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  • Phosphorylation  (55)
  • American Association for the Advancement of Science (AAAS)  (55)
  • American Society of Hematology
  • Cell Press
  • EMBO Press
  • Essen : Verl. Glückauf
  • Krefeld : Geologischer Dienst Nordhein-Westfalen
  • 2005-2009  (55)
  • 2006  (55)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (55)
  • American Society of Hematology
  • Cell Press
  • EMBO Press
  • Essen : Verl. Glückauf
    • +
Years
  • 2005-2009  (55)
Year
  • 1
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    Sara endosomes and the maintenance of Dpp signaling levels across mitosis (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-18
    Description: During development, cells acquire positional information by reading the concentration of morphogens. In the developing fly wing, a gradient of the transforming growth factor-beta (TGF-beta)-type morphogen decapentaplegic (Dpp) is transduced into a gradient of concentration of the phosphorylated form of the R-Smad transcription factor Mad. The endosomal protein Sara (Smad anchor for receptor activation) recruits R-Smads for phosphorylation by the type I TGF-beta receptor. We found that Sara, Dpp, and its type I receptor Thickveins were targeted to a subpopulation of apical endosomes in the developing wing epithelial cells. During mitosis, the Sara endosomes and the receptors therein associated with the spindle machinery to segregate into the two daughter cells. Daughter cells thereby inherited equal amounts of signaling molecules and thus retained the Dpp signaling levels of the mother cell.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bokel, Christian -- Schwabedissen, Anja -- Entchev, Eugeni -- Renaud, Olivier -- Gonzalez-Gaitan, Marcos -- New York, N.Y. -- Science. 2006 Nov 17;314(5802):1135-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Max Planck Institute of Molecular Cell Biology and Genetics, Pfotenhauerstrasse 108, 01307 Dresden, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17110576" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Cell Division ; DNA-Binding Proteins/metabolism ; Drosophila Proteins/*metabolism ; Drosophila melanogaster/cytology/*metabolism ; Endosomes/*metabolism ; Epithelial Cells/cytology/metabolism ; *Mitosis ; Phosphorylation ; Point Mutation ; Protein-Serine-Threonine Kinases/metabolism ; Receptors, Cell Surface/metabolism ; *Signal Transduction ; Smad Proteins, Receptor-Regulated/metabolism ; Transcription Factors/metabolism ; Transforming Growth Factor beta/*metabolism ; Wings, Animal/cytology/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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  • 2
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    Molecular linkage between the kinase ATM and NF-kappaB signaling in response to genotoxic stimuli (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-02-25
    Description: The transcription factor NF-kappaB modulates apoptotic responses induced by genotoxic stress. We show that NF-kappaB essential modulator (NEMO), the regulatory subunit of IkappaB kinase (IKK) (which phosphorylates the NF-kappaB inhibitor IkappaB), associates with activated ataxia telangiectasia mutated (ATM) after the induction of DNA double-strand breaks. ATM phosphorylates serine-85 of NEMO to promote its ubiquitin-dependent nuclear export. ATM is also exported in a NEMO-dependent manner to the cytoplasm, where it associates with and causes the activation of IKK in a manner dependent on another IKK regulator, a protein rich in glutamate, leucine, lysine, and serine (ELKS). Thus, regulated nuclear shuttling of NEMO links two signaling kinases, ATM and IKK, to activate NF-kappaB by genotoxic signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wu, Zhao-Hui -- Shi, Yuling -- Tibbetts, Randal S -- Miyamoto, Shigeki -- R01-CA77474/CA/NCI NIH HHS/ -- R01-CA81065/CA/NCI NIH HHS/ -- R01-GM067868/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 24;311(5764):1141-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of Wisconsin-Madison, 301 SMI, 1300 University Avenue, Madison, WI 53706, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16497931" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Adaptor Proteins, Signal Transducing/genetics/metabolism ; Amino Acid Motifs ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins/*metabolism ; Cell Line ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; *DNA Damage ; DNA-Binding Proteins/*metabolism ; Humans ; I-kappa B Kinase/*metabolism ; I-kappa B Proteins/genetics/metabolism ; NF-kappa B/metabolism ; Nerve Tissue Proteins/genetics/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; SUMO-1 Protein/metabolism ; *Signal Transduction ; Tumor Suppressor Proteins/*metabolism ; Ubiquitin/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 signaling. A new way to burn fat (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neels, Jaap G -- Olefsky, Jerrold M -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1756-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Diego, 9500 Gilman Drive, La Jolla, CA 92093-0673, USA. jolefsky@ucsd.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794069" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl-CoA Carboxylase/antagonists & inhibitors/*metabolism ; Adipocytes/metabolism ; Adipose Tissue/*metabolism ; Animals ; Cell Cycle Proteins/*metabolism ; Energy Intake ; Energy Metabolism ; Enzyme Activation ; Fasting ; Fatty Acids/metabolism ; Hepatocytes/metabolism ; Insulin/physiology ; Insulin Resistance ; *Lipid Metabolism ; Lipogenesis ; Liver/metabolism ; Malonyl Coenzyme A/metabolism ; Mice ; Models, Biological ; Nuclear Proteins/*metabolism ; Obesity/therapy ; Oxidation-Reduction ; Phosphorylation ; Proto-Oncogene Proteins c-akt/antagonists & inhibitors/metabolism ; Signal Transduction ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/*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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  • 4
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    Transcription. Gene expression needs a break to unwind before carrying on (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-06-24
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Haince, Jean-Francois -- Rouleau, Michele -- Poirier, Guy G -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1752-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Health and Environment Unit, Faculty of Medicine, Laval University Medical Research Center, 2705 Boulevard Laurier, Quebec City, QC, G1V 4G2, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794066" target="_blank"〉PubMed〈/a〉
    Keywords: Chromatin/chemistry/metabolism ; DNA/*metabolism ; DNA Repair ; DNA Topoisomerases, Type II/*metabolism ; DNA-Activated Protein Kinase/metabolism ; DNA-Binding Proteins/antagonists & inhibitors/*metabolism ; Enzyme Activation ; Gene Expression ; Histones/metabolism ; Humans ; Models, Genetic ; Nucleosomes/metabolism ; Phosphorylation ; Poly Adenosine Diphosphate Ribose/metabolism ; Poly(ADP-ribose) Polymerases/*metabolism ; Response Elements ; Topoisomerase II Inhibitors ; Transcription Factors/metabolism ; *Transcription, Genetic ; *Transcriptional Activation
    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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  • 5
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    ATM engages autodegradation of the E3 ubiquitin ligase COP1 after DNA damage (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-26
    Description: The ataxia telangiectasia mutated (ATM) protein kinase is a critical component of a DNA-damage response network configured to maintain genomic integrity. The abundance of an essential downstream effecter of this pathway, the tumor suppressor protein p53, is tightly regulated by controlled degradation through COP1 and other E3 ubiquitin ligases, such as MDM2 and Pirh2; however, the signal transduction pathway that regulates the COP1-p53 axis following DNA damage remains enigmatic. We observed that in response to DNA damage, ATM phosphorylated COP1 on Ser(387) and stimulated a rapid autodegradation mechanism. Ionizing radiation triggered an ATM-dependent movement of COP1 from the nucleus to the cytoplasm, and ATM-dependent phosphorylation of COP1 on Ser(387) was both necessary and sufficient to disrupt the COP1-p53 complex and subsequently to abrogate the ubiquitination and degradation of p53. Furthermore, phosphorylation of COP1 on Ser(387) was required to permit p53 to become stabilized and to exert its tumor suppressor properties in response to DNA damage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dornan, David -- Shimizu, Harumi -- Mah, Angie -- Dudhela, Tanay -- Eby, Michael -- O'rourke, Karen -- Seshagiri, Somasekar -- Dixit, Vishva M -- New York, N.Y. -- Science. 2006 Aug 25;313(5790):1122-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiological Chemistry, Genentech, Inc., 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/16931761" target="_blank"〉PubMed〈/a〉
    Keywords: Ataxia Telangiectasia Mutated Proteins ; Cell Cycle Proteins/genetics/*metabolism ; Cell Line ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Cytoplasm/metabolism ; *DNA Damage ; DNA-Binding Proteins/genetics/*metabolism ; Escherichia coli/genetics/metabolism ; Etoposide/pharmacology ; Humans ; Mutation ; Nuclear Proteins/genetics/*metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Proteasome Endopeptidase Complex/metabolism ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; RNA, Small Interfering ; Radiation, Ionizing ; Recombinant Fusion Proteins/metabolism ; Transfection ; Tumor Suppressor Protein p53/genetics/metabolism ; Tumor Suppressor Proteins/genetics/*metabolism ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/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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  • 6
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    S6K1- and betaTRCP-mediated degradation of PDCD4 promotes protein translation and cell growth (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-21
    Description: The tumor suppressor programmed cell death protein 4 (PDCD4) inhibits the translation initiation factor eIF4A, an RNA helicase that catalyzes the unwinding of secondary structure at the 5' untranslated region (5'UTR) of messenger RNAs (mRNAs). In response to mitogens, PDCD4 was rapidly phosphorylated on Ser67 by the protein kinase S6K1 and subsequently degraded via the ubiquitin ligase SCF(betaTRCP). Expression in cultured cells of a stable PDCD4 mutant that is unable to bind betaTRCP inhibited translation of an mRNA with a structured 5'UTR, resulted in smaller cell size, and slowed down cell cycle progression. We propose that regulated degradation of PDCD4 in response to mitogens allows efficient protein synthesis and consequently cell growth.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dorrello, N Valerio -- Peschiaroli, Angelo -- Guardavaccaro, Daniele -- Colburn, Nancy H -- Sherman, Nicholas E -- Pagano, Michele -- R01-CA76584/CA/NCI NIH HHS/ -- R01-GM57587/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):467-71.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, NYU Cancer Institute, New York University School of Medicine, 550 First Avenue, MSB 599, New York, NY 10016, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053147" target="_blank"〉PubMed〈/a〉
    Keywords: 5' Untranslated Regions ; Amino Acid Motifs ; Apoptosis Regulatory Proteins/chemistry/genetics/*metabolism ; Binding Sites ; Cell Line ; Cell Line, Tumor ; *Cell Proliferation ; Cell Size ; Eukaryotic Initiation Factor-4A/antagonists & inhibitors/metabolism ; Eukaryotic Initiation Factor-4F/metabolism ; Eukaryotic Initiation Factor-4G/metabolism ; Eukaryotic Initiation Factors/metabolism ; Humans ; Mitogens/pharmacology ; Phosphorylation ; *Protein Biosynthesis ; RNA, Small Interfering ; RNA-Binding Proteins/chemistry/genetics/*metabolism ; Ribosomal Protein S6 Kinases/metabolism ; SKP Cullin F-Box Protein Ligases/*metabolism ; Serine/metabolism ; Serum ; Signal Transduction ; beta-Transducin Repeat-Containing Proteins/genetics/*metabolism
    Print ISSN: 0036-8075
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  • 7
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    Cytokinin signaling and its inhibitor AHP6 regulate cell fate during vascular development (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-01-10
