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Volumn 3, Issue , 2002, Pages

A p130Cas tyrosine phosphorylated substrate domain decoy disrupts v-Crk signaling

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BINDING PROTEIN; DOCKING PROTEIN; FOCAL ADHESION KINASE; JANUS KINASE; MUTANT PROTEIN; PROTEIN P130; PROTEIN SH2; PROTEIN TYROSINE KINASE; PROTEIN V CRK; UNCLASSIFIED DRUG;

EID: 2342495279     PISSN: 14712121     EISSN: None     Source Type: Journal    
DOI: 10.1186/1471-2121-3-18     Document Type: Article
Times cited : (19)

References (51)
  • 1
    • 0033121275 scopus 로고    scopus 로고
    • The role of {alpha}v integrins during angiogenesis: Insights into potential mechanisms of action and clinical development
    • Eliceiri BP, Cheresh DA: The role of {alpha}v integrins during angiogenesis: insights into potential mechanisms of action and clinical development. J. Clin. Invest. 1999, 103:1227-1230
    • (1999) J. Clin. Invest. , vol.103 , pp. 1227-1230
    • Eliceiri, B.P.1    Cheresh, D.A.2
  • 2
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer RA, Sachsenmaier C, Cooper JA, Soriano P: Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 1999, 18:2459-2471
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 3
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb M, Polte T, Hanks S: Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: a role for Src family kinases. Mol. Cell. Biol. 1995, 15:954-963
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.1    Polte, T.2    Hanks, S.3
  • 4
    • 6844259884 scopus 로고    scopus 로고
    • Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential
    • Mao W, Irby R, Coppola D, Fu L, Wloch M, Turner J, Yu H, Garcia R, Jove R, Yeatman T: Activation of c-Src by receptor tyrosine kinases in human colon cancer cells with high metastatic potential. Oncogene. 1997, 15:3083-3090
    • (1997) Oncogene , vol.15 , pp. 3083-3090
    • Mao, W.1    Irby, R.2    Coppola, D.3    Fu, L.4    Wloch, M.5    Turner, J.6    Yu, H.7    Garcia, R.8    Jove, R.9    Yeatman, T.10
  • 6
    • 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, Hirai H: A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J 1994, 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
  • 7
    • 0030889320 scopus 로고    scopus 로고
    • Characterization of the kinase activity essential for tyrosine phosphorylation of p130Cas in fibroblasts
    • Sakai R, Nakamoto T, Ozawa K, Aizawa S, Hirai H: Characterization of the kinase activity essential for tyrosine phosphorylation of p130Cas in fibroblasts. Oncogene. 1997, 14:1419-1426
    • (1997) Oncogene , vol.14 , pp. 1419-1426
    • Sakai, R.1    Nakamoto, T.2    Ozawa, K.3    Aizawa, S.4    Hirai, H.5
  • 8
    • 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, Ruoslahti E: Introduction of p130cas signaling complex formation upon integrin-mediated cell adhesion: a role for Src family kinases. Mol. Cell. Biol. 1996, 16:2606-2613
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 9
    • 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. 1995, 270:22259-22262
    • (1995) J. Biol. Chem. , vol.270 , pp. 22259-22262
    • Vuori, K.1    Ruoslahti, E.2
  • 11
    • 0028790834 scopus 로고
    • Ornithine decarboxylase- and ras-induced cell transformations: Reversal by protein tyrosine kinase inhibitors and role of pp130CAS
    • Auvinen M, Paasinen-Sohns A, Hirai H, Andersson L, Holtta E: Ornithine decarboxylase- and ras-induced cell transformations: reversal by protein tyrosine kinase inhibitors and role of pp130CAS. Mol. Cell. Biol. 1995, 15:6513-6525
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6513-6525
    • Auvinen, M.1    Paasinen-Sohns, A.2    Hirai, H.3    Andersson, L.4    Holtta, E.5
  • 12
    • 0026658116 scopus 로고
    • Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro
