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Volumn 17, Issue 7, 1997, Pages 3884-3897

Requirements for localization of p130(cas) to focal adhesions

Author keywords

[No Author keywords available]

Indexed keywords

INTEGRIN; PROTEIN SERINE THREONINE KINASE; BCAR1 PROTEIN, MOUSE; CRK ASSOCIATED SUBSTRATE PROTEIN; PHOSPHOPROTEIN; PROTEIN; PROTEIN KINASE P60; PROTEIN P130; RECOMBINANT PROTEIN;

EID: 0030611402     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.17.7.3884     Document Type: Article
Times cited : (139)

References (44)
  • 3
    • 0028889968 scopus 로고
    • Overexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreading
    • Bergman, M., V. Joukov, I. Virtanen, and K. Alitalo. 1995. Overexpressed Csk tyrosine kinase is localized in focal adhesions, causes reorganization of alpha v beta 5 integrin, and interferes with HeLa cell spreading. Mol. Cell. Biol. 15:711-722.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 711-722
    • Bergman, M.1    Joukov, V.2    Virtanen, I.3    Alitalo, K.4
  • 4
    • 0027227263 scopus 로고
    • Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin
    • Bockholt, S. M., and K. Burridge. 1993. Cell spreading on extracellular matrix proteins induces tyrosine phosphorylation of tensin. J. Biol. Chem. 268:14565-14567.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14565-14567
    • Bockholt, S.M.1    Burridge, K.2
  • 5
    • 0029146869 scopus 로고
    • An examination of focal adhesion formation and tyrosine phosphorylation in fibroblasts isolated from src-, fyn-, and yes- mice
    • Bockholt, S. M., and K. Burridge. 1995. An examination of focal adhesion formation and tyrosine phosphorylation in fibroblasts isolated from src-, fyn-, and yes-mice. Cell Adhesion Commun. 3:91-100.
    • (1995) Cell Adhesion Commun. , vol.3 , pp. 91-100
    • Bockholt, S.M.1    Burridge, K.2
  • 7
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge, K., K. Fath, T. Kelly, G. Nuckolls, and C. Turner. 1988. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 4:487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 8
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J. Cell Biol. 119:893-903.
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 9
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A., and J. S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 10
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan, J. L., and D. Shalloway. 1992. Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 358:690-692.
    • (1992) Nature , vol.358 , pp. 690-692
    • Guan, J.L.1    Shalloway, D.2
  • 12
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks, S. K., M. B. Calalb, M. C. Harper, and S. K. Patel. 1992. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA 89:8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 14
    • 0025010018 scopus 로고
    • Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells
    • Hirai, H., and H. E. Varmus. 1990. Mutations in src homology regions 2 and 3 of activated chicken c-src that result in preferential transformation of mouse or chicken cells. Proc. Natl. Acad. Sci. USA 87:8592-8596.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 8592-8596
    • Hirai, H.1    Varmus, H.E.2
  • 16
    • 0029562687 scopus 로고
    • Molecular cloning. of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn
    • Ishino, M., T. Ohba, H. Sasaki, and T. Sasaki. 1995. Molecular cloning. of a cDNA encoding a phosphoprotein, Efs, which contains a Src homology 3 domain and associates with Fyn. Oncogene 11:2331-2338.
    • (1995) Oncogene , vol.11 , pp. 2331-2338
    • Ishino, M.1    Ohba, T.2    Sasaki, H.3    Sasaki, T.4
  • 17
    • 0027996890 scopus 로고
    • Lymphocyte antigen receptor activation of a focal adhesion kinase-related tyrosine kinase substrate
