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  • Chemistry
  • Phosphorylation
  • American Association for the Advancement of Science (AAAS)  (164)
  • Elsevier
  • Silver Spring, MD
  • 1990-1994  (164)
Collection
Keywords
Publisher
  • American Association for the Advancement of Science (AAAS)  (164)
  • Elsevier
  • Silver Spring, MD
  • Wiley-Blackwell  (50,832)
  • Springer  (21)
Years
Year
  • 1
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    An alternative to SH2 domains for binding tyrosine-phosphorylated proteins (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-16
    Description: Src homology 2 (SH2) domains bind specifically to tyrosine-phosphorylated proteins that participate in signaling by growth factors and oncogenes. A protein domain was identified that bound specifically to the tyrosine-phosphorylated form of its target protein but differs from known SH2 sequences. Phosphotyrosine-binding (PTB) domains were found in two proteins: SHC, a protein implicated in signaling through Ras; and SCK, encoded by a previously uncharacterized gene. The PTB domain of SHC specifically bound to a tyrosine-phosphorylated 145-kilodalton protein. PTB domains are an alternative to SH2 domains for specifically recruiting tyrosine-phosphorylated proteins into signaling complexes and are likely to take part in signaling by many growth factors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kavanaugh, W M -- Williams, L T -- K11 HL02714/HL/NHLBI NIH HHS/ -- R01 HL32898/HL/NHLBI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 16;266(5192):1862-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Medicine, University of California, San Francisco 94143.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527937" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; *Adaptor Proteins, Signal Transducing ; *Adaptor Proteins, Vesicular Transport ; Amino Acid Sequence ; Animals ; Cell Line ; Humans ; Mice ; Molecular Sequence Data ; Phosphoproteins/*metabolism ; Phosphorylation ; Phosphotyrosine ; Platelet-Derived Growth Factor/pharmacology ; Protein Binding ; Protein-Tyrosine Kinases/chemistry/metabolism ; Proteins/chemistry/*metabolism ; Shc Signaling Adaptor Proteins ; *Signal Transduction ; Tyrosine/*analogs & derivatives/metabolism
    Print ISSN: 0036-8075
    Electronic ISSN: 1095-9203
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  • 2
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    Association of insulin receptor substrate-1 with integrins (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-12-02
    Description: Insulin stimulation was found to promote association of the alpha v beta 3 integrin (a vitronectin receptor) with insulin receptor substrate-1 (IRS-1), an intracellular protein that mediates insulin signaling by binding other signaling molecules, including growth factor receptor-bound protein 2 (Grb2) and phosphatidylinositol-3' kinase. Insulin-treated cells expressing the alpha v beta 3 integrin showed 2.5 times more DNA synthesis when plated on vitronectin than on other substrates, whereas cells expressing another vitronectin receptor, alpha v beta 5, did not show this difference. The association between integrin and IRS-1 may be a mechanism for the synergistic action of growth factor and extracellular matrix receptors.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Vuori, K -- Ruoslahti, E -- CA 28896/CA/NCI NIH HHS/ -- CA 30199/CA/NCI NIH HHS/ -- CA 42507/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Dec 2;266(5190):1576-8.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Cancer Research Center, La Jolla Cancer Research Foundation, CA 92037.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7527156" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Collagen ; DNA/biosynthesis ; Glycoproteins ; Humans ; Insulin/pharmacology ; Insulin Receptor Substrate Proteins ; Integrins/*metabolism ; Molecular Sequence Data ; Phosphoproteins/*metabolism ; Phosphorylation ; Rats ; Receptor, Insulin ; Receptors, Cytoadhesin/*metabolism ; Receptors, Vitronectin ; Transfection ; Tumor Cells, Cultured ; Vitronectin
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  • 3