    Description: The cell lineages that form the transporting tissues (xylem and phloem) and the intervening pluripotent procambial tissue originate from stem cells near the root tip. We demonstrate that in Arabidopsis, cytokinin phytohormones negatively regulate protoxylem specification. AHP6, an inhibitory pseudophosphotransfer protein, counteracts cytokinin signaling, allowing protoxylem formation. Conversely, cytokinin signaling negatively regulates the spatial domain of AHP6 expression. Thus, by controlling the identity of cell lineages, the reciprocal interaction of cytokinin signaling and its spatially specific modulator regulates proliferation and differentiation of cell lineages during vascular development, demonstrating a previously unrecognized regulatory circuit underlying meristem organization.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mahonen, Ari Pekka -- Bishopp, Anthony -- Higuchi, Masayuki -- Nieminen, Kaisa M -- Kinoshita, Kaori -- Tormakangas, Kirsi -- Ikeda, Yoshihisa -- Oka, Atsuhiro -- Kakimoto, Tatsuo -- Helariutta, Yka -- New York, N.Y. -- Science. 2006 Jan 6;311(5757):94-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Molecular Biology Laboratory, Institute of Biotechnology, POB 56, FI-00014, University of Helsinki, Finland.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16400151" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Alleles ; Arabidopsis/*cytology/genetics/growth & development/*metabolism ; Arabidopsis Proteins/genetics/*metabolism/physiology ; Cell Differentiation ; Cell Division ; Cell Lineage ; Cloning, Molecular ; Cytokinins/*metabolism ; Genes, Plant ; Kinetin/metabolism/pharmacology ; Meristem/cytology/growth & development/metabolism ; Morphogenesis ; Phenotype ; Phosphorylation ; Plant Growth Regulators/*metabolism ; Plant Roots/*cytology/growth & development/metabolism ; Plant Shoots/metabolism ; Plants, Genetically Modified ; *Signal Transduction ; Suppression, Genetic ; Zeatin/metabolism/pharmacology
    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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    Escherichia coli induces DNA double-strand breaks in eukaryotic cells (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-12
    Description: Transient infection of eukaryotic cells with commensal and extraintestinal pathogenic Escherichia coli of phylogenetic group B2 blocks mitosis and induces megalocytosis. This trait is linked to a widely spread genomic island that encodes giant modular nonribosomal peptide and polyketide synthases. Contact with E. coli expressing this gene cluster causes DNA double-strand breaks and activation of the DNA damage checkpoint pathway, leading to cell cycle arrest and eventually to cell death. Discovery of hybrid peptide-polyketide genotoxins in E. coli will change our view on pathogenesis and commensalism and open new biotechnological applications.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nougayrede, Jean-Philippe -- Homburg, Stefan -- Taieb, Frederic -- Boury, Michele -- Brzuszkiewicz, Elzbieta -- Gottschalk, Gerhard -- Buchrieser, Carmen -- Hacker, Jorg -- Dobrindt, Ulrich -- Oswald, Eric -- New York, N.Y. -- Science. 2006 Aug 11;313(5788):848-51.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉INRA, UMR1225, Ecole Nationale Veterinaire de Toulouse, Toulouse F-31076, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16902142" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Ataxia Telangiectasia Mutated Proteins ; Cell Cycle ; Cell Cycle Proteins/metabolism ; Cell Death ; Cell Line ; Cell Nucleus/chemistry ; Cytotoxins/*metabolism ; DNA/analysis ; *DNA Damage ; DNA-Binding Proteins/metabolism ; Escherichia coli/genetics/*pathogenicity/*physiology ; G2 Phase ; *Genomic Islands ; HeLa Cells ; Histones/metabolism ; Humans ; Intestinal Mucosa/cytology/microbiology ; Molecular Sequence Data ; Mutagenesis ; Mutagens/*metabolism ; Peptides/*metabolism ; Phosphorylation ; Polyketide Synthases/genetics ; Protein-Serine-Threonine Kinases/metabolism ; Rats ; Signal Transduction ; Tumor Suppressor 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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  • 9
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    Cell biology. Balancing life-or-death decisions (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bartek, Jiri -- Lukas, Jiri -- New York, N.Y. -- Science. 2006 Oct 13;314(5797):261-2.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Cancer Biology and Centre for Genotoxic Stress Research, Danish Cancer Society, Strandboulevarden 49, DK-2100 Copenhagen, Denmark. jb@cancer.dk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038611" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; BRCA2 Protein/metabolism ; Cell Cycle ; Cell Nucleus/metabolism ; Cell Survival ; Cyclin-Dependent Kinase 2/antagonists & inhibitors/*metabolism ; *DNA Damage ; DNA Repair ; DNA Replication ; Forkhead Transcription Factors/*metabolism ; Gene Expression Regulation ; Humans ; Mice ; Models, Biological ; Phosphorylation ; RNA, Small Interfering ; Transcription, Genetic ; cdc25 Phosphatases/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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  • 10
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    Anaphase inactivation of the spindle checkpoint (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-11
    Description: The spindle checkpoint delays cell cycle progression until microtubules attach each pair of sister chromosomes to opposite poles of the mitotic spindle. Following sister chromatid separation, however, the checkpoint ignores chromosomes whose kinetochores are attached to only one spindle pole, a state that activates the checkpoint prior to metaphase. We demonstrate that, in budding yeast, mutual inhibition between the anaphase-promoting complex (APC) and Mps1, an essential component of the checkpoint, leads to sustained inactivation of the spindle checkpoint. Mps1 protein abundance decreases in anaphase, and Mps1 is a target of the APC. Furthermore, expression of Mps1 in anaphase, or repression of the APC in anaphase, reactivates the spindle checkpoint. This APC-Mps1 feedback circuit allows cells to irreversibly inactivate the checkpoint during anaphase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Palframan, William J -- Meehl, Janet B -- Jaspersen, Sue L -- Winey, Mark -- Murray, Andrew W -- GM43987/GM/NIGMS NIH HHS/ -- GM51312/GM/NIGMS NIH HHS/ -- R37 GM043987/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):680-4. Epub 2006 Jul 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Biological Laboratories, Harvard University, 16 Divinity Avenue, Cambridge, MA 02138, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16825537" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Anaphase/*physiology ; Anaphase-Promoting Complex-Cyclosome ; Cdc20 Proteins ; Cell Cycle Proteins/metabolism ; Chromosomes, Fungal/physiology ; Feedback, Physiological ; GTP-Binding Proteins/metabolism ; Kinetochores/physiology ; Mad2 Proteins ; Mitosis ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/genetics/*metabolism ; Protein-Tyrosine Kinases/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*cytology/metabolism ; Saccharomyces cerevisiae Proteins/genetics/*metabolism ; Securin ; Spindle Apparatus/*physiology ; Ubiquitin-Protein Ligase Complexes/*metabolism
    Print ISSN: 0036-8075
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  • 11
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    Caveolin-1 is essential for liver regeneration (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-09-16
    Description: Liver regeneration is an orchestrated cellular response that coordinates cell activation, lipid metabolism, and cell division. We found that caveolin-1 gene-disrupted mice (cav1-/- mice) exhibited impaired liver regeneration and low survival after a partial hepatectomy. Hepatocytes showed dramatically reduced lipid droplet accumulation and did not advance through the cell division cycle. Treatment of cav1-/- mice with glucose (which is a predominant energy substrate when compared to lipids) drastically increased survival and reestablished progression of the cell cycle. Thus, caveolin-1 plays a crucial role in the mechanisms that coordinate lipid metabolism with the proliferative response occurring in the liver after cellular injury.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fernandez, Manuel A -- Albor, Cecilia -- Ingelmo-Torres, Mercedes -- Nixon, Susan J -- Ferguson, Charles -- Kurzchalia, Teymuras -- Tebar, Francesc -- Enrich, Carlos -- Parton, Robert G -- Pol, Albert -- New York, N.Y. -- Science. 2006 Sep 15;313(5793):1628-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Departament de Biologia Cellular, Facultat de Medicina, Institut d'Investigacions Biomediques August Pi i Sunyer, Universitat de Barcelona, Casanova 143, 08036 Barcelona, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16973879" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Caveolae/metabolism ; Caveolin 1/genetics/*physiology ; Cell Cycle ; Cell Division ; Fatty Acids/blood/metabolism ; Glucose/administration & dosage ; Hepatectomy ; Hepatocyte Growth Factor/metabolism ; Hepatocytes/cytology/*metabolism ; *Lipid Metabolism ; Lipids/blood ; Liver/metabolism/ultrastructure ; *Liver Regeneration ; Male ; Mice ; Phosphorylation ; RNA, Small Interfering ; STAT3 Transcription Factor/metabolism ; Signal Transduction ; Triglycerides/blood/metabolism
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  • 12
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    CDK2-dependent phosphorylation of FOXO1 as an apoptotic response to DNA damage (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-14
    Description: The function of cyclin-dependent kinase 2 (CDK2) is often abolished after DNA damage. The inhibition of CDK2 plays a central role in DNA damage-induced cell cycle arrest and DNA repair. However, whether CDK2 also influences the survival of cells under genotoxic stress is unknown. Forkhead box O (FOXO) transcription factors are emerging as key regulators of cell survival. CDK2 specifically phosphorylated FOXO1 at serine-249 (Ser249) in vitro and in vivo. Phosphorylation of Ser249 resulted in cytoplasmic localization and inhibition of FOXO1. This phosphorylation was abrogated upon DNA damage through the cell cycle checkpoint pathway that is dependent on the protein kinases Chk1 and Chk2. Moreover, silencing of FOXO1 by small interfering RNA diminished DNA damage-induced death in both p53-deficient and p53-proficient cells. This effect was reversed by restored expression of FOXO1 in a manner depending on phosphorylation of Ser249. Functional interaction between CDK2 and FOXO1 provides a mechanism that regulates apoptotic cell death after DNA strand breakage.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Huang, Haojie -- Regan, Kevin M -- Lou, Zhenkun -- Chen, Junjie -- Tindall, Donald J -- CA91956/CA/NCI NIH HHS/ -- DK60920/DK/NIDDK NIH HHS/ -- DK65236/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 13;314(5797):294-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Molecular Biology, Mayo Clinic College of Medicine, Rochester, MN 55905, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038621" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Apoptosis ; Camptothecin/pharmacology ; Cell Line, Tumor ; Cell Nucleus/metabolism ; Checkpoint Kinase 2 ; Cyclin-Dependent Kinase 2/antagonists & inhibitors/genetics/*metabolism ; Cytoplasm/metabolism ; *DNA Damage ; Forkhead Transcription Factors/antagonists & inhibitors/*metabolism ; Humans ; Mice ; Phosphorylation ; Phosphoserine/metabolism ; Protein Kinases/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; RNA, Small Interfering ; Recombinant Fusion Proteins/metabolism ; Signal Transduction ; Transcription, Genetic ; Transfection ; Tumor Suppressor Protein p53/metabolism
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  • 13
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    A positive feedback loop promotes transcription surge that jump-starts Salmonella virulence circuit (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-12-13
    Description: The PhoP/PhoQ two-component system is a master regulator of Salmonella pathogenicity. Here we report that induction of the PhoP/PhoQ system results in an initial surge of PhoP phosphorylation; the occupancy of target promoters by the PhoP protein; and the transcription of PhoP-activated genes, which then subsides to reach new steady-state levels. This surge in PhoP activity is due to PhoP positively activating its own transcription, because a strain constitutively expressing the PhoP protein attained steady-state levels of activation asymptotically, without the surge. The strain constitutively expressing the PhoP protein was attenuated for virulence in mice, demonstrating that the surge conferred by PhoP's positive feedback loop is necessary to jump-start Salmonella's virulence program.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shin, Dongwoo -- Lee, Eun-Jin -- Huang, Henry -- Groisman, Eduardo A -- AI49561/AI/NIAID NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1607-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Microbiology, Howard Hughes Medical Institute, Washington University School of Medicine, Campus Box 8230, 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/17158330" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Bacterial Proteins/*genetics/*metabolism ; *Feedback, Physiological ; Gene Expression Regulation, Bacterial ; Magnesium/metabolism ; Mice ; Phosphorylation ; Promoter Regions, Genetic ; RNA, Bacterial/genetics/metabolism ; RNA, Messenger/genetics/metabolism ; Salmonella Infections, Animal/microbiology ; Salmonella typhimurium/*genetics/metabolism/*pathogenicity ; *Transcription, Genetic ; Virulence
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  • 14
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    Activity-dependent regulation of MEF2 transcription factors suppresses excitatory synapse number (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-02-18