    • Kanner, S. B., A. Aruffo, and P. Y. Chan. 1994. Lymphocyte antigen receptor activation of a focal adhesion kinase-related tyrosine kinase substrate. Proc. Natl. Acad. Sci. USA 91:10484-10487.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10484-10487
    • Kanner, S.B.1    Aruffo, A.2    Chan, P.Y.3
  • 18
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-coded tyrosine kinases
    • Kanner, S. B., A. B. Reynolds, R. R. Vines, and J. T. Parsons. 1990. Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-coded tyrosine kinases. Proc. Natl. Acad. Sci. USA 87:3328-3332.
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 3328-3332
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 19
    • 0028151515 scopus 로고
    • Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527
    • Kaplan, K. B., K. B. Bibbins, J. R. Swedlow, M. Arnaud, D. O. Morgan, and H. E. Varmus. 1994. Association of the amino-terminal half of c-Src with focal adhesions alters their properties and is regulated by phosphorylation of tyrosine 527. EMBO J. 13:4745-4756.
    • (1994) EMBO J. , vol.13 , pp. 4745-4756
    • Kaplan, K.B.1    Bibbins, K.B.2    Swedlow, J.R.3    Arnaud, M.4    Morgan, D.O.5    Varmus, H.E.6
  • 20
    • 0029034939 scopus 로고
    • C-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase independent mechanism
    • Kaplan, K. B., J. R. Swedlow, D. O. Morgan, and H. E. Varmus. 1995.C-Src enhances the spreading of src-/-fibroblasts on fibronectin by a kinase independent mechanism. Genes Dev. 9:1505-1517.
    • (1995) Genes Dev. , vol.9 , pp. 1505-1517
    • Kaplan, K.B.1    Swedlow, J.R.2    Morgan, D.O.3    Varmus, H.E.4
  • 21
    • 0029891787 scopus 로고    scopus 로고
    • Cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae
    • Cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae. Mol. Cell. Biol. 16:3327-3337.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3327-3337
    • Law, S.F.1    Estojak, J.2    Wang, B.3    Mysliwiec, T.4    Kruh, G.5    Golemis, E.A.6
  • 23
    • 0020501846 scopus 로고
    • Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses
    • Lipsich, L. A., A. J. Lewis, and J. S. Brugge. 1983. Isolation of monoclonal antibodies that recognize the transforming proteins of avian sarcoma viruses. J. Virol. 48:352-360.
    • (1983) J. Virol. , vol.48 , pp. 352-360
    • Lipsich, L.A.1    Lewis, A.J.2    Brugge, J.S.3
  • 25
    • 0012108774 scopus 로고
    • Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells
    • Maher, P. A., E. B. Pasquale, J. Y. Wang, and S. J. Singer. 1985. Phosphotyrosine-containing proteins are concentrated in focal adhesions and intercellular junctions in normal cells. Proc. Natl. Acad. Sci. USA 82:6576-6580.
    • (1985) Proc. Natl. Acad. Sci. USA , vol.82 , pp. 6576-6580
    • Maher, P.A.1    Pasquale, E.B.2    Wang, J.Y.3    Singer, S.J.4
  • 26
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mayer, B. J., H. Hirai, and R. Sakai. 1995. Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr. Biol. 5:296-305.
    • (1995) Curr. Biol. , vol.5 , pp. 296-305
    • Mayer, B.J.1    Hirai, H.2    Sakai, R.3
  • 27
    • 0029904694 scopus 로고    scopus 로고
    • Structure and function of Cas-L, a 105-kD Crk-associated substraterelated protein that is involved in beta 1 integrin-mediated signaling in lymphocytes
    • Minegishi, M., K. Tachibana, T. Sato, S. Iwata, Y. Nojima, and C. Morimoto. 1996. Structure and function of Cas-L, a 105-kD Crk-associated substraterelated protein that is involved in beta 1 integrin-mediated signaling in lymphocytes. J. Exp. Med. 184:1365-1375.
    • (1996) J. Exp. Med. , vol.184 , pp. 1365-1375
    • Minegishi, M.1    Tachibana, K.2    Sato, T.3    Iwata, S.4    Nojima, Y.5    Morimoto, C.6