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    Activation and regeneration of rhodopsin in the insect visual cycle (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: Light absorption by rhodopsin generates metarhodopsin, which activates heterotrimeric guanine nucleotide-binding proteins (G proteins) in photoreceptor cells of vertebrates and invertebrates. In contrast to vertebrate metarhodopsins, most invertebrate metarhodopsins are thermally stable and regenerate rhodopsin by absorption of a second photon. In experiments with Rh1 Drosophila rhodopsin, the thermal stability of metarhodopsin was found not to be an intrinsic property of the visual pigment but a consequence of its interaction with arrestin (49 kilodaltons). The stabilization of metarhodopsin resulted in a large decrease in the efficiency of G protein activation. Light absorption by thermally stable metarhodopsin initially regenerated an inactive rhodopsin-like intermediate, which was subsequently converted in the dark to active rhodopsin. The accumulation of inactive rhodopsin at higher light levels may represent a mechanism for gain regulation in the insect visual cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Kiselev, A -- Subramaniam, S -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1369-73.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore, MD 21205.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973725" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Antigens/*metabolism ; Arrestin ; Darkness ; Drosophila ; Eye Proteins/*metabolism ; GTP-Binding Proteins/*metabolism ; *Light ; Models, Biological ; Phosphorylation ; Photoreceptor Cells, Invertebrate/*metabolism ; Rhodopsin/*analogs & derivatives/chemistry/*metabolism ; Spectrophotometry, Ultraviolet ; Temperature
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  • 4
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    The PCL2 (ORFD)-PHO85 cyclin-dependent kinase complex: a cell cycle regulator in yeast (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-25
    Description: Cyclin-dependent kinase (cdk) complexes are essential activators of cell cycle progression in all eukaryotes. In contrast to mammalian cells, in which multiple cdk's contribute to cell cycle regulation, the yeast cell cycle is largely controlled by the activity of a single cdk, CDC28. Analysis of the putative G1 cyclin PCL2 (ORFD) identified a second cyclin-cdk complex that contributes to cell cycle progression in yeast. PCL2 interacted with the cdk PHO85 in vivo and in vitro and formed a kinase complex that had G1-periodic activity. Under genetic conditions in which the Start transition was compromised, PHO85 and its associated cyclin subunits were essential for cell cycle commitment. Because PHO85 and another cyclin-like molecule, PHO80, also take part in inorganic phosphate metabolism, this cdk enzyme may integrate responses to nutritional conditions with the cell cycle.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Measday, V -- Moore, L -- Ogas, J -- Tyers, M -- Andrews, B -- New York, N.Y. -- Science. 1994 Nov 25;266(5189):1391-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular and Medical Genetics, University of Toronto, Ontario, Canada.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973731" target="_blank"〉PubMed〈/a〉
    Keywords: CDC28 Protein Kinase, S cerevisiae/metabolism ; Cyclin-Dependent Kinases/*metabolism ; Cyclins/genetics/*metabolism ; *DNA-Binding Proteins ; Fungal Proteins/genetics/*metabolism ; *G1 Phase ; Models, Biological ; Phosphorylation ; Recombinant Fusion Proteins/metabolism ; Saccharomyces cerevisiae/*cytology/growth & development/metabolism ; *Saccharomyces cerevisiae Proteins ; Temperature ; Transcription Factors/metabolism
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  • 5
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    Analysis and expression of a cloned pre-T cell receptor gene (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-18
    Description: The T cell antigen receptor (TCR) beta chain regulates early T cell development in the absence of the TCR alpha chain. The developmentally controlled gene described here encodes the pre-TCR alpha (pT alpha) chain, which covalently associates with TCR beta and with the CD3 proteins forms a pre-TCR complex that transduces signals in immature thymocytes. Unlike the lambda 5 pre-B cell receptor protein, the pT alpha chain is a type I transmembrane protein whose cytoplasmic tail contains two potential phosphorylation sites and a Src homology 3 (SH3)-domain binding sequence. Pre-TCR alpha transfection experiments indicated that surface expression of the pre-TCR is controlled by additional developmentally regulated proteins. Identification of the pT alpha gene represents an essential step in the structure-function analysis of the pre-TCR complex.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Saint-Ruf, C -- Ungewiss, K -- Groettrup, M -- Bruno, L -- Fehling, H J -- von Boehmer, H -- New York, N.Y. -- Science. 1994 Nov 18;266(5188):1208-12.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Unite INSERM 373, Institut Necker, Paris, France.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973703" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Antigens, CD3/metabolism ; Base Sequence ; Cell Line ; *Cloning, Molecular ; DNA, Complementary/genetics ; *Gene Expression Regulation, Developmental ; Gene Rearrangement ; Membrane Glycoproteins/chemistry/*genetics/metabolism ; Mice ; Mice, Inbred C57BL ; Molecular Sequence Data ; Open Reading Frames ; Phosphorylation ; Polymerase Chain Reaction ; Rabbits ; Receptors, Antigen, T-Cell, alpha-beta/chemistry/*genetics/metabolism ; Signal Transduction ; T-Lymphocytes/*immunology ; Transfection