    Description: In the mammalian nervous system, neuronal activity regulates the strength and number of synapses formed. The genetic program that coordinates this process is poorly understood. We show that myocyte enhancer factor 2 (MEF2) transcription factors suppressed excitatory synapse number in a neuronal activity- and calcineurin-dependent manner as hippocampal neurons formed synapses. In response to increased neuronal activity, calcium influx into neurons induced the activation of the calcium/calmodulin-regulated phosphatase calcineurin, which dephosphorylated and activated MEF2. When activated, MEF2 promoted the transcription of a set of genes, including arc and synGAP, that restrict synapse number. These findings define an activity-dependent transcriptional program that may control synapse number during development.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Flavell, Steven W -- Cowan, Christopher W -- Kim, Tae-Kyung -- Greer, Paul L -- Lin, Yingxi -- Paradis, Suzanne -- Griffith, Eric C -- Hu, Linda S -- Chen, Chinfei -- Greenberg, Michael E -- AG05870/AG/NIA NIH HHS/ -- HD18655/HD/NICHD NIH HHS/ -- NS28829/NS/NINDS NIH HHS/ -- R01 EY013613/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 17;311(5763):1008-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Neurobiology Program, Children's Hospital, and Departments of Neurology and Neurobiology, 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/16484497" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcineurin/metabolism ; Calcium/metabolism ; Cells, Cultured ; Cytoskeletal Proteins/genetics ; Dendrites/physiology/ultrastructure ; Excitatory Postsynaptic Potentials ; GTPase-Activating Proteins/genetics ; Gene Expression Regulation ; Glutamic Acid/metabolism ; Hippocampus/cytology/*physiology ; MEF2 Transcription Factors ; Mutation ; Myogenic Regulatory Factors/genetics/*physiology ; Nerve Tissue Proteins/genetics ; Neurons/*physiology ; Oligonucleotide Array Sequence Analysis ; Phosphorylation ; RNA Interference ; Rats ; Rats, Long-Evans ; Recombinant Fusion Proteins/metabolism ; Synapses/*physiology ; Synaptic Transmission ; Transcription, Genetic ; Transfection
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  • 15
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    Protrudin induces neurite formation by directional membrane trafficking (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-11-04
    Description: Guanosine triphosphatases of the Rab family are key regulators of membrane trafficking, with Rab11 playing a specific role in membrane recycling. We identified a mammalian protein, protrudin, that promoted neurite formation through interaction with the guanosine diphosphate (GDP)-bound form of Rab11. Phosphorylation of protrudin by extracellular signal-regulated kinase (ERK) in response to nerve growth factor promoted protrudin association with Rab11-GDP. Down-regulation of protrudin by RNA interference induced membrane extension in all directions and inhibited neurite formation. Thus, protrudin regulates Rab11-dependent membrane recycling to promote the directional membrane trafficking required for neurite formation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shirane, Michiko -- Nakayama, Keiichi I -- New York, N.Y. -- Science. 2006 Nov 3;314(5800):818-21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Cellular Biology, Medical Institute of Bioregulation, Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, Fukuoka 812-8582, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17082457" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Carrier Proteins/chemistry/genetics/*metabolism ; Cell Adhesion Molecules/metabolism ; Cell Line ; Cell Membrane/*metabolism ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Guanosine Diphosphate/metabolism ; HeLa Cells ; Humans ; MAP Kinase Kinase 1/metabolism ; Membrane Proteins ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Nerve Growth Factor/pharmacology/physiology ; Neurites/*physiology ; PC12 Cells ; Phosphorylation ; RNA Interference ; Rats ; Recombinant Fusion Proteins/chemistry/metabolism ; Vesicular Transport Proteins ; rab GTP-Binding Proteins/metabolism
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  • 16
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    The Neurospora checkpoint kinase 2: a regulatory link between the circadian and cell cycles (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-01
    Description: The clock gene period-4 (prd-4) in Neurospora was identified by a single allele displaying shortened circadian period and altered temperature compensation. Positional cloning followed by functional tests show that PRD-4 is an ortholog of mammalian checkpoint kinase 2 (Chk2). Expression of prd-4 is regulated by the circadian clock and, reciprocally, PRD-4 physically interacts with the clock component FRQ, promoting its phosphorylation. DNA-damaging agents can reset the clock in a manner that depends on time of day, and this resetting is dependent on PRD-4. Thus, prd-4, the Neurospora Chk2, identifies a molecular link that feeds back conditionally from circadian output to input and the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pregueiro, Antonio M -- Liu, Qiuyun -- Baker, Christopher L -- Dunlap, Jay C -- Loros, Jennifer J -- MH44651/MH/NIMH NIH HHS/ -- P01 GM068087/GM/NIGMS NIH HHS/ -- R01 GM034985/GM/NIGMS NIH HHS/ -- R37GM34985/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 4;313(5787):644-9. Epub 2006 Jun 29.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics, Dartmouth Medical School, Hanover, NH 03755, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809488" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; *Cell Cycle ; Checkpoint Kinase 2 ; *Circadian Rhythm ; Cloning, Molecular ; DNA Damage ; Feedback, Physiological ; Fungal Proteins/chemistry/genetics/metabolism ; Gene Expression Regulation, Fungal ; Genes, Fungal ; Methyl Methanesulfonate/pharmacology ; Molecular Sequence Data ; Mutation ; Neurospora/*enzymology/genetics ; Neurospora crassa/cytology/*enzymology/*physiology ; Phosphorylation ; Protein-Serine-Threonine Kinases/chemistry/*genetics/*metabolism
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  • 17
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    Signal transduction. Protein synthesis and oncogenesis meet again (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-10-21
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Sonenberg, Nahum -- Pause, Arnim -- New York, N.Y. -- Science. 2006 Oct 20;314(5798):428-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and McGill Cancer Centre, McGill University, 3655 Promenade Sir William Osler, Montreal, Quebec, Canada H3G 1Y6. nahum.sonenberg@mcgill.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17053135" target="_blank"〉PubMed〈/a〉
    Keywords: Apoptosis Regulatory Proteins/*metabolism ; *Cell Proliferation ; Eukaryotic Initiation Factor-4A/antagonists & inhibitors/metabolism ; Eukaryotic Initiation Factor-4F/metabolism ; Humans ; Neoplasms/pathology/*physiopathology ; Phosphorylation ; *Protein Biosynthesis ; Protein Kinases/metabolism ; RNA Caps/metabolism ; RNA-Binding Proteins/*metabolism ; Repressor Proteins/metabolism ; Ribosomal Protein S6 Kinases/metabolism ; SKP Cullin F-Box Protein Ligases/metabolism ; *Signal Transduction ; TOR Serine-Threonine Kinases ; Ubiquitin-Protein Ligases/metabolism ; beta-Transducin Repeat-Containing Proteins/metabolism
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  • 18
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    Hypothalamic mTOR signaling regulates food intake (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-05-13
    Description: The mammalian Target of Rapamycin (mTOR) protein is a serine-threonine kinase that regulates cell-cycle progression and growth by sensing changes in energy status. We demonstrated that mTOR signaling plays a role in the brain mechanisms that respond to nutrient availability, regulating energy balance. In the rat, mTOR signaling is controlled by energy status in specific regions of the hypothalamus and colocalizes with neuropeptide Y and proopiomelanocortin neurons in the arcuate nucleus. Central administration of leucine increases hypothalamic mTOR signaling and decreases food intake and body weight. The hormone leptin increases hypothalamic mTOR activity, and the inhibition of mTOR signaling blunts leptin's anorectic effect. Thus, mTOR is a cellular fuel sensor whose hypothalamic activity is directly tied to the regulation of energy intake.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Cota, Daniela -- Proulx, Karine -- Smith, Kathi A Blake -- Kozma, Sara C -- Thomas, George -- Woods, Stephen C -- Seeley, Randy J -- DK 17844/DK/NIDDK NIH HHS/ -- DK 54080/DK/NIDDK NIH HHS/ -- DK 54890/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 May 12;312(5775):927-30.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Psychiatry, University of Cincinnati, Genome Research Institute, 2170 East Galbraith Road, Cincinnati, OH 45237, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16690869" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arcuate Nucleus of Hypothalamus/cytology/enzymology/metabolism ; *Eating ; *Energy Intake ; *Energy Metabolism ; Fasting ; Hypothalamus/enzymology/*metabolism ; Injections, Intraventricular ; Leptin/pharmacology ; Leucine/*administration & dosage/pharmacology ; Neurons/enzymology/*metabolism ; Neuropeptide Y/genetics/metabolism ; Phosphorylation ; Protein Kinases/*metabolism ; Rats ; Rats, Long-Evans ; Ribosomal Protein S6/metabolism ; Ribosomal Protein S6 Kinases/metabolism ; STAT3 Transcription Factor/metabolism ; *Signal Transduction ; Sirolimus/administration & dosage/pharmacology ; TOR Serine-Threonine Kinases ; Valine/administration & dosage/pharmacology ; Weight Loss
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  • 19
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    Virology. Sensing viral RNA amid your own (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-11-11
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Fujita, Takashi -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):935-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Genetics, Institute for Virus Research, Kyoto University, Kyoto 606- 8507, Japan. tfujita@virus.kyoto-u.ac.jp〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17095686" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Cytoplasm/metabolism/virology ; DEAD-box RNA Helicases/chemistry/*metabolism ; Humans ; Immunity, Innate ; Interferons/biosynthesis ; Nucleic Acid Conformation ; Phosphates/metabolism ; Phosphorylation ; RNA Caps/metabolism ; RNA, Double-Stranded/chemistry/metabolism ; RNA, Viral/chemistry/*metabolism ; Signal Transduction ; Toll-Like Receptors/metabolism ; Viral Nonstructural Proteins/metabolism ; Virus Diseases/immunology
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  • 20
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    Learning induces long-term potentiation in the hippocampus (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-08-26
    Description: Years of intensive investigation have yielded a sophisticated understanding of long-term potentiation (LTP) induced in hippocampal area CA1 by high-frequency stimulation (HFS). These efforts have been motivated by the belief that similar synaptic modifications occur during memory formation, but it has never been shown that learning actually induces LTP in CA1. We found that one-trial inhibitory avoidance learning in rats produced the same changes in hippocampal glutamate receptors as induction of LTP with HFS and caused a spatially restricted increase in the amplitude of evoked synaptic transmission in CA1 in vivo. Because the learning-induced synaptic potentiation occluded HFS-induced LTP, we conclude that inhibitory avoidance training induces LTP in CA1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Whitlock, Jonathan R -- Heynen, Arnold J -- Shuler, Marshall G -- Bear, Mark F -- New York, N.Y. -- Science. 2006 Aug 25;313(5790):1093-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Picower Institute for Learning and Memory, Department of Brain and Cognitive Sciences, Massachusetts Institute of Technology, Cambridge, MA 02139, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16931756" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/*physiology ; Conditioning (Psychology) ; Electric Stimulation ; Electrodes, Implanted ; Excitatory Postsynaptic Potentials ; Hippocampus/*physiology ; Long-Term Potentiation/*physiology ; Male ; Memory/*physiology ; Phosphorylation ; Phosphoserine/metabolism ; Rats ; Rats, Long-Evans ; Receptors, AMPA/metabolism ; Synapses/metabolism/*physiology ; Synaptic Transmission
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  • 21
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    Yersinia YopJ acetylates and inhibits kinase activation by blocking phosphorylation (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-05-27
