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Volumn 17, Issue 9, 1998, Pages 2554-2565

Insulin regulates the dynamic balance between Ras and Rap1 signaling by coordinating the assembly states of the Grb2-SOS and CrkII-C3G complexes

Author keywords

C3G; CrkII; Insulin; Rap1; Ras

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; HUMAN INSULIN; HYBRID PROTEIN; INSULIN; PHOSPHOTRANSFERASE; RAS PROTEIN; RHEUMATOID ARTHRITIS PROTEIN; UNCLASSIFIED DRUG;

EID: 0032080085     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.9.2554     Document Type: Article
Times cited : (82)

References (97)
  • 2
    • 0029813117 scopus 로고    scopus 로고
    • A potential SH3 domain-binding site in the Crk SH2 domain
    • Anafi,M., Rosen,M.K., Gish,G.D., Kay,L.E. and Pawson,T. (1996) A potential SH3 domain-binding site in the Crk SH2 domain. J. Biol. Chem., 271, 21365-21374.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21365-21374
    • Anafi, M.1    Rosen, M.K.2    Gish, G.D.3    Kay, L.E.4    Pawson, T.5
  • 3
    • 0028175091 scopus 로고
    • Raf meets Ras: Completing the framework of a signal transduction pathway
    • Avruch,J., Zhang,X. and Kyriakis,J. (1994) Raf meets Ras: completing the framework of a signal transduction pathway. Trends. Biochem. Sci., 19, 279-283.
    • (1994) Trends. Biochem. Sci. , vol.19 , pp. 279-283
    • Avruch, J.1    Zhang, X.2    Kyriakis, J.3
  • 4
    • 0028809479 scopus 로고
    • The mouse B-Raf gene encodes multiple protein isoforms with tissue-specific expression
    • Barnier,J.V., Papin,C., Eychene,A., Lecoq,O. and Calothy,G. (1995) The mouse B-Raf gene encodes multiple protein isoforms with tissue-specific expression. J. Biol. Chem., 270, 23381-23389.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23381-23389
    • Barnier, J.V.1    Papin, C.2    Eychene, A.3    Lecoq, O.4    Calothy, G.5
  • 5
    • 0028953268 scopus 로고
    • Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk
    • Beitner-Johnson,D. and LeRoith,D. (1995) Insulin-like growth factor-I stimulates tyrosine phosphorylation of endogenous c-Crk. J. Biol. Chem., 270, 5187-5190.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5187-5190
    • Beitner-Johnson, D.1    LeRoith, D.2
  • 7
    • 0026658116 scopus 로고
    • Tyrosine-phosphorylated epidermal growth factor receptor and cellular p 130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro
    • Birge,R.B., Fajardo,J.E., Mayer,B.J. and Hanafusa,H. (1992) Tyrosine-phosphorylated epidermal growth factor receptor and cellular p 130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro. J. Biol. Chem., 267, 10588-10595.
    • (1992) J. Biol. Chem. , vol.267 , pp. 10588-10595
    • Birge, R.B.1    Fajardo, J.E.2    Mayer, B.J.3    Hanafusa, H.4
  • 8
    • 0027219262 scopus 로고
    • Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts
    • Birge,R.B., Fajardo,J.E., Reichman,C., Shoelson,S.E., Songyang,Z., Cantley,L.C. and Hanafusa,H. (1993) Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol. Cell. Biol., 13, 4648-4656.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4648-4656
    • Birge, R.B.1    Fajardo, J.E.2    Reichman, C.3    Shoelson, S.E.4    Songyang, Z.5    Cantley, L.C.6    Hanafusa, H.7
  • 9
    • 0027233448 scopus 로고
    • Signal transduction via the MAP kinases: Proceed at your own RSK
    • Blenis,J. (1993) Signal transduction via the MAP kinases: proceed at your own RSK. Proc. Natl Acad. Sci. USA, 90, 5889-5892.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 5889-5892
    • Blenis, J.1
  • 10
    • 0028358806 scopus 로고
    • Diversity in function and regulation of MAP kinase pathways
    • Blumer,J. and Johnson,G.L. (1994) Diversity in function and regulation of MAP kinase pathways. Trends Biochem. Sci., 19, 236-240.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 236-240
    • Blumer, J.1    Johnson, G.L.2
  • 11
    • 0027458513 scopus 로고
    • Biology of the Rap proteins, members of the ras superfamily of GTP-binding proteins
    • Bokoch,G.M. (1993) Biology of the Rap proteins, members of the ras superfamily of GTP-binding proteins. Biochem. J., 289, 17-24.
    • (1993) Biochem. J. , vol.289 , pp. 17-24
    • Bokoch, G.M.1
  • 12
    • 0028917954 scopus 로고
    • Regulation of Ras-mediated signalling: More than one way to skin a cat
    • Burgering,B.M.T. and Bos,J.L. (1995) Regulation of Ras-mediated signalling: more than one way to skin a cat. Trends Biochem. Sci., 20, 18-22.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 18-22
    • Burgering, B.M.T.1    Bos, J.L.2
  • 15
    • 0030808673 scopus 로고    scopus 로고
    • Osmotic shock stimulates GLUT4 translocation in 3T3L1 adipocytes by a novel tyrosine kinase pathway
    • Chen,D., Elmendorf,J.S., Olson,A.L., Li,X., Earp,H.S. and Pessin,J.E. (1997) Osmotic shock stimulates GLUT4 translocation in 3T3L1 adipocytes by a novel tyrosine kinase pathway. J. Biol. Chem., 272, 27401-27410.
