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  • Recombinant Fusion Proteins/metabolism  (8)
  • American Association for the Advancement of Science (AAAS)  (8)
  • American Geophysical Union (AGU)
  • 2000-2004  (8)
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Keywords
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  • American Association for the Advancement of Science (AAAS)  (8)
  • American Geophysical Union (AGU)
Years
Year
  • 1
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    VirB/D4-dependent protein translocation from Agrobacterium into plant cells (2000)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2000-11-04
    Description: The Agrobacterium VirB/D4 transport system mediates the transfer of a nucleoprotein T complex into plant cells, leading to crown gall disease. In addition, several Virulence proteins must somehow be transported to fulfill a function in planta. Here, we used fusions between Cre recombinase and VirE2 or VirF to directly demonstrate protein translocation into plant cells. Transport of the proteins was monitored by a Cre-mediated in planta recombination event resulting in a selectable phenotype and depended on the VirB/D4 transport system but did not require transferred DNA.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vergunst, A C -- Schrammeijer, B -- den Dulk-Ras, A -- de Vlaam, C M -- Regensburg-Tuink, T J -- Hooykaas, P J -- New York, N.Y. -- Science. 2000 Nov 3;290(5493):979-82.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Molecular Plant Sciences, Leiden University, Clusius Laboratory, Wassenaarseweg 64, 2333 AL, Leiden, Netherlands.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11062129" target="_blank"〉PubMed〈/a〉
    Keywords: Agrobacterium tumefaciens/genetics/*metabolism/pathogenicity ; Arabidopsis/genetics/*metabolism/microbiology ; Bacterial Proteins/*metabolism ; DNA, Bacterial/genetics/metabolism ; DNA-Binding Proteins/*metabolism ; Drug Resistance ; Integrases/genetics/*metabolism ; *Ion Channels ; Kanamycin/pharmacology ; Plant Roots/metabolism ; Plants, Genetically Modified ; Plasmids ; Polymerase Chain Reaction ; *Protein Transport ; Recombinant Fusion Proteins/metabolism ; *Viral Proteins ; Virulence ; *Virulence Factors
    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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    G-protein signaling through tubby proteins (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-05-26
    Description: Dysfunction of the tubby protein results in maturity-onset obesity in mice. Tubby has been implicated as a transcription regulator, but details of the molecular mechanism underlying its function remain unclear. Here we show that tubby functions in signal transduction from heterotrimeric GTP-binding protein (G protein)-coupled receptors. Tubby localizes to the plasma membrane by binding phosphatidylinositol 4,5-bisphosphate through its carboxyl terminal "tubby domain." X-ray crystallography reveals the atomic-level basis of this interaction and implicates tubby domains as phosphorylated-phosphatidyl- inositol binding factors. Receptor-mediated activation of G protein alphaq (Galphaq) releases tubby from the plasma membrane through the action of phospholipase C-beta, triggering translocation of tubby to the cell nucleus. The localization of tubby-like protein 3 (TULP3) is similarly regulated. These data suggest that tubby proteins function as membrane-bound transcription regulators that translocate to the nucleus in response to phosphoinositide hydrolysis, providing a direct link between G-protein signaling and the regulation of gene expression.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Santagata, S -- Boggon, T J -- Baird, C L -- Gomez, C A -- Zhao, J -- Shan, W S -- Myszka, D G -- Shapiro, L -- New York, N.Y. -- Science. 2001 Jun 15;292(5524):2041-50. Epub 2001 May 24.