    • Birge R, Fajardo J, Mayer B, Hanafusa H: Tyrosine-phosphorylated epidermal growth factor receptor and cellular p130 provide high affinity binding substrates to analyze Crk-phosphotyrosine-dependent interactions in vitro. J. Biol. Chem. 1992, 267:10588-10595
    • (1992) J. Biol. Chem. , vol.267 , pp. 10588-10595
    • Birge, R.1    Fajardo, J.2    Mayer, B.3    Hanafusa, H.4
  • 15
    • 0033584466 scopus 로고    scopus 로고
    • Cas, an assembling molecule of actin filaments, promotes cell movement, cell migration, and cell spreading in fibroblasts
    • Cas, an assembling molecule of actin filaments, promotes cell movement, cell migration, and cell spreading in fibroblasts. Biochem. Biophys. Res. Commun. 1999, 262:25-30
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 25-30
    • Honda, H.1    Nakamoto, T.2    Sakai, R.3    Hirai, H.4
  • 16
    • 0032559562 scopus 로고    scopus 로고
    • CAS/ Crk coupling serves as a "molecular switch" for induction of cell migration
    • Klemke R, Leng J, Molander R, Brooks P, Vuori K, Cheresh D: CAS/ Crk coupling serves as a "molecular switch" for induction of cell migration. J Cell Biol 1998, 140:961-972
    • (1998) J. Cell Biol. , vol.140 , pp. 961-972
    • Klemke, R.1    Leng, J.2    Molander, R.3    Brooks, P.4    Vuori, K.5    Cheresh, D.6
  • 17
    • 0033556443 scopus 로고    scopus 로고
    • Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: Differential involvement of focal adhesion kinase and p130Cas
    • Tamura M, Gu J, Takino T, Yamada K: Tumor suppressor PTEN inhibition of cell invasion, migration, and growth: differential involvement of focal adhesion kinase and p130Cas. Cancer Res 1999, 59:442-449
    • (1999) Cancer Res. , vol.59 , pp. 442-449
    • Tamura, M.1    Gu, J.2    Takino, T.3    Yamada, K.4
  • 19
    • 0035958959 scopus 로고    scopus 로고
    • Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions
    • Pellicena P, Miller W: Processive phosphorylation of p130Cas by Src depends on SH3-polyproline interactions. J. Biol. Chem. 2001, 276:28190-28196
    • (2001) J. Biol. Chem. , vol.276 , pp. 28190-28196
    • Pellicena, P.1    Miller, W.2
  • 20
    • 0032866076 scopus 로고    scopus 로고
    • Cas mediates transcriptional activation of the serum response element by Src
    • Hakak Y, Martin G: Cas mediates transcriptional activation of the serum response element by Src. Mol. Cell. Biol. 1999, 19:6953-6962
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 6953-6962
    • Hakak, Y.1    Martin, G.2
  • 23
    • 0033566368 scopus 로고    scopus 로고
    • Cas-binding thymic stromal cell protein regulated by adhesion and inflammatory cytokines
    • Cas-binding thymic stromal cell protein regulated by adhesion and inflammatory cytokines. J. lmmunol. 1999, 163:2104-2112
    • (1999) J. Immunol. , vol.163 , pp. 2104-2112
    • Cai, D.1    Clayton, L.2    Smolyar, A.3    Lerner, A.4
  • 27
    • 0034630157 scopus 로고    scopus 로고
    • Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells
    • Donaldson J, Dempsey P, Reddy S, Bouton A, Coffey R, Hanks S: Crk-associated substrate p130(Cas) interacts with nephrocystin and both proteins localize to cell-cell contacts of polarized epithelial cells. Exp. Cell Res. 2000, 256:168-178
    • (2000) Exp. Cell Res. , vol.256 , pp. 168-178
    • Donaldson, J.1    Dempsey, P.2    Reddy, S.3    Bouton, A.4    Coffey, R.5    Hanks, S.6
  • 29
    • 0029666251 scopus 로고    scopus 로고
    • Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase
    • Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase. J. Biol. Chem. 1996, 271:13649-13655
    • (1996) J. Biol. Chem. , vol.271 , pp. 13649-13655
    • Harte, M.1    Hildebrand, J.2    Burnham, M.3    Bouton, A.4    Parsons, J.5
  • 32
    • 0031962488 scopus 로고    scopus 로고
    • Transformation suppression by protein tyrosine phosphatase 1B requires a functional SH3 ligand
