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Volumn 7, Issue 4, 1996, Pages 543-550

Insulin-induced tyrosine phosphorylation of a M(r) 70,000 protein revealed by association with the Src homology 2 (SH2) and SH3 domains of p120GAP and Grb2

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; INSULIN RECEPTOR; PROTEIN TYROSINE KINASE;

EID: 0029829795     PISSN: 10449523     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (8)

References (46)
  • 1
    • 0023188325 scopus 로고
    • After insulin binds
    • Washington DC
    • Rosen, O. M. After insulin binds. Science (Washington DC), 237: 1452-1458, 1987.
    • (1987) Science , vol.237 , pp. 1452-1458
    • Rosen, O.M.1
  • 2
    • 0023834406 scopus 로고
    • A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor
    • White, M. F., Shoelson, S. E., Keutmann, H., and Kahn, C. R. A cascade of tyrosine autophosphorylation in the β-subunit activates the phosphotransferase of the insulin receptor. J. Biol. Chem., 263: 2969-2980, 1988.
    • (1988) J. Biol. Chem. , vol.263 , pp. 2969-2980
    • White, M.F.1    Shoelson, S.E.2    Keutmann, H.3    Kahn, C.R.4
  • 4
    • 0027466903 scopus 로고
    • Insulin-induced phosphorylation of the 46- And 52-kDa Shc proteins
    • Pronk, G. J., McGlade, J., Pelicci, G., Pawson, T., and Bos, J L. Insulin-induced phosphorylation of the 46- and 52-kDa Shc proteins. J. Biol. Chem., 268: 5748-5753, 1993
    • (1993) J. Biol. Chem. , vol.268 , pp. 5748-5753
    • Pronk, G.J.1    McGlade, J.2    Pelicci, G.3    Pawson, T.4    Bos, J.L.5
  • 5
    • 0026627960 scopus 로고
    • Identification of murine homologues of the Orosophila son of sevenless gene: Potential activators of ras
    • Bowtell, D., Fu, P., Simon, M., and Senior, P. Identification of murine homologues of the Orosophila son of sevenless gene: potential activators of ras. Proc Natl. Acad. Sci. USA, 89: 6511-6515, 1992.
    • (1992) Proc Natl. Acad. Sci. USA , vol.89 , pp. 6511-6515
    • Bowtell, D.1    Fu, P.2    Simon, M.3    Senior, P.4
  • 6
    • 0027153103 scopus 로고
    • ras through the formation of a complex of receptor, Grb2 adaptor protein, and SOS nucleotide exchange factor
    • ras through the formation of a complex of receptor, Grb2 adaptor protein, and SOS nucleotide exchange factor. Cell, 73: 611-620, 1993.
    • (1993) Cell , vol.73 , pp. 611-620
    • Buday, L.1    Downward, J.2
  • 8
    • 0027910431 scopus 로고
    • Association of SOS Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation
    • Egan, S. E , Giddings, B. W., Brooks, M. W., Buday, L., Sizeland, A. M., and Weinberg, R. A. Association of SOS Ras exchange protein with Grb2 is implicated in tyrosine kinase signal transduction and transformation. Nature (Lond.), 363: 45-51, 1993.
    • (1993) Nature (Lond.) , vol.363 , pp. 45-51
    • Egan, S.E.1    Giddings, B.W.2    Brooks, M.W.3    Buday, L.4    Sizeland, A.M.5    Weinberg, R.A.6
  • 10
    • 0027294981 scopus 로고
    • The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSOS1
    • Rozakis-Adcock, M., Fernley, R., Wade, J., Pawson, T., and Bowtell, D. The SH2 and SH3 domains of mammalian Grb2 couple the EGF receptor to the Ras activator mSOS1. Nature (Lond.), 363: 83-85, 1993.
    • (1993) Nature (Lond.) , vol.363 , pp. 83-85
    • Rozakis-Adcock, M.1    Fernley, R.2    Wade, J.3    Pawson, T.4    Bowtell, D.5
  • 12
    • 0027288587 scopus 로고
    • The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: Implications for insulin control of ras signalling
    • Skolnik, E. Y., Lee, C. H., Batzer, A., Vicentini, L. M., Zhou, M., Daly, R., Myers, M. J. J., Backer, J. M., Ullrich, A., White, M. F., and Schlessinger, J. The SH2/SH3 domain-containing protein GRB2 interacts with tyrosine-phosphorylated IRS1 and Shc: implications for insulin control of ras signalling. EMBO J., 12: 1929-1936, 1993.