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Ruttenberg Cancer Center, Structural Biology Program, Department of Physiology and Biophysics, Mount Sinai School of Medicine of New York University, 1425 Madison Avenue New York, NY 10029, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11375483" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; Adaptor Proteins, Signal Transducing ; Amino Acid Sequence ; Animals ; Cell Membrane/metabolism ; Cell Nucleus/*metabolism ; Cells, Cultured ; Crystallography, X-Ray ; GTP-Binding Protein alpha Subunits, Gq-G11 ; Gene Expression Regulation ; Heterotrimeric GTP-Binding Proteins/*metabolism ; Humans ; Isoenzymes/*metabolism ; Membrane Lipids/metabolism ; Mice ; Models, Biological ; Molecular Sequence Data ; Nuclear Localization Signals ; Obesity/genetics/metabolism ; Phosphatidylinositol 4,5-Diphosphate/*metabolism ; Phosphatidylinositol Phosphates/metabolism ; Phospholipase C beta ; Phosphorylation ; Protein Structure, Tertiary ; Proteins/chemistry/genetics/*metabolism ; Receptor, Serotonin, 5-HT2C ; Receptors, Muscarinic/metabolism ; Receptors, Serotonin/metabolism ; Recombinant Fusion Proteins/metabolism ; *Signal Transduction ; Transcription Factors/chemistry/genetics/*metabolism ; Type C Phospholipases/*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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    Single-molecule speckle analysis of actin filament turnover in lamellipodia (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-02-09
    Description: Lamellipodia are thin, veil-like extensions at the edge of cells that contain a dynamic array of actin filaments. We describe an approach for analyzing spatial regulation of actin polymerization and depolymerization in vivo in which we tracked single molecules of actin fused to the green fluorescent protein. Polymerization and the lifetime of actin filaments in lamellipodia were measured with high spatial precision. Basal polymerization and depolymerization occurred throughout lamellipodia with largely constant kinetics, and polymerization was promoted within one micron of the lamellipodium tip. Most of the actin filaments in the lamellipodium were generated by polymerization away from the tip.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Watanabe, Naoki -- Mitchison, Timothy J -- GM48027/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Feb 8;295(5557):1083-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell Biology, Harvard Medical School, Boston, MA 02115, USA. naoki_watanabe@hms.harvard.edu〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11834838" target="_blank"〉PubMed〈/a〉
    Keywords: Actin Cytoskeleton/drug effects/*metabolism/ultrastructure ; Actin-Related Protein 2 ; Actin-Related Protein 3 ; Actins/*metabolism ; Animals ; Biopolymers ; Cell Line ; *Cytoskeletal Proteins ; *Depsipeptides ; Fibroblasts ; Fluorescence ; Green Fluorescent Proteins ; Half-Life ; Luminescent Proteins ; Models, Biological ; Peptides, Cyclic/pharmacology ; Pseudopodia/*metabolism/ultrastructure ; Recombinant Fusion Proteins/metabolism ; Xenopus
    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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    Fusion of cells by flipped SNAREs (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-06-14
    Description: The SNARE (soluble N-ethylmaleimide-sensitive factor attachment protein receptor) hypothesis suggests that pairs of proteins known as vesicle (v-) SNAREs and target membrane (t-) SNAREs interact specifically to control and mediate intracellular membrane fusion events. Here, cells expressing the interacting domains of v- and t-SNAREs on the cell surface were found to fuse spontaneously, demonstrating that SNAREs are sufficient to fuse biological membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hu, Chuan -- Ahmed, Mahiuddin -- Melia, Thomas J -- Sollner, Thomas H -- Mayer, Thomas -- Rothman, James E -- New York, N.Y. -- Science. 2003 Jun 13;300(5626):1745-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cellular Biochemistry and Biophysics Program, Memorial Sloan-Kettering Cancer Center, 1275 York Avenue, Box 251, New York, NY 10021, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12805548" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens, Surface/chemistry/*metabolism ; COS Cells ; *Cell Fusion ; Cell Membrane/*metabolism ; Cercopithecus aethiops ; Endoplasmic Reticulum/metabolism ; Glycosylation ; Membrane Fusion/physiology ; Membrane Proteins/chemistry/genetics/*metabolism ; Mutation ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Protein Binding ; Protein Folding ; Protein Structure, Tertiary ; R-SNARE Proteins ; Recombinant Fusion Proteins/metabolism ; Synaptosomal-Associated Protein 25 ; Syntaxin 1 ; Transfection
    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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    A functional screen for the type III (Hrp) secretome of the plant pathogen Pseudomonas syringae (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-03-02