    • (1997) J. Biol. Chem. , vol.272 , pp. 27401-27410
    • Chen, D.1    Elmendorf, J.S.2    Olson, A.L.3    Li, X.4    Earp, H.S.5    Pessin, J.E.6
  • 16
    • 0028899751 scopus 로고
    • Disassembly of son-of-sevenless proteins from Grb2 during p21(ras) desensitization by insulin
    • Cherniack,A., Klarlund,J., Conway,B. and Czech,M. (1995) Disassembly of son-of-sevenless proteins from Grb2 during p21(ras) desensitization by insulin. J. Biol. Chem., 270, 1485-1488.
    • (1995) J. Biol. Chem. , vol.270 , pp. 1485-1488
    • Cherniack, A.1    Klarlund, J.2    Conway, B.3    Czech, M.4
  • 17
    • 0027170176 scopus 로고
    • RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat 1 fibroblasts
    • Cook,S., Rubinfeld,B., Albert,I., and McCormick,F. (1993) RapV12 antagonizes Ras-dependent activation of ERK1 and ERK2 by LPA and EGF in Rat 1 fibroblasts. EMBO J., 12, 3475-3485.
    • (1993) EMBO J. , vol.12 , pp. 3475-3485
    • Cook, S.1    Rubinfeld, B.2    Albert, I.3    McCormick, F.4
  • 18
    • 0027165150 scopus 로고
    • The mitogen-activated protein kinase signal transduction pathway
    • Davis,R.J. (1993) The mitogen-activated protein kinase signal transduction pathway. J. Biol Chem., 268, 14553-14556.
    • (1993) J. Biol Chem. , vol.268 , pp. 14553-14556
    • Davis, R.J.1
  • 19
    • 0029014973 scopus 로고
    • Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases
    • Dent,P., Jelinek,J., Morrison,D.K., Weber,M.J. and Sturgill,T.W. (1995) Reversal of Raf-1 activation by purified and membrane-associated protein phosphatases. Science, 268, 1902-1906.
    • (1995) Science , vol.268 , pp. 1902-1906
    • Dent, P.1    Jelinek, J.2    Morrison, D.K.3    Weber, M.J.4    Sturgill, T.W.5
  • 20
    • 0030756069 scopus 로고    scopus 로고
    • Phosphorylation of Raf-1 serine 338-serine339 is an essential regulatory event for Ras-dependent activation and biological signaling
    • Diaz,B., Barnard,D., Filson,A., MacDonald,S., King,A. and Marshall,M. (1997) Phosphorylation of Raf-1 serine 338-serine339 is an essential regulatory event for Ras-dependent activation and biological signaling. Moi Cell. Biol., 17, 4509-4516.
    • (1997) Moi Cell. Biol. , vol.17 , pp. 4509-4516
    • Diaz, B.1    Barnard, D.2    Filson, A.3    MacDonald, S.4    King, A.5    Marshall, M.6
  • 21
    • 0027957728 scopus 로고
    • The GRB2/Sem-5 adaptor protein
    • Downward,J. (1994) The GRB2/Sem-5 adaptor protein. FEBS Lett., 338, 113-117.
    • (1994) FEBS Lett. , vol.338 , pp. 113-117
    • Downward, J.1
  • 22
    • 0029955128 scopus 로고    scopus 로고
    • Control of ras activation
    • Downward,J. (1996) Control of ras activation. Cancer Surv., 27, 87-100.
    • (1996) Cancer Surv. , vol.27 , pp. 87-100
    • Downward, J.1
  • 23
    • 0027364980 scopus 로고
    • Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase
    • Fabian,J.R., Daar,I.O. and Morrison,D.K. (1993) Critical tyrosine residues regulate the enzymatic and biological activity of Raf-1 kinase. Mol. Cell. Biol., 13, 7170-7179.
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 7170-7179
    • Fabian, J.R.1    Daar, I.O.2    Morrison, D.K.3
  • 24
    • 0028243505 scopus 로고
    • C-Abl kinase regulates the protein binding activity of c-Crk
    • Feller,S.M., Knudsen,B. and Hanafusa,H. (1994) c-Abl kinase regulates the protein binding activity of c-Crk. EMBO J., 13, 2341-2351.
    • (1994) EMBO J. , vol.13 , pp. 2341-2351
    • Feller, S.M.1    Knudsen, B.2    Hanafusa, H.3
  • 25
    • 0029030240 scopus 로고
    • Cellular proteins binding to the first src homology 3 (SH3) domain of the protooncogene product c-Crk indicate c-Crk-specific signaling pathways
    • Feller,S.M., Knudsen,B. and Hanafusa,H. (1995) Cellular proteins binding to the first src homology 3 (SH3) domain of the protooncogene product c-Crk indicate c-Crk-specific signaling pathways. Oncogene, 10, 1465-1473.