    Description: Yersinia species use a variety of type III effector proteins to target eukaryotic signaling systems. The effector YopJ inhibits mitogen-activated protein kinase (MAPK) and the nuclear factor kappaB (NFkappaB) signaling pathways used in innate immune response by preventing activation of the family of MAPK kinases (MAPKK). We show that YopJ acted as an acetyltransferase, using acetyl-coenzyme A (CoA) to modify the critical serine and threonine residues in the activation loop of MAPKK6 and thereby blocking phosphorylation. The acetylation on MAPKK6 directly competed with phosphorylation, preventing activation of the modified protein. This covalent modification may be used as a general regulatory mechanism in biological signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mukherjee, Sohini -- Keitany, Gladys -- Li, Yan -- Wang, Yong -- Ball, Haydn L -- Goldsmith, Elizabeth J -- Orth, Kim -- R01-AI056404/AI/NIAID NIH HHS/ -- R21-DK072134/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 May 26;312(5777):1211-4.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology, University of Texas Southwestern Medical Center, Dallas, TX 75390, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16728640" target="_blank"〉PubMed〈/a〉
    Keywords: Acetyl Coenzyme A/metabolism ; Acetylation ; Acetyltransferases/metabolism ; Bacterial Proteins/*metabolism ; Catalytic Domain ; Cell Line ; Cell-Free System ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Humans ; I-kappa B Kinase/*metabolism ; MAP Kinase Kinase 6/chemistry/*metabolism ; MAP Kinase Signaling System ; NF-kappa B/metabolism ; Phosphorylation ; Recombinant Proteins/metabolism ; Serine/metabolism ; Signal Transduction ; Threonine/metabolism ; Yersinia/*metabolism/pathogenicity
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  • 22
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    Brassinosteroids regulate dissociation of BKI1, a negative regulator of BRI1 signaling, from the plasma membrane (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-07-22
    Description: Brassinosteroids, the steroid hormones of plants, are perceived at the plasma membrane by a leucine-rich repeat receptor serine/threonine kinase called BRI1. We report a BRI1-interacting protein, BKI1, which is a negative regulator of brassinosteroid signaling. Brassinosteroids cause the rapid dissociation of BKI1-yellow fluorescent protein from the plasma membrane in a process that is dependent on BRI1-kinase. BKI1 is a substrate of BRI1 kinase and limits the interaction of BRI1 with its proposed coreceptor, BAK1, suggesting that BKI1 prevents the activation of BRI1.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Wang, Xuelu -- Chory, Joanne -- New York, N.Y. -- Science. 2006 Aug 25;313(5790):1118-22. Epub 2006 Jul 20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute and Plant Biology Laboratory, Salk Institute for Biological Studies, 10010 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/16857903" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*metabolism ; Arabidopsis Proteins/chemistry/genetics/*metabolism ; Brassinosteroids ; Cell Membrane/*metabolism ; Cholestanols/*metabolism/pharmacology ; Gene Expression Regulation, Plant ; Meristem/metabolism ; Molecular Sequence Data ; Nuclear Proteins/metabolism ; Phosphorylation ; Plants, Genetically Modified ; Protein Binding ; Protein Kinases/chemistry/genetics/*metabolism ; Protein Structure, Tertiary ; RNA Interference ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Steroids, Heterocyclic/*metabolism/pharmacology ; Two-Hybrid System Techniques
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  • 23
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    TRB3 links the E3 ubiquitin ligase COP1 to lipid metabolism (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-06-24
    Description: During fasting, increased concentrations of circulating catecholamines promote the mobilization of lipid stores from adipose tissue in part by phosphorylating and inactivating acetyl-coenzyme A carboxylase (ACC), the rate-limiting enzyme in fatty acid synthesis. Here, we describe a parallel pathway, in which the pseudokinase Tribbles 3 (TRB3), whose abundance is increased during fasting, stimulates lipolysis by triggering the degradation of ACC in adipose tissue. TRB3 promoted ACC ubiquitination through an association with the E3 ubiquitin ligase constitutive photomorphogenic protein 1 (COP1). Indeed, adipocytes deficient in TRB3 accumulated larger amounts of ACC protein than did wild-type cells. Because transgenic mice expressing TRB3 in adipose tissue are protected from diet-induced obesity due to enhanced fatty acid oxidation, these results demonstrate how phosphorylation and ubiquitination pathways converge on a key regulator of lipid metabolism to maintain energy homeostasis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Qi, Ling -- Heredia, Jose E -- Altarejos, Judith Y -- Screaton, Robert -- Goebel, Naomi -- Niessen, Sherry -- Macleod, Ian X -- Liew, Chong Wee -- Kulkarni, Rohit N -- Bain, James -- Newgard, Christopher -- Nelson, Michael -- Evans, Ronald M -- Yates, John -- Montminy, Marc -- DK064142/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1763-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Peptide Biology Laboratories and Gene Expression Laboratories, Salk Institute for Biological Studies, La Jolla, CA 92037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794074" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3-L1 Cells ; Acetyl-CoA Carboxylase/antagonists & inhibitors/*metabolism ; Adipocytes/metabolism ; Adipose Tissue/cytology/*metabolism ; Adipose Tissue, Brown/cytology/metabolism ; Animals ; Cell Cycle Proteins/*metabolism ; Cell Line ; Dietary Fats/administration & dosage ; Energy Metabolism ; Fasting ; Fatty Acids/metabolism ; Gene Expression ; Humans ; *Lipid Metabolism ; Lipolysis ; Mice ; Mice, Transgenic ; Nuclear Proteins/*metabolism ; Obesity/prevention & control ; Oxidation-Reduction ; Phosphorylation ; Thinness ; Ubiquitin/metabolism ; Ubiquitin-Protein Ligases/*metabolism ; Weight Gain
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  • 24
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    Chemical rescue of a mutant enzyme in living cells (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-03-04
    Description: The restoration of catalytic activity to mutant enzymes by small molecules is well established for in vitro systems. Here, we show that the protein tyrosine kinase Src arginine-388--〉alanine (R388A) mutant can be rescued in live cells with the use of the small molecule imidazole. Cellular rescue of a viral Src homolog was rapid and reversible and conferred predicted oncogenic properties. Using chemical rescue in combination with mass spectrometry, we confirmed six known Src kinase substrates and identified several new protein targets. Chemical rescue data suggest that cellular Src is active under basal conditions. Rescue of R388A cellular Src provided insights into the mitogen-activated protein kinase pathway. This chemical rescue approach will likely have many applications in cell signaling.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Qiao, Yingfeng -- Molina, Henrik -- Pandey, Akhilesh -- Zhang, Jin -- Cole, Philip A -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1293-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology and Molecular Sciences, 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/16513984" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/metabolism ; Animals ; Cell Line ; Cell Transformation, Neoplastic ; Fluorescence Resonance Energy Transfer ; Gene Expression Profiling ; Gene Expression Regulation ; Growth Substances/metabolism/pharmacology ; Humans ; Imidazoles/*metabolism/pharmacology ; Kinetics ; Mice ; Mitogen-Activated Protein Kinases/metabolism ; Mutation ; Nuclear Proteins/metabolism ; Oligonucleotide Array Sequence Analysis ; Phenotype ; Phosphorylation ; Phosphotyrosine/metabolism ; Proto-Oncogene Proteins/metabolism ; Proto-Oncogene Proteins pp60(c-src)/*genetics/*metabolism ; Recombinant Proteins/metabolism ; Transfection ; src Homology Domains
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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    Molecular biology. Accurate RNA siting and splicing gets help from a DEK-hand (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kress, Tracy L -- Guthrie, Christine -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1886-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143-0448, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809518" target="_blank"〉PubMed〈/a〉
    Keywords: Base Sequence ; Chromatin Assembly and Disassembly ; Chromosomal Proteins, Non-Histone/*metabolism ; Dimerization ; Dinucleoside Phosphates/metabolism ; *Introns ; Models, Genetic ; Nuclear Proteins/metabolism ; Oncogene Proteins/*metabolism ; Phosphorylation ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Messenger/metabolism ; Recombinant Proteins/metabolism ; Ribonucleoprotein, U2 Small Nuclear/metabolism ; Ribonucleoproteins/metabolism ; Spliceosomes/metabolism
    Print ISSN: 0036-8075
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  • 26
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    RIG-I-mediated antiviral responses to single-stranded RNA bearing 5'-phosphates (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-14
    Description: Double-stranded RNA (dsRNA) produced during viral replication is believed to be the critical trigger for activation of antiviral immunity mediated by the RNA helicase enzymes retinoic acid-inducible gene I (RIG-I) and melanoma differentiation-associated gene 5 (MDA5). We showed that influenza A virus infection does not generate dsRNA and that RIG-I is activated by viral genomic single-stranded RNA (ssRNA) bearing 5'-phosphates. This is blocked by the influenza protein nonstructured protein 1 (NS1), which is found in a complex with RIG-I in infected cells. These results identify RIG-I as a ssRNA sensor and potential target of viral immune evasion and suggest that its ability to sense 5'-phosphorylated RNA evolved in the innate immune system as a means of discriminating between self and nonself.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Pichlmair, Andreas -- Schulz, Oliver -- Tan, Choon Ping -- Naslund, Tanja I -- Liljestrom, Peter -- Weber, Friedemann -- Reis e Sousa, Caetano -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):997-1001. Epub 2006 Oct 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Immunobiology Laboratory, Cancer Research UK, London Research Institute, London WC2A 3PX, UK.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038589" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Cytoplasm/metabolism/virology ; DEAD-box RNA Helicases/genetics/*metabolism ; Dendritic Cells/virology ; Encephalomyocarditis virus/genetics/immunology/metabolism ; Genome, Viral ; Humans ; *Immunity, Innate ; Influenza A virus/*genetics/*immunology/metabolism/physiology ; Interferon-alpha/biosynthesis ; Interferon-beta/biosynthesis ; Mice ; Mice, Inbred C57BL ; Phosphates/metabolism ; Phosphorylation ; RNA Caps/metabolism ; RNA, Double-Stranded/metabolism ; RNA, Viral/chemistry/genetics/*metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection ; Vesicular stomatitis Indiana virus/genetics/immunology/metabolism ; Viral Nonstructural Proteins/genetics/metabolism ; Virus Replication
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  • 27
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    The Ste5 scaffold allosterically modulates signaling output of the yeast mating pathway (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-01-21
    Description: Scaffold proteins organize signaling proteins into pathways and are often viewed as passive assembly platforms. We found that the Ste5 scaffold has a more active role in the yeast mating pathway: A fragment of Ste5 allosterically activated autophosphorylation of the mitogen-activated protein kinase Fus3. The resulting form of Fus3 is partially active-it is phosphorylated on only one of two key residues in the activation loop. Unexpectedly, at a systems level, autoactivated Fus3 appears to have a negative regulatory role, promoting Ste5 phosphorylation and a decrease in pathway transcriptional output. Thus, scaffolds not only direct basic pathway connectivity but can precisely tune quantitative pathway input-output properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bhattacharyya, Roby P -- Remenyi, Attila -- Good, Matthew C -- Bashor, Caleb J -- Falick, Arnold M -- Lim, Wendell A -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):822-6. Epub 2006 Jan 19.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California-San Francisco, 600 16th Street, San Francisco, CA 94143-2240, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16424299" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/*chemistry/genetics/*metabolism ; Allosteric Regulation ; Amino Acid Motifs ; Binding Sites ; Crystallography, X-Ray ; Down-Regulation ; Enzyme Activation ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinases/*chemistry/*metabolism ; Models, Biological ; Models, Molecular ; Mutation ; Pheromones/*physiology ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/*chemistry/genetics/*metabolism ; Transcription, Genetic
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    Neuroscience. Getting a read on Rett syndrome (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-12-13
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Miller, Greg -- New York, N.Y. -- Science. 2006 Dec 8;314(5805):1536-7.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17158303" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/pathology/physiopathology ; Brain-Derived Neurotrophic Factor/genetics/metabolism ; Corticotropin-Releasing Hormone/genetics/physiology ; Female ; Gene Silencing ; Humans ; Mental Disorders/genetics ; Methyl-CpG-Binding Protein 2/*genetics/metabolism/*physiology ; Mice ; Mutation ; Neurons/pathology/physiology ; Phosphorylation ; Rett Syndrome/*genetics/pathology/*physiopathology