    • Liu F, Sells M, Chernoff J: Transformation suppression by protein tyrosine phosphatase 1B requires a functional SH3 ligand. Mol. Cell. Biol. 1998, 18:250-259
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 250-259
    • Liu, F.1    Sells, M.2    Chernoff, J.3
  • 35
    • 0023649672 scopus 로고
    • c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation
    • c-src transforming ability by mutation of its primary sites of tyrosine phosphorylation. Cell 1987, 49:65-73
    • (1987) Cell , vol.49 , pp. 65-73
    • Kmiecik, T.1    Shalloway, D.2
  • 36
    • 0025931005 scopus 로고
    • Regulation of the oncogenic activity of the cellular src protein requires the correct spacing between the kinase domain and the C-terminal phosphorylated tyrosine (Tyr-527)
    • Cobb B, Payne D, Reynolds A, Parsons J: Regulation of the oncogenic activity of the cellular src protein requires the correct spacing between the kinase domain and the C-terminal phosphorylated tyrosine (Tyr-527) Mol. Cell. Biol. 1991, 11:5832-5838
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 5832-5838
    • Cobb, B.1    Payne, D.2    Reynolds, A.3    Parsons, J.4
  • 37
    • 0027219262 scopus 로고
    • Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts
    • Birge R, Fajardo J, Reichman C, Shoelson S, Songyang Z, Cantley L, Hanafusa H: Identification and characterization of a high-affinity interaction between v-Crk and tyrosine-phosphorylated paxillin in CT10-transformed fibroblasts. Mol. Cell. Biol. 1993, 13:4648-4656
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 4648-4656
    • Birge, R.1    Fajardo, J.2    Reichman, C.3    Shoelson, S.4    Songyang, Z.5    Cantley, L.6    Hanafusa, H.7
  • 38
    • 0031004266 scopus 로고    scopus 로고
    • Downstream of Crk adaptor signaling pathway: Activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G
    • Tanaka S, Ouchi T, Hanafusa H: Downstream of Crk adaptor signaling pathway: activation of Jun kinase by v-Crk through the guanine nucleotide exchange protein C3G. Proc. Natl. Acad. Sci. USA 1997, 94:2356-2361
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2356-2361
    • Tanaka, S.1    Ouchi, T.2    Hanafusa, H.3
  • 39
    • 0030180321 scopus 로고    scopus 로고
    • SH2 and SH3-containing adaptor proteins: Redundant or independent mediators of intracellular signal transduction
    • Birge R, Knudsen B, Besser D, Hanafusa H: SH2 and SH3-containing adaptor proteins: redundant or independent mediators of intracellular signal transduction. Genes Cells 1996, 1:595-613
    • (1996) Genes Cells , vol.1 , pp. 595-613
    • Birge, R.1    Knudsen, B.2    Besser, D.3    Hanafusa, H.4
  • 40
    • 0031080595 scopus 로고    scopus 로고
    • Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck
    • Lu W, Katz S, Gupta R, Mayer B: Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. Curr. Biol. 1997, 7:85-94
    • (1997) Curr. Biol. , vol.7 , pp. 85-94
    • Lu, W.1    Katz, S.2    Gupta, R.3    Mayer, B.4
  • 41
    • 17444453459 scopus 로고    scopus 로고
    • The effects of phosphorylation on adaptor protein function
    • Cherezova L, Gatesman A, Flynn D: The effects of phosphorylation on adaptor protein function. Front. Biosci. 2002, 7:d164-203
    • (2002) Front. Biosci. , vol.7
    • Cherezova, L.1    Gatesman, A.2    Flynn, D.3
  • 42
    • 0029257493 scopus 로고
    • Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases
    • Mayer B, Hirai H, Sakai R: Evidence that SH2 domains promote processive phosphorylation by protein-tyrosine kinases. Curr. Biol. 1995, 5:296-305
    • (1995) Curr. Biol. , vol.5 , pp. 296-305
    • Mayer, B.1    Hirai, H.2    Sakai, R.3
  • 43
    • 0034769929 scopus 로고    scopus 로고
    • Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src
    • Ruest PJ, Shin N-Y, Polte TR, Zhang X, Hanks SK: Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src. Mol. Cell. Biol. 2001, 21:7641-7652