    • (1995) Oncogene , vol.10 , pp. 1465-1473
    • Feller, S.M.1    Knudsen, B.2    Hanafusa, H.3
  • 26
    • 0031014969 scopus 로고    scopus 로고
    • 2+-mediated activation of Rap1 in human platelets
    • 2+-mediated activation of Rap1 in human platelets. EMBO J., 16, 252-259.
    • (1997) EMBO J. , vol.16 , pp. 252-259
    • Franke, B.1    Akkerman, J.W.2    Bos, J.L.3
  • 27
    • 0025874250 scopus 로고
    • Evidence supporting a passive role for the insulin receptor transmembrane domain in insulin-dependent signal transduction
    • Frattali,A., Treadway,J. and Pessin,J. (1991) Evidence supporting a passive role for the insulin receptor transmembrane domain in insulin-dependent signal transduction. J. Biol. Chem., 266, 9829-9834.
    • (1991) J. Biol. Chem. , vol.266 , pp. 9829-9834
    • Frattali, A.1    Treadway, J.2    Pessin, J.3
  • 29
    • 0028881018 scopus 로고
    • Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G
    • Gotoh,T. et al. (1995) Identification of Rap1 as a target for the Crk SH3 domain-binding guanine nucleotide-releasing factor C3G. Mol. Cell. Biol., 15, 6746-6753.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6746-6753
    • Gotoh, T.1
  • 31
    • 0025355524 scopus 로고
    • Inhibition of the ras p21 GTPase-activating protein-stimulated GTPase activity of c-Ha-ras p21 by smg p21 having the same putative effector domain as ras p21s
    • Hata,Y., Kikuchi,A., Sasaki,T., Schaber,M.D., Gibbs,J.B. and Takai,Y. (1990) Inhibition of the ras p21 GTPase-activating protein-stimulated GTPase activity of c-Ha-ras p21 by smg p21 having the same putative effector domain as ras p21s. J. Cell Biol., 265, 7104-7107.
    • (1990) J. Cell Biol. , vol.265 , pp. 7104-7107
    • Hata, Y.1    Kikuchi, A.2    Sasaki, T.3    Schaber, M.D.4    Gibbs, J.B.5    Takai, Y.6
  • 32
    • 0028347526 scopus 로고
    • Expression of the v-crk oncogene product in PC 12 cells results in rapid differentiation by both nerve growth factor- And epidermal growth factor-dependent pathways
    • Hempstead,B.L., Birge,R.B., Fajardo,J.E., Glassman,R., Mahadeo,D., Kraemer,R. and Hanafusa,H. (1994) Expression of the v-crk oncogene product in PC 12 cells results in rapid differentiation by both nerve growth factor- and epidermal growth factor-dependent pathways. Mol. Cell. Biol., 14, 1964-1971.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1964-1971
    • Hempstead, B.L.1    Birge, R.B.2    Fajardo, J.E.3    Glassman, R.4    Mahadeo, D.5    Kraemer, R.6    Hanafusa, H.7
  • 33
    • 0029913467 scopus 로고    scopus 로고
    • Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A. and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor
    • Herrmann,C., Horn,G., Spaargaren,M. and Wittinghofer,A. (1996) Differential interaction of the ras family GTP-binding proteins H-Ras, Rap1A. and R-Ras with the putative effector molecules Raf kinase and Ral-guanine nucleotide exchange factor. J. Biol. Chem., 271, 6794-6800.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6794-6800
    • Herrmann, C.1    Horn, G.2    Spaargaren, M.3    Wittinghofer, A.4
  • 34
    • 0028897113 scopus 로고
    • Transcriptional regulation by extracellular signals: Mechanisms and specificity
    • Hill,C.S. and Treisman,R. (1995) Transcriptional regulation by extracellular signals: mechanisms and specificity. Cell, 80, 199-211.