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  • 29
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    Prevention of Brca1-mediated mammary tumorigenesis in mice by a progesterone antagonist (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-12-02
    Description: Women with mutations in the breast cancer susceptibility gene BRCA1 are predisposed to breast and ovarian cancers. Why the BRCA1 protein suppresses tumor development specifically in ovarian hormone-sensitive tissues remains unclear. We demonstrate that mammary glands of nulliparous Brca1/p53-deficient mice accumulate lateral branches and undergo extensive alveologenesis, a phenotype that occurs only during pregnancy in wild-type mice. Progesterone receptors, but not estrogen receptors, are overexpressed in the mutant mammary epithelial cells because of a defect in their degradation by the proteasome pathway. Treatment of Brca1/p53-deficient mice with the progesterone antagonist mifepristone (RU 486) prevented mammary tumorigenesis. These findings reveal a tissue-specific function for the BRCA1 protein and raise the possibility that antiprogesterone treatment may be useful for breast cancer prevention in individuals with BRCA1 mutations.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Poole, Aleksandra Jovanovic -- Li, Ying -- Kim, Yoon -- Lin, Suh-Chin J -- Lee, Wen-Hwa -- Lee, Eva Y-H P -- CA049649/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1467-70.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, University of California, Irvine, CA 92697-4037, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17138902" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Breast Neoplasms/genetics/metabolism ; Cell Line, Tumor ; Cell Proliferation ; Epithelial Cells/cytology/metabolism ; Estradiol/pharmacology ; Estrous Cycle ; Female ; *Genes, BRCA1 ; Genes, p53 ; Hormone Antagonists/*pharmacology/therapeutic use ; Humans ; Mammary Glands, Animal/cytology/metabolism ; Mammary Neoplasms, Animal/genetics/*prevention & control ; Mice ; Mifepristone/*pharmacology/therapeutic use ; Mutation ; Phosphorylation ; Progesterone/*antagonists & inhibitors/pharmacology ; Proteasome Endopeptidase Complex/metabolism ; RNA, Small Interfering ; Receptors, Estrogen/metabolism ; Receptors, Progesterone/genetics/*metabolism ; Ubiquitin/metabolism
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    Intron removal requires proofreading of U2AF/3' splice site recognition by DEK (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-01
    Description: Discrimination between splice sites and similar, nonsplice sequences is essential for correct intron removal and messenger RNA formation in eukaryotes. The 65- and 35-kD subunits of the splicing factor U2AF, U2AF65 and U2AF35, recognize, respectively, the pyrimidine-rich tract and the conserved terminal AG present at metazoan 3' splice sites. We report that DEK, a chromatin- and RNA-associated protein mutated or overexpressed in certain cancers, enforces 3' splice site discrimination by U2AF. DEK phosphorylated at serines 19 and 32 associates with U2AF35, facilitates the U2AF35-AG interaction and prevents binding of U2AF65 to pyrimidine tracts not followed by AG. DEK and its phosphorylation are required for intron removal, but not for splicing complex assembly, which indicates that proofreading of early 3' splice site recognition influences catalytic activation of the spliceosome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Soares, Luis Miguel Mendes -- Zanier, Katia -- Mackereth, Cameron -- Sattler, Michael -- Valcarcel, Juan -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1961-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Centre de Regulacio Genomica, Passeig Maritim 37-49, 08003 Barcelona, Spain.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809543" target="_blank"〉PubMed〈/a〉
    Keywords: Adenosine Triphosphate/metabolism ; Chromosomal Proteins, Non-Histone/genetics/*metabolism ; Dimerization ; Dinucleoside Phosphates/metabolism ; HeLa Cells ; Humans ; *Introns ; Mutation ; Nuclear Proteins/*metabolism ; Oncogene Proteins/genetics/*metabolism ; Phosphorylation ; Pyrimidines/metabolism ; RNA Precursors/*metabolism ; *RNA Splicing ; RNA, Messenger/metabolism ; Recombinant Proteins/metabolism ; Ribonucleoprotein, U2 Small Nuclear ; Ribonucleoproteins/*metabolism ; Spliceosomes/metabolism
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    Neuroscience. ZAP and ZIP, a story to forget (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-26
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Bliss, Tim V P -- Collingridge, Graham L -- Laroche, Serge -- MC_U117512674/Medical Research Council/United Kingdom -- New York, N.Y. -- Science. 2006 Aug 25;313(5790):1058-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Neurophysiology, MRC National Institute for Medical Research, Mill Hill, London NW7 1AA, UK. tbliss@nimr.mrc.ac.uk〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16931746" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Avoidance Learning/physiology ; Dentate Gyrus/physiology ; Electric Stimulation ; Heat-Shock Proteins/pharmacology ; Hippocampus/*physiology ; *Long-Term Potentiation/drug effects ; Long-Term Synaptic Depression/physiology ; Memory/*physiology ; Models, Neurological ; Neurons/physiology ; Phosphorylation ; Protein Kinase C/antagonists & inhibitors/metabolism ; Rats ; Receptors, AMPA/metabolism ; Synapses/*physiology ; Transcription, Genetic
    Print ISSN: 0036-8075
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  • 32
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    Activity- and mTOR-dependent suppression of Kv1.1 channel mRNA translation in dendrites (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-07
    Description: Mammalian target of rapamycin (mTOR) is implicated in synaptic plasticity and local translation in dendrites. We found that the mTOR inhibitor, rapamycin, increased the Kv1.1 voltage-gated potassium channel protein in hippocampal neurons and promoted Kv1.1 surface expression on dendrites without altering its axonal expression. Moreover, endogenous Kv1.1 mRNA was detected in dendrites. Using Kv1.1 fused to the photoconvertible fluorescence protein Kaede as a reporter for local synthesis, we observed Kv1.1 synthesis in dendrites upon inhibition of mTOR or the N-methyl-d-aspartate (NMDA) glutamate receptor. Thus, synaptic excitation may cause local suppression of dendritic Kv1 channels by reducing their local synthesis.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Raab-Graham, Kimberly F -- Haddick, Patrick C G -- Jan, Yuh Nung -- Jan, Lily Yeh -- MH13010/MH/NIMH NIH HHS/ -- MH65334/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):144-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Departments of Physiology and Biochemistry, University of California, San Francisco, CA 94158, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17023663" target="_blank"〉PubMed〈/a〉
    Keywords: 3' Untranslated Regions ; Animals ; Cells, Cultured ; Dendrites/drug effects/*metabolism ; Excitatory Postsynaptic Potentials ; Hippocampus/drug effects/*metabolism ; In Vitro Techniques ; Kv1.1 Potassium Channel/*biosynthesis/*genetics ; Neuronal Plasticity ; Neurons/metabolism/virology ; Oligonucleotide Array Sequence Analysis ; Phosphorylation ; Protein Biosynthesis ; Protein Kinase Inhibitors/pharmacology ; Protein Kinases/*physiology ; RNA, Messenger/genetics/metabolism ; Rats ; Rats, Sprague-Dawley ; Receptors, N-Methyl-D-Aspartate/antagonists & inhibitors/metabolism ; Recombinant Fusion Proteins/metabolism ; Sindbis Virus/physiology ; Sirolimus/pharmacology ; Synapses/physiology ; TOR Serine-Threonine Kinases
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    Cell signaling. H2O2, a necessary evil for cell signaling (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-07-01
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rhee, Sue Goo -- New York, N.Y. -- Science. 2006 Jun 30;312(5782):1882-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Life Science and Technology, Ewha Women's University, Seoul 120-750, South Korea. rheesg@ewha.ac.kr〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16809515" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Membrane/metabolism ; Cysteine/metabolism ; Cytosol/metabolism ; Humans ; Hydrogen Peroxide/*metabolism ; NADP/metabolism ; Organelles/metabolism ; Oxidation-Reduction ; Peroxidases/metabolism ; Peroxiredoxins ; Phosphorylation ; Protein Tyrosine Phosphatases/metabolism ; Protein-Tyrosine Kinases/metabolism ; Proteins/metabolism ; Reactive Oxygen Species/metabolism ; Receptors, Cell Surface/metabolism ; *Signal Transduction ; Tyrosine/metabolism
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  • 34
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    Cell signaling. A sophisticated scaffold wields a new trick (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-02-14
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Breitkreutz, Ashton -- Tyers, Mike -- New York, N.Y. -- Science. 2006 Feb 10;311(5762):789-90.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Campbell Family Institute for Breast Cancer Research, Toronto Medical Discovery Tower, Toronto, Canada M5G 1L7. abreitkr@uhnres.utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16469909" target="_blank"〉PubMed〈/a〉
    Keywords: Adaptor Proteins, Signal Transducing/chemistry/genetics/*metabolism ; Binding Sites ; *MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase Kinases ; Mitogen-Activated Protein Kinases/chemistry/*metabolism ; Models, Biological ; Mutation ; Pheromones/physiology ; Phosphorylation ; Protein Binding ; Protein Conformation ; Protein Kinases/metabolism ; Saccharomyces cerevisiae/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Tyrosine/metabolism
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    Microbiology. Bacteria seize control by acetylating host proteins (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-05-30
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Worby, Carolyn A -- Dixon, Jack E -- New York, N.Y. -- Science. 2006 May 26;312(5777):1150-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, University of California at San Diego, 9500 Gilman Drive, La Jolla, CA 92093, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16731519" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Acetyltransferases/metabolism ; Bacterial Proteins/*metabolism ; Enzyme Activation ; Humans ; I-kappa B Kinase/*metabolism ; MAP Kinase Kinase 1/metabolism ; MAP Kinase Kinase 6/*metabolism ; MAP Kinase Kinase Kinases/metabolism ; MAP Kinase Signaling System ; Mitogen-Activated Protein Kinase Kinases/metabolism ; Models, Biological ; NF-kappa B/metabolism ; Phosphorylation ; SUMO-1 Protein/metabolism ; Serine/metabolism ; Signal Transduction ; Threonine/metabolism ; Yersinia/*metabolism/pathogenicity ; Yersinia pestis/metabolism/pathogenicity ; p38 Mitogen-Activated Protein Kinases/metabolism
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  • 36
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    Ubiquitinated TDP-43 in frontotemporal lobar degeneration and amyotrophic lateral sclerosis (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-07
    Description: Ubiquitin-positive, tau- and alpha-synuclein-negative inclusions are hallmarks of frontotemporal lobar degeneration with ubiquitin-positive inclusions and amyotrophic lateral sclerosis. Although the identity of the ubiquitinated protein specific to either disorder was unknown, we showed that TDP-43 is the major disease protein in both disorders. Pathologic TDP-43 was hyper-phosphorylated, ubiquitinated, and cleaved to generate C-terminal fragments and was recovered only from affected central nervous system regions, including hippocampus, neocortex, and spinal cord. TDP-43 represents the common pathologic substrate linking these neurodegenerative disorders.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Neumann, Manuela -- Sampathu, Deepak M -- Kwong, Linda K -- Truax, Adam C -- Micsenyi, Matthew C -- Chou, Thomas T -- Bruce, Jennifer -- Schuck, Theresa -- Grossman, Murray -- Clark, Christopher M -- McCluskey, Leo F -- Miller, Bruce L -- Masliah, Eliezer -- Mackenzie, Ian R -- Feldman, Howard -- Feiden, Wolfgang -- Kretzschmar, Hans A -- Trojanowski, John Q -- Lee, Virginia M-Y -- AG10124/AG/NIA NIH HHS/ -- AG17586/AG/NIA NIH HHS/ -- T32 AG00255/AG/NIA NIH HHS/ -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):130-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, 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/17023659" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amyotrophic Lateral Sclerosis/*metabolism/pathology ; Antibodies, Monoclonal ; *Brain Chemistry ; Cerebral Cortex/chemistry/pathology ; DNA-Binding Proteins/*analysis/chemistry/genetics/immunology ; Dementia/genetics/*metabolism/pathology ; Fluorescent Antibody Technique ; Hippocampus/chemistry/pathology ; Humans ; Immunoblotting ; Molecular Sequence Data ; Motor Neurons/chemistry/pathology ; Neurons/chemistry/pathology ; Peptide Fragments/chemistry ; Phosphorylation ; Spinal Cord/*chemistry/pathology ; Ubiquitin/*analysis