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  • 6
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    Interaction of IL-2R beta and gamma c chains with Jak1 and Jak3: implications for XSCID and XCID (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-11
    Description: Interleukin-2 (IL-2) signaling requires the dimerization of the IL-2 receptor beta.(IL-2R beta) and common gamma (gamma c) chains. Mutations of gamma c can result in X-linked severe combined immunodeficiency (XSCID). IL-2, IL-4, IL-7 (whose receptors are known to contain gamma c), and IL-9 (whose receptor is shown here to contain gamma c) induced the tyrosine phosphorylation and activation of the Janus family tyrosine kinases Jak1 and Jak3. Jak1 and Jak3 associated with IL-2R beta and gamma c, respectively; IL-2 induced Jak3-IL-2R beta and increased Jak3-gamma c associations. Truncations of gamma c, and a gamma c, point mutation causing moderate X-linked combined immunodeficiency (XCID), decreased gamma c-Jak3 association. Thus, gamma c mutations in at least some XSCID and XCID patients prevent normal Jak3 activation, suggesting that mutations of Jak3 may result in an XSCID-like phenotype.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Russell, S M -- Johnston, J A -- Noguchi, M -- Kawamura, M -- Bacon, C M -- Friedmann, M -- Berg, M -- McVicar, D W -- Witthuhn, B A -- Silvennoinen, O -- P30 CA21765/CA/NCI NIH HHS/ -- R01 DK42932/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1042-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Laboratory of Molecular Immunology, National Heart, Lung, and Blood Institute, Bethesda, MD 20892.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973658" target="_blank"〉PubMed〈/a〉
    Keywords: Animals ; Cell Line ; Enzyme Activation ; Humans ; Interleukin-2/pharmacology ; Janus Kinase 1 ; Janus Kinase 3 ; Mutation ; Phosphorylation ; Point Mutation ; Protein-Tyrosine Kinases/genetics/*metabolism ; Receptors, Interleukin-2/genetics/*metabolism ; Severe Combined Immunodeficiency/genetics/*immunology/metabolism ; Transfection ; Tyrosine/metabolism
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  • 7
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    Prevention of T cell anergy by signaling through the gamma c chain of the IL-2 receptor (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-11
    Description: When stimulated through their antigen receptor without requisite costimulation, T cells enter a state of antigen-specific unresponsiveness termed anergy. In this study, signaling through the common gamma chain of the interleukin-2 (IL-2), IL-4, and IL-7 receptors in the presence of antigen was found to be sufficient to prevent the induction of anergy. After culture with IL-2, IL-4, or IL-7, Jak3 kinase was tyrosine-phosphorylated, which correlated with the prevention of anergy. Therefore, a signal through the common gamma chain may regulate the decision of T cells to either clonally expand or enter a state of anergy.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Boussiotis, V A -- Barber, D L -- Nakarai, T -- Freeman, G J -- Gribben, J G -- Bernstein, G M -- D'Andrea, A D -- Ritz, J -- Nadler, L M -- AI 35225/AI/NIAID NIH HHS/ -- CA 40216/CA/NCI NIH HHS/ -- New York, N.Y. -- Science. 1994 Nov 11;266(5187):1039-42.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Division of Hematologic Malignancies, Dana-Farber Cancer Institute, Boston, MA 02115.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973657" target="_blank"〉PubMed〈/a〉
    Keywords: Cell Line ; Clonal Anergy/*immunology ; Clone Cells ; HLA-DR7 Antigen/immunology ; Humans ; Interleukins/immunology ; Janus Kinase 3 ; Lymphocyte Activation ; Phosphorylation ; Protein-Tyrosine Kinases/metabolism ; Receptors, Antigen, T-Cell/metabolism ; Receptors, Interleukin-2/immunology/*metabolism ; *Signal Transduction ; T-Lymphocytes/*immunology/metabolism ; Tumor Necrosis Factor-alpha/immunology
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  • 8
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    Ligands for EPH-related receptor tyrosine kinases that require membrane attachment or clustering for activity (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: The EPH-related transmembrane tyrosine kinases constitute the largest known family of receptor-like tyrosine kinases, with many members displaying specific patterns of expression in the developing and adult nervous system. A family of cell surface-bound ligands exhibiting distinct, but overlapping, specificities for these EPH-related kinases was identified. These ligands were unable to act as conventional soluble factors. However, they did function when presented in membrane-bound form, suggesting that they require direct cell-to-cell contact to activate their receptors. Membrane attachment may serve to facilitate ligand dimerization or aggregation, because antibody-mediated clustering activated previously inactive soluble forms of these ligands.