    • (1993) EMBO J. , vol.12 , pp. 1929-1936
    • Skolnik, E.Y.1    Lee, C.H.2    Batzer, A.3    Vicentini, L.M.4    Zhou, M.5    Daly, R.6    Myers, M.J.J.7    Backer, J.M.8    Ullrich, A.9    White, M.F.10    Schlessinger, J.11
  • 14
    • 0027158159 scopus 로고
    • The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp
    • Kuhné, M. R., Pawson, T., Lienhard, G. E., and Feng, G. S. The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp. J. Biol. Chem., 268: 11479-11481, 1993.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11479-11481
    • Kuhné, M.R.1    Pawson, T.2    Lienhard, G.E.3    Feng, G.S.4
  • 15
    • 0027411585 scopus 로고
    • SH2 domains exhibit high affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange
    • Felder, S., Zhou, M., Hu, P., Ullrich, A., Chaudhuri, M., White, M., Shoelson, S. E., and Schlessinger, J. SH2 domains exhibit high affinity binding to tyrosine-phosphorylated peptides yet also exhibit rapid dissociation and exchange. Mol. Cell. Biol., 13: 1449-1455, 1993.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 1449-1455
    • Felder, S.1    Zhou, M.2    Hu, P.3    Ullrich, A.4    Chaudhuri, M.5    White, M.6    Shoelson, S.E.7    Schlessinger, J.8
  • 16
    • 0025765803 scopus 로고
    • SH2 and SH3 domains. elements that control interactions of cytoplasmic signaling proteins
    • Washington DC
    • Koch, C. A., Anderson, D., Moran, M. F., Ellis C., and Pawson, T SH2 and SH3 domains. elements that control interactions of cytoplasmic signaling proteins. Science (Washington DC), 252: 668-674, 1991.
    • (1991) Science , vol.252 , pp. 668-674
    • Koch, C.A.1    Anderson, D.2    Moran, M.F.3    Ellis, C.4    Pawson, T.5
  • 18
    • 0023135248 scopus 로고
    • Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes
    • Bernier, M., Laird, D. M., and Lane, M D Insulin-activated tyrosine phosphorylation of a 15-kilodalton protein in intact 3T3-L1 adipocytes. Proc. Natl. Acad. Sci. USA, 84: 1844-1848, 1987.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 1844-1848
    • Bernier, M.1    Laird, D.M.2    Lane, M.D.3
  • 19
    • 0021997899 scopus 로고
    • Evidence for the involvement of vicinal sulfhydryl groups in insulin-activated hexose transport by 3T3-L1 adipocytes
    • Frost, S. C., and Lane, M. D Evidence for the involvement of vicinal sulfhydryl groups in insulin-activated hexose transport by 3T3-L1 adipocytes. J. Biol. Chem., 260: 2646-2652, 1985.
    • (1985) J. Biol. Chem. , vol.260 , pp. 2646-2652
    • Frost, S.C.1    Lane, M.D.2
  • 20
    • 0023655364 scopus 로고
    • Effect of phenylarsine oxide on insulin-dependent protein phosphorylation and glucose transport in 3T3-L1 Adipocytes
    • Frost, S. C., Kohanski, R. A., and Lane, M. D. Effect of phenylarsine oxide on insulin-dependent protein phosphorylation and glucose transport in 3T3-L1 Adipocytes. J. Biol. Chem., 262: 9872-9876, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 9872-9876
    • Frost, S.C.1    Kohanski, R.A.2    Lane, M.D.3
  • 21
    • 0025860032 scopus 로고
    • Phosphotyrosyl turnover in insulin signaling
    • Liao, K., Hoffman, R. D., and Lane, M. D. Phosphotyrosyl turnover in insulin signaling. J. Biol. Chem., 266: 6544-6553, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 6544-6553
    • Liao, K.1    Hoffman, R.D.2    Lane, M.D.3
  • 23
    • 0025718750 scopus 로고
    • Insulin-induced p21ras activation does not require protein kinase C, but a protein sensitive to phenylarsine oxide
    • Medema, R. H., Burgering, B. M T., and Bos, J. L Insulin-induced p21ras activation does not require protein kinase C, but a protein sensitive to phenylarsine oxide. J. Biol. Chem., 266: 21186-21189, 1991.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21186-21189
    • Medema, R.H.1    Burgering, B.M.T.2    Bos, J.L.3
  • 24
    • 0028124504 scopus 로고
    • Role of SH-PTP2, a protein tyrosine phosphatase with src homology 2 domains, in insulin-stimulated ras activation
    • Noguchi, T., Matozaki, T., Horita, K., Fujioka, Y., and Kasuga, M. Role of SH-PTP2, a protein tyrosine phosphatase with src homology 2 domains, in insulin-stimulated ras activation. Mol. Cell. Biol., 14: 6674-6682, 1994.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 6674-6682
    • Noguchi, T.1    Matozaki, T.2    Horita, K.3    Fujioka, Y.4    Kasuga, M.5
  • 25
    • 0027531637 scopus 로고
    • SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases
    • Washington DC
    • Feng, G. S., Hui, C C., and Pawson, T. SH2-containing phosphotyrosine phosphatase as a target of protein-tyrosine kinases. Science (Washington DC), 259: 1607-1611, 1993.