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    Comment on "PDK1 nucleates T cell receptor-induced signaling complex for NF-kappaB activation" (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-08
    Description: We observe that protein kinase C (PKC) is phosphorylated on the activation loop at threonine 538 (Thr-538) before T cell activation. Our results are inconsistent with the conclusions of Lee et al. (Reports, 1 April 2005, p. 114) that the Thr-538 phosphorylation of PKC is regulated by T cell receptor activation. Other mechanisms, such as autophosphorylation of Thr-219, might orchestrate the cellular function of PKC in T cells.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Gruber, Thomas -- Freeley, Michael -- Thuille, Nikolaus -- Heit, Isabelle -- Shaw, Stephen -- Long, Aideen -- Baier, Gottfried -- New York, N.Y. -- Science. 2006 Apr 7;312(5770):55; author reply 55.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department for Medical Genetics, Molecular and Clinical Pharmacology, Innsbruck Medical University, Austria.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16601177" target="_blank"〉PubMed〈/a〉
    Keywords: 3-Phosphoinositide-Dependent Protein Kinases ; Animals ; Antibodies/immunology ; Antigens, CD28/immunology ; Antigens, CD3/immunology ; Cells, Cultured ; Humans ; Isoenzymes/*metabolism ; Jurkat Cells ; Lymphocyte Activation ; Mice ; NF-kappa B/*metabolism ; Phosphorylation ; Protein Kinase C/*metabolism ; Protein-Serine-Threonine Kinases/*metabolism ; Receptors, Antigen, T-Cell/metabolism ; Signal Transduction ; T-Lymphocytes/enzymology/immunology/*metabolism ; Threonine/metabolism
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    Auxiliary subunits assist AMPA-type glutamate receptors (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-03-04
    Description: Glutamate, the major excitatory neurotransmitter in the brain, acts primarily on two types of ionotropic receptors: alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors and N-methyl-d-aspartate (NMDA) receptors. Work over the past decade indicates that regulated changes in the number of synaptic AMPA receptors may serve as a mechanism for information storage. Recent studies demonstrate that a family of small transmembrane AMPA receptor regulatory proteins (TARPs) controls both AMPA receptor trafficking and channel gating. TARPs provide the first example of auxiliary subunits of ionotropic receptors. Here we review the pivotal role that TARPs play in the life cycle of AMPA receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Nicoll, Roger A -- Tomita, Susumu -- Bredt, David S -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1253-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cellular and Molecular Pharmacology, University of California at San Francisco, San Francisco, CA 94143, USA. nicoll@cmp.ucsf.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16513974" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/*metabolism ; Calcium Channels/*metabolism ; Hippocampus/metabolism ; Ion Channel Gating ; Mice ; Models, Biological ; Neuronal Plasticity ; Neurons/metabolism ; Phosphorylation ; Protein Binding ; Protein Transport ; Receptors, AMPA/*metabolism ; Synapses/*metabolism ; Synaptic Transmission
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    Germline mutations in genes within the MAPK pathway cause cardio-facio-cutaneous syndrome (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-01-28
    Description: Cardio-facio-cutaneous (CFC) syndrome is a sporadic developmental disorder involving characteristic craniofacial features, cardiac defects, ectodermal abnormalities, and developmental delay. We demonstrate that heterogeneous de novo missense mutations in three genes within the mitogen-activated protein kinase (MAPK) pathway cause CFC syndrome. The majority of cases (18 out of 23) are caused by mutations in BRAF, a gene frequently mutated in cancer. Of the 11 mutations identified, two result in amino acid substitutions that occur in tumors, but most are unique and suggest previously unknown mechanisms of B-Raf activation. Furthermore, three of five individuals without BRAF mutations had missense mutations in either MEK1 or MEK2, downstream effectors of B-Raf. Our findings highlight the involvement of the MAPK pathway in human development and will provide a molecular diagnosis of CFC syndrome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Rodriguez-Viciana, Pablo -- Tetsu, Osamu -- Tidyman, William E -- Estep, Anne L -- Conger, Brenda A -- Cruz, Molly Santa -- McCormick, Frank -- Rauen, Katherine A -- HD048502/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2006 Mar 3;311(5765):1287-90. Epub 2006 Jan 26.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Comprehensive Cancer Center and Cancer Research Institute, University of California, San Francisco, CA 94115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16439621" target="_blank"〉PubMed〈/a〉
    Keywords: Abnormalities, Multiple/*genetics ; Adolescent ; Adult ; Amino Acid Substitution ; Child ; Child, Preschool ; Craniofacial Abnormalities/genetics ; Extracellular Signal-Regulated MAP Kinases/metabolism ; Female ; *Germ-Line Mutation ; Growth Disorders/genetics ; Heart Defects, Congenital/genetics ; Humans ; Infant ; MAP Kinase Kinase 1/genetics ; MAP Kinase Kinase 2/genetics ; MAP Kinase Kinase Kinases/metabolism ; MAP Kinase Signaling System ; Male ; Mitogen-Activated Protein Kinases/genetics/*metabolism ; Mutation, Missense ; Phosphorylation ; Proto-Oncogene Proteins B-raf/genetics ; Skin Abnormalities/genetics ; Syndrome ; Transfection
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    Action of TFII-I outside the nucleus as an inhibitor of agonist-induced calcium entry (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-07
    Description: TFII-I is a transcription factor and a target of phosphorylation by Bruton's tyrosine kinase. In humans, deletions spanning the TFII-I locus are associated with a cognitive defect, the Williams-Beuren cognitive profile. We report an unanticipated role of TFII-I outside the nucleus as a negative regulator of agonist-induced calcium entry (ACE) that suppresses surface accumulation of TRPC3 (transient receptor potential C3) channels. Inhibition of ACE by TFII-I requires phosphotyrosine residues that engage the SH2 (Src-homology 2) domains of phospholipase C-g (PLC-g) and an interrupted, pleckstrin homology (PH)-like domain that binds the split PH domain of PLC-g. Our observations suggest a model in which TFII-I suppresses ACE by competing with TRPC3 for binding to PLC-g.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Caraveo, Gabriela -- van Rossum, Damian B -- Patterson, Randen L -- Snyder, Solomon H -- Desiderio, Stephen -- New York, N.Y. -- Science. 2006 Oct 6;314(5796):122-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Genetics, Institute for Cell Engineering, 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/17023658" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Bradykinin/pharmacology ; Calcium/*metabolism ; Calcium Channels/*metabolism ; Cell Line ; Cell Membrane/metabolism ; Cytoplasm/metabolism ; Humans ; Models, Biological ; Molecular Sequence Data ; PC12 Cells ; Phospholipase C gamma/chemistry/*metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Rats ; TRPC Cation Channels/*metabolism ; Transcription Factors, TFII/chemistry/*metabolism ; Uridine Triphosphate/pharmacology ; src Homology Domains
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    Nuclear receptor Rev-erbalpha is a critical lithium-sensitive component of the circadian clock (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-02-18
    Description: Lithium is commonly used to treat bipolar disorder, which is associated with altered circadian rhythm. Lithium is a potent inhibitor of glycogen synthase kinase 3 (GSK3), which regulates circadian rhythm in several organisms. In experiments with cultured cells, we show here that GSK3beta phosphorylates and stabilizes the orphan nuclear receptor Rev-erbalpha, a negative component of the circadian clock. Lithium treatment of cells leads to rapid proteasomal degradation of Rev-erbalpha and activation of clock gene Bmal1. A form of Rev-erbalpha that is insensitive to lithium interferes with the expression of circadian genes. Control of Rev-erbalpha protein stability is thus a critical component of the peripheral clock and a biological target of lithium therapy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yin, Lei -- Wang, Jing -- Klein, Peter S -- Lazar, Mitchell A -- DK 19525/DK/NIDDK NIH HHS/ -- DK45586/DK/NIDDK NIH HHS/ -- MH058324/MH/NIMH NIH HHS/ -- R01 MH058324/MH/NIMH NIH HHS/ -- R01 MH058324-07/MH/NIMH NIH HHS/ -- R01 MH058324-08/MH/NIMH NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 17;311(5763):1002-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Endocrinology, Diabetes, and Metabolism, and University of Pennsylvania School of Medicine, 415 Curie Boulevard, Philadelphia, PA 19104, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16484495" target="_blank"〉PubMed〈/a〉
    Keywords: ARNTL Transcription Factors ; Amino Acid Sequence ; Animals ; Basic Helix-Loop-Helix Transcription Factors/genetics/metabolism ; Biological Clocks/*physiology ; Cell Line ; Cell Line, Tumor ; Circadian Rhythm/*physiology ; DNA-Binding Proteins/chemistry/genetics/*metabolism ; Down-Regulation ; Gene Expression Regulation ; Glycogen Synthase Kinase 3/antagonists & inhibitors/metabolism ; Humans ; Lithium Chloride/*pharmacology ; Mice ; Molecular Sequence Data ; NIH 3T3 Cells ; Nuclear Receptor Subfamily 1, Group D, Member 1 ; Phosphorylation ; Promoter Regions, Genetic ; Proteasome Endopeptidase Complex/metabolism ; Proteasome Inhibitors ; Receptors, Cytoplasmic and Nuclear/chemistry/genetics/*metabolism
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    Multiple phosphorylation sites confer reproducibility of the rod's single-photon responses (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-07-29
    Description: Although signals controlled by single molecules are expected to be inherently variable, rod photoreceptors generate reproducible responses to single absorbed photons. We show that this unexpected reproducibility-the consistency of amplitude and duration of rhodopsin activity-varies in a graded and systematic manner with the number but not the identity of phosphorylation sites on rhodopsin's C terminus. These results indicate that each phosphorylation site provides an independent step in rhodopsin deactivation and that collectively these steps tightly control rhodopsin's active lifetime. Other G protein cascades may exploit a similar mechanism to encode accurately the timing and number of receptor activation.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Doan, Thuy -- Mendez, Ana -- Detwiler, Peter B -- Chen, Jeannie -- Rieke, Fred -- EY-02048/EY/NEI NIH HHS/ -- EY-11850/EY/NEI NIH HHS/ -- EY-12155/EY/NEI NIH HHS/ -- T32EY-07031/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 2006 Jul 28;313(5786):530-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Program in Neurobiology and Behavior, University of Washington, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16873665" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Arrestin/metabolism ; Electrophysiology ; Mice ; Mice, Transgenic ; Models, Biological ; Mutation ; Patch-Clamp Techniques ; Phosphorylation ; *Photons ; Retinal Rod Photoreceptor Cells/*metabolism ; Rhodopsin/genetics/*metabolism ; Vision, Ocular
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    Rapid chemically induced changes of PtdIns(4,5)P2 gate KCNQ ion channels (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-09-23
    Description: To resolve the controversy about messengers regulating KCNQ ion channels during phospholipase C-mediated suppression of current, we designed translocatable enzymes that quickly alter the phosphoinositide composition of the plasma membrane after application of a chemical cue. The KCNQ current falls rapidly to zero when phosphatidylinositol 4,5-bisphosphate [PtdIns(4,5)P2 or PI(4,5)P2] is depleted without changing Ca2+, diacylglycerol, or inositol 1,4,5-trisphosphate. Current rises by 30% when PI(4,5)P2 is overproduced and does not change when phosphatidylinositol 3,4,5-trisphosphate is raised. Hence, the depletion of PI(4,5)P2 suffices to suppress current fully, and other second messengers are not needed. Our approach is ideally suited to study biological signaling networks involving membrane phosphoinositides.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3579521/" 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/PMC3579521/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Suh, Byung-Chang -- Inoue, Takanari -- Meyer, Tobias -- Hille, Bertil -- AR17803/AR/NIAMS NIH HHS/ -- GM63702/GM/NIGMS NIH HHS/ -- MH64801/MH/NIMH NIH HHS/ -- NS08174/NS/NINDS NIH HHS/ -- R01 GM030179/GM/NIGMS NIH HHS/ -- R01 GM030179-24A1/GM/NIGMS NIH HHS/ -- R01 GM030179-25/GM/NIGMS NIH HHS/ -- R01 GM063702/GM/NIGMS NIH HHS/ -- R01 MH064801/MH/NIMH NIH HHS/ -- R01 NS008174/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1454-7. Epub 2006 Sep 21.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16990515" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Calcium/metabolism ; Cell Line ; Cell Membrane/*metabolism ; Diglycerides/metabolism ; Dimerization ; Humans ; *Ion Channel Gating ; KCNQ Potassium Channels/*metabolism ; KCNQ2 Potassium Channel/metabolism ; KCNQ3 Potassium Channel/metabolism ; Mice ; NIH 3T3 Cells ; Oxotremorine/analogs & derivatives/pharmacology ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphoric Monoester Hydrolases/metabolism ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Second Messenger Systems ; Sirolimus/analogs & derivatives/pharmacology