    • (1995) Cell , vol.80 , pp. 199-211
    • Hill, C.S.1    Treisman, R.2
  • 35
    • 0030030357 scopus 로고    scopus 로고
    • Insulin stimulation of a MEK-dependent but ERK-independent SOS protein kinase
    • Holt,K., Kasson,B. and Pessin,J. (1996a) Insulin stimulation of a MEK-dependent but ERK-independent SOS protein kinase. Mol. Cell. Biol., 16, 577-583.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 577-583
    • Holt, K.1    Kasson, B.2    Pessin, J.3
  • 37
    • 0030910890 scopus 로고    scopus 로고
    • Coassociation of Rap1A and Ha-Ras with Raf-1 N-terminal region interferes with Ras-dependent activation of Raf-1
    • Hu,C.-D., Kariya,K., Kotani,G., Shirouzu,M., Yokoyama,S. and Kataoka,T. (1997) Coassociation of Rap1A and Ha-Ras with Raf-1 N-terminal region interferes with Ras-dependent activation of Raf-1. J. Biol. Chem., 272, 11702-11705.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11702-11705
    • Hu, C.-D.1    Kariya, K.2    Kotani, G.3    Shirouzu, M.4    Yokoyama, S.5    Kataoka, T.6
  • 38
    • 0030771490 scopus 로고    scopus 로고
    • Enhancement of guanine-nucleotide exchange activity of C3G for Rap1 by the expression of Crk, CrkL, and Grb2
    • Ichiba,T., Kuraishi,Y., Sakai,O., Nagata,S., Groffen,J., Kurata,T., Hattori,S. and Matsuda,M. (1997) Enhancement of guanine-nucleotide exchange activity of C3G for Rap1 by the expression of Crk, CrkL, and Grb2. J. Biol. Chem., 272, 22215-22220.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22215-22220
    • Ichiba, T.1    Kuraishi, Y.2    Sakai, O.3    Nagata, S.4    Groffen, J.5    Kurata, T.6    Hattori, S.7    Matsuda, M.8
  • 39
    • 0029768637 scopus 로고    scopus 로고
    • B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins
    • Ingham,R.J., Krebs,D.L., Barbazuk,S.M., Turck,C.W., Hirai,H., Matsuda,M. and Gold,M.R. (1996) B cell antigen receptor signaling induces the formation of complexes containing the Crk adapter proteins. J. Biol. Chem., 271, 32306-32314.
    • (1996) J. Biol. Chem. , vol.271 , pp. 32306-32314
    • Ingham, R.J.1    Krebs, D.L.2    Barbazuk, S.M.3    Turck, C.W.4    Hirai, H.5    Matsuda, M.6    Gold, M.R.7
  • 40
    • 0030862349 scopus 로고    scopus 로고
    • Evidence for functional roles of Crk-II in insulin and epidermal growth factor signaling in Rat-1 fibroblasts overexpressing insulin receptors
    • Ishiki,M., Toshiyasu,S., Ishihara,H., Imamura,T., Usui,I., Takata,Y. and Kobayashi,M. (1997) Evidence for functional roles of Crk-II in insulin and epidermal growth factor signaling in Rat-1 fibroblasts overexpressing insulin receptors. Endocrinology, 138, 4950-4958.
    • (1997) Endocrinology , vol.138 , pp. 4950-4958
    • Ishiki, M.1    Toshiyasu, S.2    Ishihara, H.3    Imamura, T.4    Usui, I.5    Takata, Y.6    Kobayashi, M.7
  • 41
    • 0026726820 scopus 로고
    • Reversion of middle T antigen-transformed rat-2 cell by Krev-1 - Implications for the role of p21c-ras in polyomavirus-mediated transformation
    • Jelink,M.A. and Hassell,J.A. (1992) Reversion of middle T antigen-transformed rat-2 cell by Krev-1 - implications for the role of p21c-ras in polyomavirus-mediated transformation. Oncogene, 7, 1687-1698.
    • (1992) Oncogene , vol.7 , pp. 1687-1698
    • Jelink, M.A.1    Hassell, J.A.2
  • 42
    • 0030029343 scopus 로고    scopus 로고
    • Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation
    • Jelinek,T., Dent,P., Sturgill,T.W. and Weber,M.J. (1996) Ras-induced activation of Raf-1 is dependent on tyrosine phosphorylation. Mol. Cell. Biol, 16, 1027-1034.
    • (1996) Mol. Cell. Biol , vol.16 , pp. 1027-1034
    • Jelinek, T.1    Dent, P.2    Sturgill, T.W.3    Weber, M.J.4
  • 43
    • 0027953703 scopus 로고
    • Insulin action, diabetogenes, and the cause of type II diabetes
    • Kahn,C.R. (1994) Insulin action, diabetogenes, and the cause of type II diabetes. Diabetes, 43, 1066-1084.
    • (1994) Diabetes , vol.43 , pp. 1066-1084
    • Kahn, C.R.1
  • 44
    • 0030998473 scopus 로고    scopus 로고
    • Insulin stimulates the phosphorylation of the 66 and 52 kDa She isoforms by distinct pathways
    • Kao,A.W., Waters,S.B., Okada,S. and Pessin,J.E. (1997) Insulin stimulates the phosphorylation of the 66 and 52 kDa She isoforms by distinct pathways. Endocrinology, 138, 2474-2480.
    • (1997) Endocrinology , vol.138 , pp. 2474-2480
    • Kao, A.W.1    Waters, S.B.2    Okada, S.3    Pessin, J.E.4
  • 45
    • 0024600222 scopus 로고
    • A ras-related gene with transformation suppressor activity
    • Kitayama,H., Sugimoto,Y., Matsuzaki,T., Ikawa,Y. and Noda,M. (1989) A ras-related gene with transformation suppressor activity. Cell, 56, 77-84.