    • (2001) Mol. Cell. Biol. , vol.21 , pp. 7641-7652
    • Ruest, P.J.1    Shin, N.-Y.2    Polte, T.R.3    Zhang, X.4    Hanks, S.K.5
  • 44
    • 0031032777 scopus 로고    scopus 로고
    • Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: Involvement of the Grb2, p130cas, and Nck adaptor proteins
    • Schlaepfer D, Broome M, Hunter T: Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins. Mol. Cell. Biol. 1997, 17:1702-1713
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1702-1713
    • Schlaepfer, D.1    Broome, M.2    Hunter, T.3
  • 45
    • 0029666251 scopus 로고    scopus 로고
    • p130Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase
    • Harte M, Hildebrand J, Burnham M, Bouton A, Parsons J: p130Cas, a substrate associated with v-Src and v-Crk, localizes to focal adhesions and binds to focal adhesion kinase. J. Biol. Chem. 1996, 271:13649-13655
    • (1996) J. Biol. Chem. , vol.271 , pp. 13649-13655
    • Harte, M.1    Hildebrand, J.2    Burnham, M.3    Bouton, A.4    Parsons, J.5
  • 46
    • 0028260229 scopus 로고
    • Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src
    • Sabe H, Hata A, Okada M, Nakagawa H, Hanafusa H: Analysis of the binding of the Src homology 2 domain of Csk to tyrosine-phosphorylated proteins in the suppression and mitotic activation of c-Src. PNAS 1994, 91:3984-3988
    • (1994) PNAS , vol.91 , pp. 3984-3988
    • Sabe, H.1    Hata, A.2    Okada, M.3    Nakagawa, H.4    Hanafusa, H.5
  • 47
    • 0028926468 scopus 로고
    • Epitope-tag vectors for eukaryotic protein production
    • Sells M, Chernoff J: Epitope-tag vectors for eukaryotic protein production. Gene 1995, 152:187-189
    • (1995) Gene , vol.152 , pp. 187-189
    • Sells, M.1    Chernoff, J.2
  • 48
    • 0030826662 scopus 로고    scopus 로고
    • Src-induced activation of inducible T cell kinase (ITK) requires phosphatidylinositol 3-kinase activity and the Pleckstrin homology domain of inducible T cell kinase
    • August A, Sadra A, Dupont B, Hanafusa H: Src-induced activation of inducible T cell kinase (ITK) requires phosphatidylinositol 3-kinase activity and the Pleckstrin homology domain of inducible T cell kinase. Proc. Natl. Acad. Sci. USA 1997, 94:11227-11232
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11227-11232
    • August, A.1    Sadra, A.2    Dupont, B.3    Hanafusa, H.4
  • 49
    • 0026648707 scopus 로고
    • Activation of c-Src in cells bearing v-Crk and its suppression by Csk
    • Sabe H, Okada M, Nakagawa H, Hanafusa H: Activation of c-Src in cells bearing v-Crk and its suppression by Csk. Mol. Cell. Biol. 1992, 12:4706-4713
    • (1992) Mol. Cell. Biol. , vol.12 , pp. 4706-4713
    • Sabe, H.1    Okada, M.2    Nakagawa, H.3    Hanafusa, H.4
  • 50
    • 0025352651 scopus 로고
    • Mutagenic analysis of the v-crk oncogene: Requirement for SH2 and SH3 domains and correlation between increased cellular phosphotyrosine and transformation
    • Mayer B, Hanafusa H: Mutagenic analysis of the v-crk oncogene: requirement for SH2 and SH3 domains and correlation between increased cellular phosphotyrosine and transformation. J. Virol. 1990, 64:3581-3589
    • (1990) J. Virol. , vol.64 , pp. 3581-3589
    • Mayer, B.1    Hanafusa, H.2
  • 51
    • 0028176009 scopus 로고
    • v-src transformation of rat embryo fibroblasts. Inefficient conversion to anchorage-independent growth involves heterogeneity of primary cultures
    • Tavoloni N, Inoue H, Sabe H, Hanafusa H: v-src transformation of rat embryo fibroblasts. Inefficient conversion to anchorage-independent growth involves heterogeneity of primary cultures. J. Cell. Biol. 1994, 126:475-483
    • (1994) J. Cell. Biol. , vol.126 , pp. 475-483
    • Tavoloni, N.1    Inoue, H.2    Sabe, H.3    Hanafusa, H.4


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