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    Polo-like kinase Cdc5 controls the local activation of Rho1 to promote cytokinesis (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-06-10
    Description: The links between the cell cycle machinery and the cytoskeletal proteins controlling cytokinesis are poorly understood. The small guanine nucleotide triphosphate (GTP)-binding protein RhoA stimulates type II myosin contractility and formin-dependent assembly of the cytokinetic actin contractile ring. We found that budding yeast Polo-like kinase Cdc5 controls the targeting and activation of Rho1 (RhoA) at the division site via Rho1 guanine nucleotide exchange factors. This role of Cdc5 (Polo-like kinase) in regulating Rho1 is likely to be relevant to cytokinesis and asymmetric cell division in other organisms.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Yoshida, Satoshi -- Kono, Keiko -- Lowery, Drew M -- Bartolini, Sara -- Yaffe, Michael B -- Ohya, Yoshikazu -- Pellman, David -- New York, N.Y. -- Science. 2006 Jul 7;313(5783):108-11. Epub 2006 Jun 8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pediatric Oncology, Dana-Farber Cancer Institute and Division of Hematology/Oncology, Children's Hospital Boston and Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16763112" target="_blank"〉PubMed〈/a〉
    Keywords: Actins/metabolism ; Amino Acid Motifs ; Anaphase ; Cell Cycle Proteins/chemistry/genetics/*metabolism ; *Cytokinesis ; Guanine Nucleotide Exchange Factors/chemistry/genetics/metabolism ; Guanosine Triphosphate/metabolism ; Microfilament Proteins/metabolism ; Mitosis ; Mutation ; Phosphorylation ; Protein Kinases/chemistry/genetics/*metabolism ; Protein-Serine-Threonine Kinases ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*cytology/genetics/*metabolism ; Saccharomyces cerevisiae Proteins/chemistry/genetics/*metabolism ; Temperature ; rho GTP-Binding Proteins/*metabolism
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    Crystal structure of the rabies virus nucleoprotein-RNA complex (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-06-17
    Description: Negative-strand RNA viruses condense their genome into a helical nucleoprotein-RNA complex, the nucleocapsid, which is packed into virions and serves as a template for the RNA-dependent RNA polymerase complex. The crystal structure of a recombinant rabies virus nucleoprotein-RNA complex, organized in an undecameric ring, has been determined at 3.5 angstrom resolution. Polymerization of the nucleoprotein is achieved by domain exchange between protomers, with flexible hinges allowing nucleocapsid formation. The two core domains of the nucleoprotein clamp around the RNA at their interface and shield it from the environment. RNA sequestering by nucleoproteins is likely a common mechanism used by negative-strand RNA viruses to protect their genomes from the innate immune response directed against viral RNA in human host cells at certain stages of an infectious cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Albertini, Aurelie A V -- Wernimont, Amy K -- Muziol, Tadeusz -- Ravelli, Raimond B G -- Clapier, Cedric R -- Schoehn, Guy -- Weissenhorn, Winfried -- Ruigrok, Rob W H -- New York, N.Y. -- Science. 2006 Jul 21;313(5785):360-3. Epub 2006 Jun 15.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institut de Virologie Moleculaire et Structurale, FRE 2854 Universite Joseph Fourier-CNRS, Boite Postale 181, 38042 Grenoble, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16778023" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Crystallography, X-Ray ; DNA-Directed RNA Polymerases/metabolism ; Genome, Viral ; Models, Molecular ; Molecular Sequence Data ; Nucleic Acid Conformation ; Nucleocapsid Proteins/*chemistry/metabolism ; Phosphoproteins/metabolism ; Phosphorylation ; Protein Conformation ; Protein Folding ; Protein Structure, Quaternary ; Protein Structure, Secondary ; Protein Structure, Tertiary ; Protein Subunits/chemistry ; RNA, Viral/*chemistry/genetics/metabolism ; Rabies virus/*chemistry/genetics ; Recombinant Proteins/chemistry ; Ribonucleoproteins/*chemistry
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    A genomewide search for ribozymes reveals an HDV-like sequence in the human CPEB3 gene (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-09-23
    Description: Ribozymes are thought to have played a pivotal role in the early evolution of life, but relatively few have been identified in modern organisms. We performed an in vitro selection aimed at isolating self-cleaving RNAs from the human genome. The selection yielded several ribozymes, one of which is a conserved mammalian sequence that resides in an intron of the CPEB3 gene, which belongs to a family of genes regulating messenger RNA polyadenylation. The CPEB3 ribozyme is structurally and biochemically related to the human hepatitis delta virus (HDV) ribozymes. The occurrence of this ribozyme exclusively in mammals suggests that it may have evolved as recently as 200 million years ago. We postulate that HDV arose from the human transcriptome.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Salehi-Ashtiani, Kourosh -- Luptak, Andrej -- Litovchick, Alexander -- Szostak, Jack W -- GM53936/GM/NIGMS NIH HHS/ -- HL66678/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 22;313(5794):1788-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Department of Molecular Biology, and Center for Computational and Integrative Biology (CCIB), 7215 Simches Research Center, Massachusetts General Hospital, 185 Cambridge Street, Boston, MA 02114, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16990549" target="_blank"〉PubMed〈/a〉
    Keywords: Base Pairing ; Base Sequence ; Catalysis ; Cations, Divalent/metabolism ; Conserved Sequence ; *Evolution, Molecular ; Expressed Sequence Tags ; *Genome, Human ; Genomic Library ; Hepatitis Delta Virus/genetics ; Humans ; Hydrogen-Ion Concentration ; *Introns ; Molecular Sequence Data ; Mutation ; Nucleic Acid Conformation ; Phosphorylation ; RNA, Catalytic/chemistry/genetics/*isolation & purification/*metabolism ; RNA-Binding Proteins/*genetics
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    The muscle protein Dok-7 is essential for neuromuscular synaptogenesis (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-06-24
    Description: The formation of the neuromuscular synapse requires muscle-specific receptor kinase (MuSK) to orchestrate postsynaptic differentiation, including the clustering of receptors for the neurotransmitter acetylcholine. Upon innervation, neural agrin activates MuSK to establish the postsynaptic apparatus, although agrin-independent formation of neuromuscular synapses can also occur experimentally in the absence of neurotransmission. Dok-7, a MuSK-interacting cytoplasmic protein, is essential for MuSK activation in cultured myotubes; in particular, the Dok-7 phosphotyrosine-binding domain and its target in MuSK are indispensable. Mice lacking Dok-7 formed neither acetylcholine receptor clusters nor neuromuscular synapses. Thus, Dok-7 is essential for neuromuscular synaptogenesis through its interaction with MuSK.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Okada, Kumiko -- Inoue, Akane -- Okada, Momoko -- Murata, Yoji -- Kakuta, Shigeru -- Jigami, Takafumi -- Kubo, Sachiko -- Shiraishi, Hirokazu -- Eguchi, Katsumi -- Motomura, Masakatsu -- Akiyama, Tetsu -- Iwakura, Yoichiro -- Higuchi, Osamu -- Yamanashi, Yuji -- New York, N.Y. -- Science. 2006 Jun 23;312(5781):1802-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Regulation, Medical Research Institute, Tokyo Medical and Dental University, Tokyo 113-8510, Japan.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16794080" target="_blank"〉PubMed〈/a〉
    Keywords: Agrin/metabolism ; Amino Acid Motifs ; Amino Acid Sequence ; Animals ; Cell Differentiation ; Cell Line ; Down-Regulation ; Enzyme Activation ; Humans ; In Situ Hybridization ; Mice ; Molecular Sequence Data ; Motor Endplate/embryology/metabolism ; Muscle Denervation ; Muscle Fibers, Skeletal/cytology/metabolism ; Muscle Proteins/chemistry/genetics/*metabolism ; Muscle, Skeletal/embryology/*innervation/metabolism ; Mutation ; Neuromuscular Junction/*physiology ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Receptor Aggregation ; Receptor Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Cholinergic/genetics/*metabolism ; Synapses/*physiology ; Synaptic Transmission
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    PirB restricts ocular-dominance plasticity in visual cortex (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-19
    Description: Experience can alter synaptic connectivity throughout life, but the degree of plasticity present at each age is regulated by mechanisms that remain largely unknown. Here, we demonstrate that Paired-immunoglobulin-like receptor B (PirB), a major histocompatibility complex class I (MHCI) receptor, is expressed in subsets of neurons throughout the brain. Neuronal PirB protein is associated with synapses and forms complexes with the phosphatases Shp-1 and Shp-2. Soluble PirB fusion protein binds to cortical neurons in an MHCI-dependent manner. In mutant mice lacking functional PirB, cortical ocular-dominance plasticity is more robust at all ages. Thus, an MHCI receptor is expressed in central nervous system neurons and functions to limit the extent of experience-dependent plasticity in the visual cortex throughout life. PirB is also expressed in many other regions of the central nervous system, suggesting that it may function broadly to stabilize neural circuits.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Syken, Josh -- Grandpre, Tadzia -- Kanold, Patrick O -- Shatz, Carla J -- EY02858/EY/NEI NIH HHS/ -- F32 EY013526/EY/NEI NIH HHS/ -- F32 EY013526-01/EY/NEI NIH HHS/ -- F32EY1352/EY/NEI NIH HHS/ -- HD18655/HD/NICHD NIH HHS/ -- New York, N.Y. -- Science. 2006 Sep 22;313(5794):1795-800. Epub 2006 Aug 17.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Neurobiology, Harvard Medical School, 220 Longwood Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917027" target="_blank"〉PubMed〈/a〉
    Keywords: Aging ; Animals ; Brain/metabolism ; Cells, Cultured ; Cytoskeletal Proteins/genetics/metabolism ; Dominance, Ocular/*physiology ; Histocompatibility Antigens Class I/metabolism ; In Situ Hybridization ; Intracellular Signaling Peptides and Proteins/metabolism ; Mice ; Mice, Inbred C57BL ; Mutation ; Nerve Tissue Proteins/genetics/metabolism ; *Neuronal Plasticity ; Neurons/metabolism ; Phosphorylation ; Protein Binding ; Protein Structure, Tertiary ; Protein Tyrosine Phosphatase, Non-Receptor Type 11 ; Protein Tyrosine Phosphatase, Non-Receptor Type 6 ; Protein Tyrosine Phosphatases/metabolism ; Receptors, Immunologic/chemistry/genetics/metabolism/*physiology ; Recombinant Fusion Proteins/metabolism ; Synapses/metabolism/*physiology ; Visual Cortex/*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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    Proapoptotic BAX and BAK modulate the unfolded protein response by a direct interaction with IRE1alpha (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-04-29
    Description: Accumulation of misfolded protein in the endoplasmic reticulum (ER) triggers an adaptive stress response-termed the unfolded protein response (UPR)-mediated by the ER transmembrane protein kinase and endoribonuclease inositol-requiring enzyme-1alpha (IRE1alpha). We investigated UPR signaling events in mice in the absence of the proapoptotic BCL-2 family members BAX and BAK [double knockout (DKO)]. DKO mice responded abnormally to tunicamycin-induced ER stress in the liver, with extensive tissue damage and decreased expression of the IRE1 substrate X-box-binding protein 1 and its target genes. ER-stressed DKO cells showed deficient IRE1alpha signaling. BAX and BAK formed a protein complex with the cytosolic domain of IRE1alpha that was essential for IRE1alpha activation. Thus, BAX and BAK function at the ER membrane to activate IRE1alpha signaling and to provide a physical link between members of the core apoptotic pathway and the UPR.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hetz, Claudio -- Bernasconi, Paula -- Fisher, Jill -- Lee, Ann-Hwee -- Bassik, Michael C -- Antonsson, Bruno -- Brandt, Gabriel S -- Iwakoshi, Neal N -- Schinzel, Anna -- Glimcher, Laurie H -- Korsmeyer, Stanley J -- CA100707/CA/NCI NIH HHS/ -- P01 AI56296/AI/NIAID NIH HHS/ -- P01 CA92625/CA/NCI NIH HHS/ -- R01 AI32412/AI/NIAID NIH HHS/ -- R37 CA50239/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 2006 Apr 28;312(5773):572-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Dana-Farber Cancer Institute, and Harvard Medical School, Boston, MA 02115, USA. chetz@hsph.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16645094" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; DNA-Binding Proteins/metabolism ; Endoplasmic Reticulum/*metabolism/ultrastructure ; Endoribonucleases/*metabolism ; Gene Expression Regulation ; Heat-Shock Proteins/metabolism ; Humans ; Kidney/cytology/drug effects/metabolism ; Liver/cytology/drug effects/metabolism ; Mice ; Mice, Knockout ; Mitochondria/metabolism ; Molecular Chaperones/metabolism ; Nuclear Proteins/metabolism ; Phosphorylation ; Protein Folding ; Protein Structure, Tertiary ; Protein-Serine-Threonine Kinases/*metabolism ; Proto-Oncogene Proteins c-bcl-2/metabolism ; Recombinant Proteins/metabolism ; Signal Transduction ; Transcription Factor CHOP/metabolism ; Transcription Factors ; Tunicamycin/pharmacology ; bcl-2 Homologous Antagonist-Killer Protein/chemistry/genetics/*metabolism ; bcl-2-Associated X Protein/genetics/*metabolism ; eIF-2 Kinase/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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  • 50