    • (1989) Cell , vol.56 , pp. 77-84
    • Kitayama, H.1    Sugimoto, Y.2    Matsuzaki, T.3    Ikawa, Y.4    Noda, M.5
  • 46
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk
    • Knudsen,B.S., Feller,S.M. and Hanafusa,H. (1994) Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk. J. Biol. Chem., 269, 32781-32787.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32781-32787
    • Knudsen, B.S.1    Feller, S.M.2    Hanafusa, H.3
  • 47
    • 0028829346 scopus 로고
    • Negative feedback regulation and desensitization of insulin- And epidermal growth factor-stimulated p21ras activation
    • Langlois,W., Sasaoka,T., Saltiel,A. and Olefsky,J. (1995) Negative feedback regulation and desensitization of insulin- and epidermal growth factor-stimulated p21ras activation. J. Biol. Chem., 270, 25320-25323.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25320-25323
    • Langlois, W.1    Sasaoka, T.2    Saltiel, A.3    Olefsky, J.4
  • 48
    • 0026729382 scopus 로고
    • The SH2 and SH3 domain-containing protein Grb2 links receptor tyrosine kinases to ras signaling
    • Lowenstein,E.J. et al. (1992) The SH2 and SH3 domain-containing protein Grb2 links receptor tyrosine kinases to ras signaling. Cell, 70, 431-442.
    • (1992) Cell , vol.70 , pp. 431-442
    • Lowenstein, E.J.1
  • 50
    • 0028152333 scopus 로고
    • MAP kinase kinase kinase, MAP kinase kinase and MAP kinase
    • Marshall,C.J. (1994) MAP kinase kinase kinase, MAP kinase kinase and MAP kinase. Curr. Opin. Genet. Dev., 4, 82-89.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 82-89
    • Marshall, C.J.1
  • 51
    • 0025298967 scopus 로고
    • Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins
    • Matsuda,M., Mayer,B.J., Fukui,Y. and Hanafusa,H. (1990) Binding of transforming protein, P47gag-crk, to a broad range of phosphotyrosine-containing proteins. Science, 248, 1537-1539.
    • (1990) Science , vol.248 , pp. 1537-1539
    • Matsuda, M.1    Mayer, B.J.2    Fukui, Y.3    Hanafusa, H.4
  • 52
    • 0026686182 scopus 로고
    • Two species of human CRK cDNA encode proteins with distinct biological activities
    • Matsuda,M., Tanaka,S., Nagata,S., Kojima,A., Kurata,T. and Shibuya,M. (1992) Two species of human CRK cDNA encode proteins with distinct biological activities. Mol. Cell. Biol., 12, 3482-3489.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3482-3489
    • Matsuda, M.1    Tanaka, S.2    Nagata, S.3    Kojima, A.4    Kurata, T.5    Shibuya, M.6
  • 53
    • 0028122971 scopus 로고
    • CRK protein binds to two guanine nucleotide-releasing proteins for the ras family and modulates nerve growth factor-induced activation of ras in PC12 cells
    • Matsuda,M., Hashimoto,Y., Muroya,K., Hasegawa,H., Kurata,T., Tanaka,S., Nakamura,S. and Hattori,S. (1994) CRK protein binds to two guanine nucleotide-releasing proteins for the ras family and modulates nerve growth factor-induced activation of ras in PC12 cells. Mol. Cell. Biol., 14, 5495-5500.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5495-5500
    • Matsuda, M.1    Hashimoto, Y.2    Muroya, K.3    Hasegawa, H.4    Kurata, T.5    Tanaka, S.6    Nakamura, S.7    Hattori, S.8
  • 54
    • 0023864050 scopus 로고
    • A novel viral oncogene with structural similarity to phospholipase C
    • Mayer,B.J., Hamaguchi,M. and Hanafusa,H. (1988) A novel viral oncogene with structural similarity to phospholipase C. Nature, 332, 272-275.
    • (1988) Nature , vol.332 , pp. 272-275
    • Mayer, B.J.1    Hamaguchi, M.2    Hanafusa, H.3
  • 55
    • 0027138356 scopus 로고
    • The role of p21ras in receptor tyrosine kinase signaling
    • Medema,R.H. and Bos,J.L. (1993) The role of p21ras in receptor tyrosine kinase signaling. Crit. Rev.Oncogen., 4, 615-661.
    • (1993) Crit. Rev.Oncogen. , vol.4 , pp. 615-661
    • Medema, R.H.1    Bos, J.L.2
  • 57
    • 0027337519 scopus 로고
    • Complexes of Ras GTP with Raf-1 and mitogen-activated protein kinase kinase
    • Moodie,S.A., Willumsen,B.M., Weber,M.J. and Wolfman,A. (1993) Complexes of Ras GTP with Raf-1 and mitogen-activated protein kinase kinase. Science, 260, 1658-1661.
    • (1993) Science , vol.260 , pp. 1658-1661
    • Moodie, S.A.1    Willumsen, B.M.2    Weber, M.J.3    Wolfman, A.4
  • 58
    • 0029107760 scopus 로고
    • The 2.2 Å crystal structure structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP-analogue
    • Nassar,N., Horn,G., Herrmann,C., Scherer,A., McCormick,F. and Wittinghofer,A. (1995) The 2.2 Å crystal structure structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP-analogue. Nature, 375, 554-560.
