduction ; *Trans-Activators ; Transcription Factors/metabolism ; Vertebrates/embryology ; Wnt Proteins ; Wnt3 Protein ; *Xenopus Proteins ; Zebrafish Proteins ; beta Catenin
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 100
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    ATR and ATRIP: partners in checkpoint signaling (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-11-27
    Description: The checkpoint kinases ATM (ataxia telangiectasia mutated) and ATR (ATM and Rad3 related) transduce genomic stress signals to halt cell cycle progression and promote DNA repair. We report the identification of an ATR-interacting protein (ATRIP) that is phosphorylated by ATR, regulates ATR expression, and is an essential component of the DNA damage checkpoint pathway. ATR and ATRIP both localize to intranuclear foci after DNA damage or inhibition of replication. Deletion of ATR mediated by the Cre recombinase caused the loss of ATR and ATRIP expression, loss of DNA damage checkpoint responses, and cell death. Therefore, ATR is essential for the viability of human somatic cells. Small interfering RNA directed against ATRIP caused the loss of both ATRIP and ATR expression and the loss of checkpoint responses to DNA damage. Thus, ATRIP and ATR are mutually dependent partners in cell cycle checkpoint signaling pathways.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cortez, D -- Guntuku, S -- Qin, J -- Elledge, S J -- New York, N.Y. -- Science. 2001 Nov 23;294(5547):1713-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Verna and Mars McLean Department of Biochemistry and Molecular Biology, Howard Hughes Medical Institute, Baylor College of Medicine, One Baylor Plaza, Houston, TX 77030, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11721054" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Ataxia Telangiectasia Mutated Proteins ; *Cell Cycle ; *Cell Cycle Proteins ; Cell Death ; Cell Line ; Cell Survival ; Conserved Sequence ; DNA Damage ; DNA-Binding Proteins ; *Exodeoxyribonucleases ; Exons/genetics ; Gene Deletion ; Genes, Essential/genetics ; HeLa Cells ; Humans ; Integrases/genetics/metabolism ; Molecular Sequence Data ; Molecular Weight ; Phosphoproteins/genetics/*metabolism ; Phosphorylation ; Precipitin Tests ; Protein Binding ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Sequence Alignment ; *Signal Transduction ; Viral Proteins/genetics/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
    Published by American Association for the Advancement of Science (AAAS)
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