    • (1993) Science , vol.259 , pp. 1607-1611
    • Feng, G.S.1    Hui, C.C.2    Pawson, T.3
  • 26
    • 0025008074 scopus 로고
    • Paxillin: A new vinculin-binding protein present in focal adhesions
    • Turner, C. E., Glenney, J. R. J , and Burridge, K. Paxillin: a new vinculin-binding protein present in focal adhesions. J. Cell Biol., 111: 1059-1068, 1990.
    • (1990) J. Cell Biol. , vol.111 , pp. 1059-1068
    • Turner, C.E.1    Glenney, J.R.J.2    Burridge, K.3
  • 27
    • 0024382967 scopus 로고
    • Direct activation of the serine/threonine kinase activity of raf-1 through tyrosine phosphorylation by the PDGF b-receptor
    • Morrison, D. K., Kaplan, D. R., Escobedo, J. A., Rapp, U R., Roberts, T. M., and Williams, L. T. Direct activation of the serine/threonine kinase activity of raf-1 through tyrosine phosphorylation by the PDGF b-receptor. Cell, 58: 649-657, 1989.
    • (1989) Cell , vol.58 , pp. 649-657
    • Morrison, D.K.1    Kaplan, D.R.2    Escobedo, J.A.3    Rapp, U.R.4    Roberts, T.M.5    Williams, L.T.6
  • 28
    • 0026011855 scopus 로고
    • Interleukin 2 induces tyrosine phosphorylation and activation of p72-74 Raf-1 kinase in a T-cell line
    • Turner, B., Rapp, U. R., App, H., Greene, M., Dobashi, K., and Reed, J. Interleukin 2 induces tyrosine phosphorylation and activation of p72-74 Raf-1 kinase in a T-cell line. Proc. Natl. Acad. Sci. USA, 88: 1227-1231, 1991.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 1227-1231
    • Turner, B.1    Rapp, U.R.2    App, H.3    Greene, M.4    Dobashi, K.5    Reed, J.6
  • 30
    • 0026697169 scopus 로고
    • Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62
    • Wong, G., Müller, O., Clark, R., Conroy, L., Moran, M. F., Polakis, P., and McCormick, F. Molecular cloning and nucleic acid binding properties of the GAP-associated tyrosine phosphoprotein p62. Cell, 69: 551-558, 1992.
    • (1992) Cell , vol.69 , pp. 551-558
    • Wong, G.1    Müller, O.2    Clark, R.3    Conroy, L.4    Moran, M.F.5    Polakis, P.6    McCormick, F.7
  • 31
    • 0028947757 scopus 로고
    • Association of p62, a multifunctional SH2-and SH3-domain-binding protein, with src family tyrosine kinases, Grb2 and phospholipase Cγ
    • Richard, S., Yu, D., Blumer, K. J., Hausladen, D., Olszowy, M. W , Connely, P. A., and Shaw, A. S. Association of p62, a multifunctional SH2-and SH3-domain-binding protein, with src family tyrosine kinases, Grb2 and phospholipase Cγ. Mol. Cell. Biol., 15: 186-197, 1995.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 186-197
    • Richard, S.1    Yu, D.2    Blumer, K.J.3    Hausladen, D.4    Olszowy, M.W.5    Connely, P.A.6    Shaw, A.S.7
  • 32
    • 0028329195 scopus 로고
    • An RNA-binding protein associated with src through its SH2 and SH3 domains in mitosis
    • Taylor, S. J., and Shalloway, D. An RNA-binding protein associated with src through its SH2 and SH3 domains in mitosis. Nature (Lond.), 368: 867-870, 1994.