    • (1995) Nature , vol.375 , pp. 554-560
    • Nassar, N.1    Horn, G.2    Herrmann, C.3    Scherer, A.4    McCormick, F.5    Wittinghofer, A.6
  • 59
    • 0029794722 scopus 로고    scopus 로고
    • Interactions between Src homology (SH) 2/SH3 adaptor proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor
    • Okada,S. and Pessin,J.E. (1996) Interactions between Src homology (SH) 2/SH3 adaptor proteins and the guanylnucleotide exchange factor SOS are differentially regulated by insulin and epidermal growth factor. J. Biol. Chem., 271, 25533-25538.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25533-25538
    • Okada, S.1    Pessin, J.E.2
  • 60
    • 0028221043 scopus 로고
    • Signalling pathways initiated by receptor protein tyrosine kinases in Drosophila
    • Perrimon,N. (1994) Signalling pathways initiated by receptor protein tyrosine kinases in Drosophila. Curr. Opin. Cell Biol., 6, 260-266.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 260-266
    • Perrimon, N.1
  • 61
    • 0023721977 scopus 로고
    • Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region
    • Pizon,V., Chardin,P., Lerosey,I., Olofsson,B. and Tavitian,A. (1988) Human cDNAs rap1 and rap2 homologous to the Drosophila gene Dras3 encode proteins closely related to ras in the 'effector' region. Oncogene, 3, 201-204.
    • (1988) Oncogene , vol.3 , pp. 201-204
    • Pizon, V.1    Chardin, P.2    Lerosey, I.3    Olofsson, B.4    Tavitian, A.5
  • 62
    • 0028889436 scopus 로고
    • Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas
    • Polte,T.R. and Hanks,S.K. (1995) Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas. Proc. Natl Acad. Sci. USA, 92, 10678-10682.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 10678-10682
    • Polte, T.R.1    Hanks, S.K.2
  • 63
    • 0026895954 scopus 로고
    • The product of the cellular crk gene consists primarily of SH2 and SH3 regions
    • Reichman,C.T., Mayer,B.J., Keshau,S. and Hanafusa,H. (1992) The product of the cellular crk gene consists primarily of SH2 and SH3 regions. Cell Growth Differ., 3, 451-460.
    • (1992) Cell Growth Differ. , vol.3 , pp. 451-460
    • Reichman, C.T.1    Mayer, B.J.2    Keshau, S.3    Hanafusa, H.4
  • 64
    • 0029871329 scopus 로고    scopus 로고
    • Nerve growth factor stimulates the tyrosine phosphorylation of endogenous Crk-II and augments its association with p130Cas in PC-12 cells
    • Ribon,V. and Saltiel,A.R. (1996) Nerve growth factor stimulates the tyrosine phosphorylation of endogenous Crk-II and augments its association with p130Cas in PC-12 cells. J. Biol. Chem., 271, 7375-7380.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7375-7380
    • Ribon, V.1    Saltiel, A.R.2
  • 65
    • 0029655999 scopus 로고    scopus 로고
    • The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner
    • Ribon,V., Hubbell,S., Herrera,R. and Saltiel,A.R. (1996) The product of the cbl oncogene forms stable complexes in vivo with endogenous Crk in a tyrosine phosphorylation-dependent manner. Mol. Cell. Biol., 16, 45-52.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 45-52
    • Ribon, V.1    Hubbell, S.2    Herrera, R.3    Saltiel, A.R.4
  • 66
    • 0028916892 scopus 로고
    • Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the signaling protein Crk
    • Rosen,M.K., Yamazaki,T., Gish,G.D., Kay,C.M., Pawson,T. and Kay,L.E. (1995) Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the signaling protein Crk. Nature, 374, 477-479.
    • (1995) Nature , vol.374 , pp. 477-479
    • Rosen, M.K.1    Yamazaki, T.2    Gish, G.D.3    Kay, C.M.4    Pawson, T.5    Kay, L.E.6
  • 67
    • 0028227166 scopus 로고
    • Biochemical mechanisms of insulin resistance
    • Roth,R.A., Liu,F. and Chin,J.E. (1994) Biochemical mechanisms of insulin resistance. Harm. Res., 41, 51-55.
    • (1994) Harm. Res. , vol.41 , pp. 51-55
    • Roth, R.A.1    Liu, F.2    Chin, J.E.3
  • 68
    • 0026678172 scopus 로고
    • Association of the She and Grb2/Sem5 SH2-coniaining proteins is implicated in activation of the Ras pathway by tyrosine kinases
    • Rozakis-Adcock,M. et al. (1992) Association of the She and Grb2/Sem5 SH2-coniaining proteins is implicated in activation of the Ras pathway by tyrosine kinases. Nature, 360, 689-692.
    • (1992) Nature , vol.360 , pp. 689-692
    • Rozakis-Adcock, M.1
  • 69
    • 0028258992 scopus 로고
    • Raf-1 interferes with Ras and Rap1A effector functions in yeast
    • Ruggieri,R., Macdonald,S.G., Callow,M. and McCormick,F. (1994) Raf-1 interferes with Ras and Rap1A effector functions in yeast. Mol. Biol. Cell, 5, 173-181.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 173-181
    • Ruggieri, R.1    Macdonald, S.G.2    Callow, M.3    McCormick, F.4
  • 70
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai,R., Iwamatsu,A., Hirano,N., Ogawa,S., Tanaka,T., Mano,H., Yazaki,Y. and Hirai,H. (1994) A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J., 13, 3748-3756.