    Description: Type III secreted "effector" proteins of bacterial pathogens play central roles in virulence, yet are notoriously difficult to identify. We used an in vivo genetic screen to identify 13 effectors secreted by the type III apparatus (called Hrp, for "hypersensitive response and pathogenicity") of the plant pathogen Pseudomonas syringae. Although sharing little overall homology, the amino-terminal regions of these effectors had strikingly similar amino acid compositions. This feature facilitated the bioinformatic prediction of 38 P. syringae effectors, including 15 previously unknown proteins. The secretion of two of these putative effectors was shown to be type III--dependent. Effectors showed high interstrain variation, supporting a role for some effectors in adaptation to different hosts.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Guttman, David S -- Vinatzer, Boris A -- Sarkar, Sara F -- Ranall, Max V -- Kettler, Gregory -- Greenberg, Jean T -- GM020024/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Mar 1;295(5560):1722-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Botany, University of Toronto, 25 Willcocks Street, Toronto, ON M5S 3B2, Canada. guttman@botany.utoronto.ca〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11872842" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acids/analysis ; Arabidopsis/genetics/metabolism/*microbiology ; *Arabidopsis Proteins ; Bacterial Proteins/chemistry/*genetics/*metabolism ; Computational Biology ; DNA Transposable Elements ; *Genes, Bacterial ; Genomics ; Molecular Sequence Data ; Plant Proteins/metabolism ; Promoter Regions, Genetic ; Proteome ; Pseudomonas/*genetics/*metabolism/pathogenicity ; Recombinant Fusion Proteins/metabolism ; Virulence
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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  • 6
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    Cell cycle regulation of myosin-V by calcium/calmodulin-dependent protein kinase II (2001)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2001-08-18
    Description: Organelle transport by myosin-V is down-regulated during mitosis, presumably by myosin-V phosphorylation. We used mass spectrometry phosphopeptide mapping to show that the tail of myosin-V was phosphorylated in mitotic Xenopus egg extract on a single serine residue localized in the carboxyl-terminal organelle-binding domain. Phosphorylation resulted in the release of the motor from the organelle. The phosphorylation site matched the consensus sequence of calcium/calmodulin-dependent protein kinase II (CaMKII), and inhibitors of CaMKII prevented myosin-V release. The modulation of cargo binding by phosphorylation is likely to represent a general mechanism regulating organelle transport by myosin-V.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Karcher, R L -- Roland, J T -- Zappacosta, F -- Huddleston, M J -- Annan, R S -- Carr, S A -- Gelfand, V I -- GM-52111/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2001 Aug 17;293(5533):1317-20.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Cell and Structural Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/11509731" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Amino Acid Substitution ; Animals ; Biological Transport ; Calcium-Calmodulin-Dependent Protein Kinase Type 2 ; Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/*metabolism ; Calmodulin-Binding Proteins/chemistry/genetics/*metabolism ; Cell Extracts ; Egtazic Acid/analogs & derivatives/pharmacology ; Enzyme Inhibitors/pharmacology ; Interphase ; Mass Spectrometry ; Melanophores/metabolism/ultrastructure ; Melanosomes/*metabolism ; *Mitosis ; Molecular Motor Proteins/*metabolism ; Molecular Sequence Data ; Mutation ; *Myosin Type V ; Nerve Tissue Proteins/chemistry/genetics/*metabolism ; Ovum ; Peptides/pharmacology ; Phosphopeptides/analysis/metabolism ; Phosphorylation ; Phosphoserine/metabolism ; Recombinant Fusion Proteins/metabolism ; Transfection ; Xenopus
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 7
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    Separable roles for rent1/hUpf1 in altered splicing and decay of nonsense transcripts (2002)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2002-09-14