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Davis, S -- Gale, N W -- Aldrich, T H -- Maisonpierre, P C -- Lhotak, V -- Pawson, T -- Goldfarb, M -- Yancopoulos, G D -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):816-9.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Regeneron Pharmaceuticals, Tarrytown, NY 10591.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973638" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Animals ; Cell Line ; Cell Membrane/*metabolism ; *DNA-Binding Proteins ; Ephrin-A1 ; Ephrin-B1 ; Humans ; Ligands ; Membrane Proteins/chemistry/*metabolism ; Molecular Sequence Data ; Neurons/metabolism ; Phosphorylation ; Proteins/chemistry/*metabolism ; *Proto-Oncogene Proteins ; Receptor Protein-Tyrosine Kinases/*metabolism ; *Receptor, EphA5 ; Recombinant Fusion Proteins/metabolism ; Retroviridae Proteins, Oncogenic/*metabolism ; Solubility ; *Transcription Factors ; Transfection ; Tumor Cells, Cultured ; ets-Domain Protein Elk-1
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  • 9
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    Interaction of a protein phosphatase with an Arabidopsis serine-threonine receptor kinase (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-11-04
    Description: A protein phosphatase was cloned that interacts with a serine-threonine receptor-like kinase, RLK5, from Arabidopsis thaliana. The phosphatase, designated KAPP (kinase-associated protein phosphatase), is composed of three domains: an amino-terminal signal anchor, a kinase interaction (KI) domain, and a type 2C protein phosphatase catalytic region. Association of RLK5 with the KI domain is dependent on phosphorylation of RLK5 and can be abolished by dephosphorylation. KAPP may function as a signaling component in a pathway involving RLK5.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Stone, J M -- Collinge, M A -- Smith, R D -- Horn, M A -- Walker, J C -- New York, N.Y. -- Science. 1994 Nov 4;266(5186):793-5.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Missouri-Columbia 65211.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7973632" target="_blank"〉PubMed〈/a〉
    Keywords: Amino Acid Sequence ; Arabidopsis/*enzymology/genetics ; *Arabidopsis Proteins ; Blotting, Southern ; Catalysis ; Genes, Plant ; Molecular Sequence Data ; Phosphoprotein Phosphatases/chemistry/genetics/*metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases/*metabolism ; Sequence Homology, Amino Acid ; Signal Transduction
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  • 10
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    PHAS-I as a link between mitogen-activated protein kinase and translation initiation (1994)
    American Association for the Advancement of Science (AAAS)
    Details
    Publication Date: 1994-10-28
    Description: PHAS-I is a heat-stable protein (relative molecular mass approximately 12,400) found in many tissues. It is rapidly phosphorylated in rat adipocytes incubated with insulin or growth factors. Nonphosphorylated PHAS-I bound to initiation factor 4E (eIF-4E) and inhibited protein synthesis. Serine-64 in PHAS-I was rapidly phosphorylated by mitogen-activated (MAP) kinase, the major insulin-stimulated PHAS-I kinase in adipocyte extracts. Results obtained with antibodies, immobilized PHAS-I, and a messenger RNA cap affinity resin indicated that PHAS-I did not bind eIF-4E when serine-64 was phosphorylated. Thus, PHAS-I may be a key mediator of the stimulation of protein synthesis by the diverse group of agents and stimuli that activate MAP kinase.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Lin, T A -- Kong, X -- Haystead, T A -- Pause, A -- Belsham, G -- Sonenberg, N -- Lawrence, J C Jr -- AR41180/AR/NIAMS NIH HHS/ -- DK28312/DK/NIDDK NIH HHS/ -- New York, N.Y. -- Science. 1994 Oct 28;266(5185):653-6.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Molecular Biology and Pharmacology, Washington University School of Medicine, St. Louis, MO 63110.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7939721" target="_blank"〉PubMed〈/a〉
    Keywords: 3T3 Cells ; Adipocytes/metabolism ; Animals ; *Carrier Proteins ; Insulin/*pharmacology ; Mice ; Mitogen-Activated Protein Kinase 1 ; Peptide Initiation Factors/isolation & purification/*metabolism ; Phosphoproteins/*metabolism ; Phosphorylation ; *Protein Biosynthesis ; Protein-Serine-Threonine Kinases/*metabolism ; Protein-Tyrosine Kinases/*metabolism ; Rats ; Recombinant Proteins/metabolism ; Serine/metabolism
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    Topics: Biology , Chemistry and Pharmacology , Computer Science , Medicine , Natural Sciences in General , Physics
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