    • (1994) EMBO J. , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 71
    • 0026757356 scopus 로고
    • Smg/rapl/Krev-1 p21s inhibit the signal pathway to the c-fos promoter/enhancer from c-Ki-ras p21 but not from c-raf-1 kinase in NIH3T3 cells
    • Sakoda,T., Kaibuchi,K., Kishi,K., Kishida,S., Doi,K., Hoshino,M., Hattori,S. and Takai,Y. (1992) smg/rapl/Krev-1 p21s inhibit the signal pathway to the c-fos promoter/enhancer from c-Ki-ras p21 but not from c-raf-1 kinase in NIH3T3 cells. Oncogene, 7, 1705-1711.
    • (1992) Oncogene , vol.7 , pp. 1705-1711
    • Sakoda, T.1    Kaibuchi, K.2    Kishi, K.3    Kishida, S.4    Doi, K.5    Hoshino, M.6    Hattori, S.7    Takai, Y.8
  • 72
    • 0028986116 scopus 로고
    • Pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller,M.D. and Parsons,J.T. (1995) pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol. Cell. Biol., 15, 2635-2645.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons2
  • 73
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains
    • Schaller,M.D., Otey,C.A., Hildebrand,J.D. and Parsons,J.T. (1995) Focal adhesion kinase and paxillin bind to peptides mimicking beta integrin cytoplasmic domains. J. Cell Biol., 130, 1181-1187.
    • (1995) J. Cell Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 75
    • 0029036124 scopus 로고
    • The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R
    • Schumacher,C., Knudsen,B., Ohuchi,T., Di Fiores,P., Glassman,R.H. and Hanafusa,H. (1995) The SH3 domain of Crk binds specifically to a conserved proline-rich motif in Eps15 and Eps15R. J. Biol. Chem., 270, 15341-15347.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15341-15347
    • Schumacher, C.1    Knudsen, B.2    Ohuchi, T.3    Di Fiores, P.4    Glassman, R.H.5    Hanafusa, H.6
  • 76
    • 0031034930 scopus 로고    scopus 로고
    • Crystal structure of the Src family tyrosine kinase Hck
    • Sicheri,F., Moarefi,J. and Kuriyan,J. (1997) Crystal structure of the Src family tyrosine kinase Hck. Nature, 385, 602-609.
    • (1997) Nature , vol.385 , pp. 602-609
    • Sicheri, F.1    Moarefi, J.2    Kuriyan, J.3
  • 77
    • 0028577298 scopus 로고
    • Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras and rap
    • Spaargaren,M. and Bischoff,J.R. (1994) Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras and rap. Proc. Natl Acad. Sci. USA, 91, 12609-12613.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 12609-12613
    • Spaargaren, M.1    Bischoff, J.R.2
  • 78
    • 0029645117 scopus 로고
    • How Ras works: Structure of a kap-Raf complex
    • Sprang,S.R. (1995) How Ras works: structure of a kap-Raf complex. Structure, 3, 641-643.
    • (1995) Structure , vol.3 , pp. 641-643
    • Sprang, S.R.1
  • 79
    • 0028264812 scopus 로고
    • C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the SRC homology-3 domains of CRK and GRB2/ASH proteins
    • Tanaka,S. et al. (1994) C3G, a guanine nucleotide-releasing protein expressed ubiquitously, binds to the SRC homology-3 domains of CRK and GRB2/ASH proteins. Proc. Natl Acad. Sci. USA, 91, 3443-3447.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 3443-3447
    • Tanaka, S.1
  • 81
    • 0029152154 scopus 로고
    • V-Crk modulation of growth factor-induced PC12 cell differentiation involves the Src homology 2 domain of v-Crk and sustained activation of the Ras/mitogen-activated protein kinase pathway
    • Teng,K.K., Lander,H., Fajardo,J.E., Hanafusa,H., Hempstead,B.L. and Birge,R.B. (1995) v-Crk modulation of growth factor-induced PC12 cell differentiation involves the Src homology 2 domain of v-Crk and sustained activation of the Ras/mitogen-activated protein kinase pathway. J. Biol. Chem., 270, 20677-20685.
    • (1995) J. Biol. Chem. , vol.270 , pp. 20677-20685
    • Teng, K.K.1    Lander, H.2    Fajardo, J.E.3    Hanafusa, H.4    Hempstead, B.L.5    Birge, R.B.6
  • 82
    • 0028084337 scopus 로고
    • Ternary complex factors: Growth factor-regulated transcriptional activators
    • Treisman,R. (1994) Ternary complex factors: growth factor-regulated transcriptional activators. Curr. Opin. Genet. Dev., 4, 96-101.