    Description: The mechanism by which disruption of reading frame can influence pre-messenger RNA (pre-mRNA) processing is poorly understood. We assessed the role of factors essential for nonsense-mediated mRNA decay (NMD) in nonsense-mediated altered splicing (NAS) with the use of RNA interference (RNAi) in mammalian cells. Inhibition of rent1/hUpf1 expression abrogated both NMD and NAS of nonsense T cell receptor beta transcripts. In contrast, inhibition of rent2/hUpf2 expression did not disrupt NAS despite achieving comparable stabilization of nonsense transcripts. We also demonstrate that NAS and NMD are genetically separable functions of rent1/hUpf1. Additionally, rent1/hUpf1 enters the nucleus where it may directly influence early events in mRNA biogenesis. This provides compelling evidence that NAS relies on a component of the nonsense surveillance machinery but is not an indirect consequence of NMD.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Mendell, Joshua T -- ap Rhys, Colette M J -- Dietz, Harry C -- GM55239/GM/NIGMS NIH HHS/ -- New York, N.Y. -- Science. 2002 Oct 11;298(5592):419-22. Epub 2002 Sep 12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Institute of Genetic Medicine and Howard Hughes Medical Institute, Johns Hopkins University School of Medicine, 858 Ross Building, 720 Rutland Avenue, Baltimore, MD 21205, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12228722" target="_blank"〉PubMed〈/a〉
    Keywords: Active Transport, Cell Nucleus ; *Alternative Splicing ; Amino Acid Substitution ; Blotting, Northern ; Cell Nucleus/metabolism ; *Codon, Nonsense ; Cytoplasm/metabolism ; Equilibrative-Nucleoside Transporter 2/genetics/metabolism ; Fatty Acids, Unsaturated/pharmacology ; Gene Silencing ; Genes, T-Cell Receptor beta ; HeLa Cells ; Humans ; Mutation ; RNA Helicases/genetics/*metabolism ; RNA, Messenger/genetics/*metabolism ; RNA, Small Interfering/metabolism ; Recombinant Fusion Proteins/metabolism ; Trans-Activators/genetics/*metabolism ; Transcription Factors/genetics/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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  • 8
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    BAX and BAK regulation of endoplasmic reticulum Ca2+: a control point for apoptosis (2003)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 2003-03-08
    Description: BAX and BAK are "multidomain" proapoptotic proteins that initiate mitochondrial dysfunction but also localize to the endoplasmic reticulum (ER). Mouse embryonic fibroblasts deficient for BAX and BAK (DKO cells) were found to have a reduced resting concentration of calcium in the ER ([Ca2+]er) that results in decreased uptake of Ca2+ by mitochondria after Ca2+ release from the ER. Expression of SERCA (sarcoplasmic-endoplasmic reticulum Ca2+ adenosine triphosphatase) corrected [Ca2+]er and mitochondrial Ca2+ uptake in DKO cells, restoring apoptotic death in response to agents that release Ca2+ from intracellular stores (such as arachidonic acid, C2-ceramide, and oxidative stress). In contrast, targeting of BAX to mitochondria selectively restored apoptosis to "BH3-only" signals. A third set of stimuli, including many intrinsic signals, required both ER-released Ca2+ and the presence of mitochondrial BAX or BAK to fully restore apoptosis. Thus, BAX and BAK operate in both the ER and mitochondria as an essential gateway for selected apoptotic signals.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Scorrano, Luca -- Oakes, Scott A -- Opferman, Joseph T -- Cheng, Emily H -- Sorcinelli, Mia D -- Pozzan, Tullio -- Korsmeyer, Stanley J -- R37CA50239/CA/NCI NIH HHS/ -- T32HL07627/HL/NHLBI NIH HHS/ -- TCP02016/Telethon/Italy -- New York, N.Y. -- Science. 2003 Apr 4;300(5616):135-9. Epub 2003 Mar 6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Howard Hughes Medical Institute, Dana-Farber Cancer Institute, Brigham and Women's Hospital, Department of Pathology and Medicine, Harvard Medical School, Boston, MA 02115, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/12624178" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; *Apoptosis ; Arachidonic Acid/pharmacology ; Calcium/*metabolism ; Calcium Signaling ; Calcium-Transporting ATPases/metabolism ; Cell Fractionation ; Cell Line, Transformed ; Cells, Cultured ; Endoplasmic Reticulum/*metabolism ; Histamine/pharmacology ; Hydrogen Peroxide/pharmacology ; Ionomycin/pharmacology ; Membrane Proteins/*metabolism ; Mice ; Mice, Knockout ; Microscopy, Confocal ; Microscopy, Immunoelectron ; Mitochondria/metabolism ; Proto-Oncogene Proteins/*metabolism ; *Proto-Oncogene Proteins c-bcl-2 ; Recombinant Fusion Proteins/metabolism ; Sarcoplasmic Reticulum Calcium-Transporting ATPases ; Sphingosine/*analogs & derivatives/pharmacology ; bcl-2 Homologous Antagonist-Killer Protein ; bcl-2-Associated X Protein
    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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