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    Chemical chaperones reduce ER stress and restore glucose homeostasis in a mouse model of type 2 diabetes (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-26
    Description: Endoplasmic reticulum (ER) stress is a key link between obesity, insulin resistance, and type 2 diabetes. Here, we provide evidence that this mechanistic link can be exploited for therapeutic purposes with orally active chemical chaperones. 4-Phenyl butyric acid and taurine-conjugated ursodeoxycholic acid alleviated ER stress in cells and whole animals. Treatment of obese and diabetic mice with these compounds resulted in normalization of hyperglycemia, restoration of systemic insulin sensitivity, resolution of fatty liver disease, and enhancement of insulin action in liver, muscle, and adipose tissues. Our results demonstrate that chemical chaperones enhance the adaptive capacity of the ER and act as potent antidiabetic modalities with potential application in the treatment of type 2 diabetes.〈br /〉〈br /〉〈a href="https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4741373/" 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/PMC4741373/" target="_blank"〉This paper as free author manuscript - peer-reviewed and accepted for publication〈/a〉〈br /〉〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Ozcan, Umut -- Yilmaz, Erkan -- Ozcan, Lale -- Furuhashi, Masato -- Vaillancourt, Eric -- Smith, Ross O -- Gorgun, Cem Z -- Hotamisligil, Gokhan S -- DK52539/DK/NIDDK NIH HHS/ -- P30 DK040561/DK/NIDDK NIH HHS/ -- P30 DK040561-11/DK/NIDDK NIH HHS/ -- R01 DK052539/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 25;313(5790):1137-40.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Genetics and Complex Diseases, Harvard School of Public Health, Harvard University, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16931765" target="_blank"〉PubMed〈/a〉
    Keywords: Adipose Tissue/metabolism ; Animals ; Blood Glucose/metabolism ; Cell Line, Tumor ; Diabetes Mellitus, Type 2/drug therapy/*metabolism ; Disease Models, Animal ; Endoplasmic Reticulum/drug effects/*metabolism ; Enzyme Activation ; Eukaryotic Initiation Factor-2/metabolism ; Glucose/administration & dosage/*metabolism ; Glucose Tolerance Test ; Homeostasis ; Insulin/blood/pharmacology ; Insulin Resistance ; JNK Mitogen-Activated Protein Kinases/metabolism ; Liver/metabolism ; Mice ; Mice, Obese ; Phenylbutyrates/*pharmacology/therapeutic use ; Phosphorylation ; Receptor, Insulin/metabolism ; Signal Transduction ; Taurochenodeoxycholic Acid/*pharmacology/therapeutic use ; eIF-2 Kinase/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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    Graded regulation of the Kv2.1 potassium channel by variable phosphorylation (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-08-19
    Description: Dynamic modulation of ion channels by phosphorylation underlies neuronal plasticity. The Kv2.1 potassium channel is highly phosphorylated in resting mammalian neurons. Activity-dependent Kv2.1 dephosphorylation by calcineurin induces graded hyperpolarizing shifts in voltage-dependent activation, causing suppression of neuronal excitability. Mass spectrometry-SILAC (stable isotope labeling with amino acids in cell culture) identified 16 Kv2.1 phosphorylation sites, of which 7 were dephosphorylated by calcineurin. Mutation of individual calcineurin-regulated sites to alanine produced incremental shifts mimicking dephosphorylation, whereas mutation to aspartate yielded equivalent resistance to calcineurin. Mutations at multiple sites were additive, showing that variable phosphorylation of Kv2.1 at a large number of sites allows graded activity-dependent regulation of channel gating and neuronal firing properties.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Park, Kang-Sik -- Mohapatra, Durga P -- Misonou, Hiroaki -- Trimmer, James S -- NS42225/NS/NINDS NIH HHS/ -- R01 NS042225/NS/NINDS NIH HHS/ -- R01 NS042225-06/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2006 Aug 18;313(5789):976-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pharmacology, School of Medicine, University of California, Davis, CA 95616, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16917065" target="_blank"〉PubMed〈/a〉
    Keywords: Alanine/genetics/metabolism ; Alkaline Phosphatase/metabolism ; Animals ; Aspartic Acid/genetics/metabolism ; Brain/metabolism ; Calcineurin/metabolism ; Calcium/metabolism ; Cell Line ; Chromatography, Liquid ; Humans ; *Ion Channel Gating ; Ionomycin/pharmacology ; Mass Spectrometry ; Mutation ; Neurons/physiology ; Patch-Clamp Techniques ; Phosphorylation ; Phosphoserine/metabolism ; Phosphothreonine/metabolism ; Point Mutation ; Rats ; Recombinant Proteins/metabolism ; Serine/genetics ; Shab Potassium Channels/*metabolism ; Transfection
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 52
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    5'-Triphosphate RNA is the ligand for RIG-I (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-10-14
    Description: The structural basis for the distinction of viral RNA from abundant self RNA in the cytoplasm of virally infected cells is largely unknown. We demonstrated that the 5'-triphosphate end of RNA generated by viral polymerases is responsible for retinoic acid-inducible protein I (RIG-I)-mediated detection of RNA molecules. Detection of 5'-triphosphate RNA is abrogated by capping of the 5'-triphosphate end or by nucleoside modification of RNA, both occurring during posttranscriptional RNA processing in eukaryotes. Genomic RNA prepared from a negative-strand RNA virus and RNA prepared from virus-infected cells (but not from noninfected cells) triggered a potent interferon-alpha response in a phosphatase-sensitive manner. 5'-triphosphate RNA directly binds to RIG-I. Thus, uncapped 5'-triphosphate RNA (now termed 3pRNA) present in viruses known to be recognized by RIG-I, but absent in viruses known to be detected by MDA-5 such as the picornaviruses, serves as the molecular signature for the detection of viral infection by RIG-I.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hornung, Veit -- Ellegast, Jana -- Kim, Sarah -- Brzozka, Krzysztof -- Jung, Andreas -- Kato, Hiroki -- Poeck, Hendrik -- Akira, Shizuo -- Conzelmann, Karl-Klaus -- Schlee, Martin -- Endres, Stefan -- Hartmann, Gunther -- New York, N.Y. -- Science. 2006 Nov 10;314(5801):994-7. Epub 2006 Oct 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Clinical Pharmacology, Department of Internal Medicine, University of Munich, 80336 Munich, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17038590" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Cells, Cultured ; Cytosol/metabolism/virology ; DEAD-box RNA Helicases/*metabolism ; DNA-Directed RNA Polymerases/metabolism ; Humans ; Interferon-alpha/biosynthesis ; Interferon-beta/biosynthesis ; Ligands ; Mice ; Monocytes/metabolism ; Oligoribonucleotides/metabolism ; Phosphates/metabolism ; Phosphorylation ; RNA/chemistry/*metabolism ; RNA Caps/metabolism ; RNA, Double-Stranded/chemistry/metabolism ; RNA, Viral/chemistry/*metabolism ; Rabies virus/genetics/immunology/physiology ; Transcription, Genetic ; Transfection ; Viral Proteins/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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    A calcium-regulated MEF2 sumoylation switch controls postsynaptic differentiation (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-02-18
    Description: Postsynaptic differentiation of dendrites is an essential step in synapse formation. We report here a requirement for the transcription factor myocyte enhancer factor 2A (MEF2A) in the morphogenesis of postsynaptic granule neuron dendritic claws in the cerebellar cortex. A transcriptional repressor form of MEF2A that is sumoylated at lysine-403 promoted dendritic claw differentiation. Activity-dependent calcium signaling induced a calcineurin-mediated dephosphorylation of MEF2A at serine-408 and, thereby, promoted a switch from sumoylation to acetylation at lysine-403, which led to inhibition of dendritic claw differentiation. Our findings define a mechanism underlying postsynaptic differentiation that may modulate activity-dependent synapse development and plasticity in the brain.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Shalizi, Aryaman -- Gaudilliere, Brice -- Yuan, Zengqiang -- Stegmuller, Judith -- Shirogane, Takahiro -- Ge, Qingyuan -- Tan, Yi -- Schulman, Brenda -- Harper, J Wade -- Bonni, Azad -- AG11085/AG/NIA NIH HHS/ -- NS41021/NS/NINDS NIH HHS/ -- New York, N.Y. -- Science. 2006 Feb 17;311(5763):1012-7.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Pathology, Harvard Medical School, 77 Louis Pasteur Avenue, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16484498" target="_blank"〉PubMed〈/a〉
    Keywords: Acetylation ; Animals ; Calcineurin/metabolism ; Calcium/*metabolism ; Calcium Signaling ; Cell Differentiation ; Cell Line ; Cerebellar Cortex/cytology/*physiology ; Dendrites/physiology/*ultrastructure ; Electroporation ; Humans ; In Vitro Techniques ; MEF2 Transcription Factors ; Morphogenesis ; Myogenic Regulatory Factors/genetics/*metabolism ; Neurons/*cytology/physiology ; Phosphorylation ; RNA Interference ; Rats ; Recombinant Fusion Proteins/metabolism ; Small Ubiquitin-Related Modifier Proteins/*metabolism ; Synapses/*physiology ; Transcription, Genetic ; Transfection
    Print ISSN: 0036-8075
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    Neuroscience. SUMO wrestles the synapse (2006)
    American Association for the Advancement of Science (AAAS)
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    Publication Date: 2006-02-18
    Description: 〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Beg, Asim A -- Scheiffele, Peter -- New York, N.Y. -- Science. 2006 Feb 17;311(5763):962-3.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Center for Neurobiology and Behavior, Columbia University, New York, NY 10032, USA. ab2516@columbia.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/16484483" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Brain/cytology/*physiology ; Calcium/metabolism ; Calcium Signaling ; Cerebellum/cytology/physiology ; Dendrites/physiology/ultrastructure ; Hippocampus/cytology/physiology ; MEF2 Transcription Factors ; Myogenic Regulatory Factors/genetics/*physiology ; Neurons/*physiology ; Phosphorylation ; RNA Interference ; Rats ; Small Ubiquitin-Related Modifier Proteins/*metabolism ; Synapses/*physiology ; *Transcription, Genetic
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    Brassinosteroid signaling: a paradigm for steroid hormone signaling from the cell surface (2006)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2006-12-02
    Description: Plants use the coordinated action of several small-molecule hormones to grow and develop optimally in response to a changing environment. Among these hormones are the brassinosteroids (BRs), the polyhydroxylated steroid hormones of plants. BRs bind a small family of leucine-rich repeat receptor kinases at the cell surface, thereby initiating an intracellular signal transduction cascade that results in the altered expression of hundreds of genes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Belkhadir, Youssef -- Chory, Joanne -- New York, N.Y. -- Science. 2006 Dec 1;314(5804):1410-1.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Plant Biology Laboratory and Howard Hughes Medical Institute, Salk Institute for Biological Studies, La Jolla, CA 92037, USA. chory@salk.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/17138891" target="_blank"〉PubMed〈/a〉
    Keywords: Arabidopsis/genetics/growth & development/*metabolism ; Arabidopsis Proteins/chemistry/metabolism ; Brassinosteroids ; Cell Membrane/*metabolism ; Cholestanols/*metabolism ; Gene Expression Regulation, Plant ; Models, Biological ; Mutation ; Phosphoprotein Phosphatases/metabolism ; Phosphorylation ; Plant Growth Regulators/chemistry/*metabolism ; Protein Kinases/chemistry/metabolism ; Protein-Serine-Threonine Kinases/metabolism ; Response Elements ; *Signal Transduction ; Steroids/chemistry/*metabolism ; Steroids, Heterocyclic/*metabolism ; Transcription Factors/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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