    • (1994) Curr. Opin. Genet. Dev. , vol.4 , pp. 96-101
    • Treisman, R.1
  • 84
    • 0030293986 scopus 로고    scopus 로고
    • The She adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Tyr 239/240) that mediate protein-protein interactions
    • van der Geer,P., Wiley,S., Gish,G.D. and Pawson,T. (1996) The She adaptor protein is highly phosphorylated at conserved, twin tyrosine residues (Tyr 239/240) that mediate protein-protein interactions. Curr. Biol., 6, 1435-1444.
    • (1996) Curr. Biol. , vol.6 , pp. 1435-1444
    • Van der Geer, P.1    Wiley, S.2    Gish, G.D.3    Pawson, T.4
  • 85
    • 0027250250 scopus 로고
    • Mammalian Ras interacts directly with the serine/threonine kinase Raf
    • Vojtek,A.B., Hollenberg,S.M. and Cooper,J.A. (1993) Mammalian Ras interacts directly with the serine/threonine kinase Raf. Cell, 74, 205-214.
    • (1993) Cell , vol.74 , pp. 205-214
    • Vojtek, A.B.1    Hollenberg, S.M.2    Cooper, J.A.3
  • 86
    • 0030963439 scopus 로고    scopus 로고
    • CAMP activates MAP kinase and Elk-1 through a B-Raf- And Rap 1-dependent pathway
    • Vossler,M.R., Yao,H., York,R.D., Pan,M.-G., Rim,C.S. and Stork,P.J.S. (1997) cAMP activates MAP kinase and Elk-1 through a B-Raf- and Rap 1-dependent pathway. Cell, 89, 73-82.
    • (1997) Cell , vol.89 , pp. 73-82
    • Vossler, M.R.1    Yao, H.2    York, R.D.3    Pan, M.-G.4    Rim, C.S.5    Stork, P.J.S.6
  • 87
    • 0029664531 scopus 로고    scopus 로고
    • Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • Vuori,K., Hirai,H., Aizawa,S. and Ruoslahti,E. (1996) Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol. Cell. Biol., 16, 2606-2613.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 88
    • 0027200883 scopus 로고
    • Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro
    • Warne,P.H., Viciana,P.R. and Downward,J. (1993) Direct interaction of Ras and the amino-terminal region of Raf-1 in vitro. Nature, 364, 352-355.
    • (1993) Nature , vol.364 , pp. 352-355
    • Warne, P.H.1    Viciana, P.R.2    Downward, J.3
  • 90
    • 0028950637 scopus 로고
    • Insulin-stimulated disassociation of the SOS-Grb2 complex
    • Waters,S., Yamauchi,K. and Pessin,J. (1995b) Insulin-stimulated disassociation of the SOS-Grb2 complex. Mol. Cell. Biol., 15, 2791-2799.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2791-2799
    • Waters, S.1    Yamauchi, K.2    Pessin, J.3
  • 91
    • 0026611532 scopus 로고
    • Both p12ras and pp60v-src are required, but neither alone is sufficient to activate the Raf-1 kinase
    • Williams,N.G., Roberts,T.M. and Li,P. (1992) Both p12ras and pp60v-src are required, but neither alone is sufficient to activate the Raf-1 kinase. Proc. Natl Acad. Sci. USA, 89, 2922-2926.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2922-2926
    • Williams, N.G.1    Roberts, T.M.2    Li, P.3
  • 92
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu,W., Harrison,S.C. and Eck,M.J. (1997) Three-dimensional structure of the tyrosine kinase c-Src. Nature, 385, 595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 93
    • 0028036724 scopus 로고
    • Insulin receptor substrate-1 (IRS1) and She compete for a limited pool of Grb2 in mediating insulin downstream signaling
    • Yamauchi,K. and Pessin,J. (1994) Insulin receptor substrate-1 (IRS1) and She compete for a limited pool of Grb2 in mediating insulin downstream signaling. J. Biol. Chem., 269, 31107-31114.
    • (1994) J. Biol. Chem. , vol.269 , pp. 31107-31114
    • Yamauchi, K.1    Pessin, J.2
  • 95
    • 0026656537 scopus 로고
    • Microinjection of smg/rap1/Krev-1 p21 into Swiss 3T3 cells induces DNA synthesis and morphological changes
    • Yoshida,Y., Kawata,M., Miura,Y., Musha,T., Sasaki,T., Kikuchi,A. and Takai,Y. (1992) Microinjection of smg/rap1/Krev-1 p21 into Swiss 3T3 cells induces DNA synthesis and morphological changes. Mol. Cell. Biol., 12, 3407-3414.
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 3407-3414
    • Yoshida, Y.1    Kawata, M.2    Miura, Y.3    Musha, T.4    Sasaki, T.5    Kikuchi, A.6    Takai, Y.7
  • 96
    • 0025335812 scopus 로고
    • Identification of small clusters of divergent amino acids that mediate the opposing effects of ras and Krev-1
    • Zhang,K., Noda,M., Vass,W.C., Papageorge,A.G. and Lowy,D.R. (1990) Identification of small clusters of divergent amino acids that mediate the opposing effects of ras and Krev-1. Science. 249, 162-165.
    • (1990) Science , vol.249 , pp. 162-165
    • Zhang, K.1    Noda, M.2    Vass, W.C.3    Papageorge, A.G.4    Lowy, D.R.5


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