  • 31
    • 0028335709 scopus 로고
    • The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells
    • Ogawa, S., H. Toyoshima, H. Kozutsumi, K. Hagiwara, R. Sakai, T. Tanaka, N. Hirano, H. Mano, Y. Yazaki, and H. Hirai. 1994. The C-terminal SH3 domain of the mouse c-Crk protein negatively regulates tyrosine-phosphorylation of Crk associated p130 in rat 3Y1 cells. Oncogene 9:1669-1678.
    • (1994) Oncogene , vol.9 , pp. 1669-1678
    • Ogawa, S.1    Toyoshima, H.2    Kozutsumi, H.3    Hagiwara, K.4    Sakai, R.5    Tanaka, T.6    Hirano, N.7    Mano, H.8    Yazaki, Y.9    Hirai, H.10
  • 32
  • 34
    • 0021236588 scopus 로고
    • Detection of the v-abl gene product at cell-substratum contact sites in Abelson murine leukemia virus-transformed fibroblasts
    • Rohrschneider, L. R., and L. M. Najita. 1984. Detection of the v-abl gene product at cell-substratum contact sites in Abelson murine leukemia virus-transformed fibroblasts. J. Virol. 51:547-552.
    • (1984) J. Virol. , vol.51 , pp. 547-552
    • Rohrschneider, L.R.1    Najita, L.M.2
  • 35
    • 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., A. Iwamatsu, N. Hirano, S. Ogawa, T. Tanaka, H. Mano, Y. Yazaki, and H. Hirai. 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
  • 36
    • 0028606467 scopus 로고
    • Characterization, partial purification, and peptide sequencing of p130, the main phosphoprotein associated with v-Crk oncoprotein
    • Sakai, R., A. Iwamatsu, N. Hirano, S. Ogawa, T. Tanaka, J. Nishida, Y. Yazaki, and H. Hirai. 1994. Characterization, partial purification, and peptide sequencing of p130, the main phosphoprotein associated with v-Crk oncoprotein. J. Biol. Chem. 269:32740-32746.
    • (1994) J. Biol. Chem. , vol.269 , pp. 32740-32746
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Nishida, J.6    Yazaki, Y.7    Hirai, H.8
  • 38
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • Sasaki, H., K. Nagura, M. Ishino, H. Tobioka, K. Kotani, and T. Sasaki. 1995. Cloning and characterization of cell adhesion kinase beta, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J. Biol. Chem. 270:21206-21219.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21206-21219
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 40
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin, H., T. Staehelin, and J. Gordon. 1979. Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 41
    • 0027193449 scopus 로고
    • Differently spliced cDNAs of human leukocyte tyrosine kinase receptor tyrosine kinase predict receptor proteins with and without a tyrosine kinase domain and a soluble receptor protein
    • Toyoshima, H., H. Kozutsumi, Y. Maru, K. Hagiwara, A. Furuya, H. Mioh, N. Hanai, F. Takaku, Y. Yazaki, and H. Hirai. 1993. Differently spliced cDNAs of human leukocyte tyrosine kinase receptor tyrosine kinase predict receptor proteins with and without a tyrosine kinase domain and a soluble receptor protein. Proc. Natl. Acad. Sci. USA 90:5404-5408.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5404-5408
    • Toyoshima, H.1    Kozutsumi, H.2    Maru, Y.3    Hagiwara, K.4    Furuya, A.5    Mioh, H.6    Hanai, N.7    Takaku, F.8    Yazaki, Y.9    Hirai, H.10
  • 42
    • 0029664531 scopus 로고    scopus 로고
    • Cas signaling complex formation upon integrin-mediated cell adhesion: A role for Src family kinases
    • Cas 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
  • 43
    • 0028981376 scopus 로고
    • Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix
    • Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix. J. Biol. Chem. 270:22259-22262.
    • (1995) J. Biol. Chem. , vol.270 , pp. 22259-22262
    • Vuori, K.1    Ruoslahti, E.2


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