    • (1994) Nature (Lond.) , vol.368 , pp. 867-870
    • Taylor, S.J.1    Shalloway, D.2
  • 34
    • 0028894021 scopus 로고
    • Association of the vav-oncogene product with poly(rC)-specific RNA-binding proteins
    • Bustelo, X. R., Suen, K. L., Michael, W. M., Dreyfuss, G., and Barbacid, M. Association of the vav-oncogene product with poly(rC)-specific RNA-binding proteins. Mol. Cell. Biol., 15: 1324-1332, 1995
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1324-1332
    • Bustelo, X.R.1    Suen, K.L.2    Michael, W.M.3    Dreyfuss, G.4    Barbacid, M.5
  • 35
    • 0028216121 scopus 로고
    • Identification, molecular cloning, expression and chromosome mapping of a family of transformation up-regulated hnRNP-K proteins derived by alternative splicing
    • Dejgaard, K., Leffers, H., Rasmussen, H. H., Madsen, P., Kruse, T. A., Gesser, B., Nielsen, H., and Cells, J. E. Identification, molecular cloning, expression and chromosome mapping of a family of transformation up-regulated hnRNP-K proteins derived by alternative splicing. J. Mol. Biol., 236: 33-48, 1994.
    • (1994) J. Mol. Biol. , vol.236 , pp. 33-48
    • Dejgaard, K.1    Leffers, H.2    Rasmussen, H.H.3    Madsen, P.4    Kruse, T.A.5    Gesser, B.6    Nielsen, H.7    Cells, J.E.8
  • 36
    • 0026515523 scopus 로고
    • Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein
    • Matunis, M. J., Michael, W. M., and Dreyfuss, G. Characterization and primary structure of the poly(C)-binding heterogeneous nuclear ribonucleoprotein complex K protein. Mol. Cell. Biol., 12: 164-171, 1992.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 164-171
    • Matunis, M.J.1    Michael, W.M.2    Dreyfuss, G.3
  • 37
    • 0027238531 scopus 로고
    • The human hnRNP M proteins: Identification of a methionine/arginine-rich repeat motif in ribonucleoproteins
    • Datar, K. V., Dreyfuss, G., and Swanson, M. S. The human hnRNP M proteins: identification of a methionine/arginine-rich repeat motif in ribonucleoproteins. Nucleic Acids Res., 21: 439-446, 1993.
    • (1993) Nucleic Acids Res. , vol.21 , pp. 439-446
    • Datar, K.V.1    Dreyfuss, G.2    Swanson, M.S.3
  • 38
    • 0025893215 scopus 로고
    • Characterization of cDNAs encoding the polypyrimidine tract-binding protein
    • Gil, A., Sharp, P. A., Jamison, S. F., and Garcia-Blanco, M. A. Characterization of cDNAs encoding the polypyrimidine tract-binding protein. Genes & Dev., 5: 1224-1236, 1991.
    • (1991) Genes & Dev. , vol.5 , pp. 1224-1236
    • Gil, A.1    Sharp, P.A.2    Jamison, S.F.3    Garcia-Blanco, M.A.4
  • 39
    • 0024835141 scopus 로고
    • A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts
    • Pinol-Roma, S., Swanson, M. S., Gall, J. G., and Dreyfuss, G. A novel heterogeneous nuclear RNP protein with a unique distribution on nascent transcripts. J. Cell Biol., 109: 2575-2587, 1989.
    • (1989) J. Cell Biol. , vol.109 , pp. 2575-2587
    • Pinol-Roma, S.1    Swanson, M.S.2    Gall, J.G.3    Dreyfuss, G.4
  • 42
    • 0027408247 scopus 로고
    • Identification of a ten-amino acid proline-rich SH3 binding site
    • Washington DC
    • Ren, R., Mayer, B. J., Cicchetti, P., and Baltimore, D. Identification of a ten-amino acid proline-rich SH3 binding site. Science (Washington DC), 259: 1157-1161, 1993.
    • (1993) Science , vol.259 , pp. 1157-1161
    • Ren, R.1    Mayer, B.J.2    Cicchetti, P.3    Baltimore, D.4
  • 45
    • 0028232158 scopus 로고
    • Role of p85 subunit of phosphatidylinositol-3-kinase as an adaptor molecule linking the insulin receptor p62 and GTPase activating protein
    • Sung, C. K., Sanchez-Margalet, V., and Goldfine, I. D. Role of p85 subunit of phosphatidylinositol-3-kinase as an adaptor molecule linking the insulin receptor p62 and GTPase activating protein. J. Biol. Chem., 269: 12503-12507, 1994.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12503-12507
    • Sung, C.K.1    Sanchez-Margalet, V.2    Goldfine, I.D.3
  • 46
    • 0025651680 scopus 로고
    • Purification, characterization, and Western blot analysis of human GT-Pase-activating protein from native and recombinant sources
    • Halenbeck, R., Crosier, W. J., Clark, R., McCormick, F., and Koths, K. Purification, characterization, and Western blot analysis of human GT-Pase-activating protein from native and recombinant sources. J. Biol. Chem., 265: 21922-21928, 1990.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21922-21928
    • Halenbeck, R.1    Crosier, W.J.2    Clark, R.3    McCormick, F.4    Koths, K.5


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