메뉴 건너뛰기




Volumn 382, Issue 1, 2009, Pages 210-214

SHP-2 inhibits tyrosine phosphorylation of Cas-L and regulates cell migration

Author keywords

Cas L; Cell migration; Focal adhesion; SHP 2; Tyrosine phosphorylation

Indexed keywords

CRK ASSOCIATED SUBSTRATE PROTEIN; FIBRONECTIN; PROTEIN TYROSINE PHOSPHATASE SHP; PROTEIN TYROSINE PHOSPHATASE SHP 2;

EID: 63149148150     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2009.03.010     Document Type: Article
Times cited : (4)

References (32)
  • 1
    • 0029904694 scopus 로고    scopus 로고
    • Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes
    • Minegishi M., Tachibana K., Sato T., Iwata S., Nojima Y., and Morimoto C. Structure and function of Cas-L, a 105-kD Crk-associated substrate-related protein that is involved in beta 1 integrin-mediated signaling in lymphocytes. J. Exp. Med. 184 (1996) 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
  • 4
    • 0033214510 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta 1 integrin-induced T lymphocyte migration
    • Ohashi Y., Iwata S., Kamiguchi K., and Morimoto C. Tyrosine phosphorylation of Crk-associated substrate lymphocyte-type is a critical element in TCR- and beta 1 integrin-induced T lymphocyte migration. J. Immunol. 163 (1999) 3727-3734
    • (1999) J. Immunol. , vol.163 , pp. 3727-3734
    • Ohashi, Y.1    Iwata, S.2    Kamiguchi, K.3    Morimoto, C.4
  • 8
    • 0031813880 scopus 로고    scopus 로고
    • Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments
    • Law S.F., Zhang Y.Z., Klein-Szanto A.J., and Golemis E.A. Cell cycle-regulated processing of HEF1 to multiple protein forms differentially targeted to multiple subcellular compartments. Mol. Cell Biol. 18 (1998) 3540-3551
    • (1998) Mol. Cell Biol. , vol.18 , pp. 3540-3551
    • Law, S.F.1    Zhang, Y.Z.2    Klein-Szanto, A.J.3    Golemis, E.A.4
  • 9
    • 33644868709 scopus 로고    scopus 로고
    • Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle
    • Dadke D., Jarnik M., Pugacheva E.N., Singh M.K., and Golemis E.A. Deregulation of HEF1 impairs M-phase progression by disrupting the RhoA activation cycle. Mol. Biol. Cell 17 (2006) 1204-1217
    • (2006) Mol. Biol. Cell , vol.17 , pp. 1204-1217
    • Dadke, D.1    Jarnik, M.2    Pugacheva, E.N.3    Singh, M.K.4    Golemis, E.A.5
  • 10
    • 33645220356 scopus 로고    scopus 로고
    • HEF1-aurora A interactions: points of dialog between the cell cycle and cell attachment signaling networks
    • Pugacheva E.N., and Golemis E.A. HEF1-aurora A interactions: points of dialog between the cell cycle and cell attachment signaling networks. Cell Cycle 5 (2006) 384-391
    • (2006) Cell Cycle , vol.5 , pp. 384-391
    • Pugacheva, E.N.1    Golemis, E.A.2
  • 11
    • 27144495462 scopus 로고    scopus 로고
    • The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome
    • Pugacheva E.N., and Golemis E.A. The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome. Nat. Cell Biol. 7 (2005) 937-946
    • (2005) Nat. Cell Biol. , vol.7 , pp. 937-946
    • Pugacheva, E.N.1    Golemis, E.A.2
  • 12
    • 0034959232 scopus 로고    scopus 로고
    • Proteolysis of the docking protein HEF1 and implications for focal adhesion dynamics
    • O'Neill G.M., and Golemis E.A. Proteolysis of the docking protein HEF1 and implications for focal adhesion dynamics. Mol. Cell Biol. 21 (2001) 5094-5108
    • (2001) Mol. Cell Biol. , vol.21 , pp. 5094-5108
    • O'Neill, G.M.1    Golemis, E.A.2
  • 14
    • 0032513128 scopus 로고    scopus 로고
    • T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G
    • Ohashi Y., Tachibana K., Kamiguchi K., Fujita H., and Morimoto C. T cell receptor-mediated tyrosine phosphorylation of Cas-L, a 105-kDa Crk-associated substrate-related protein, and its association of Crk and C3G. J. Biol. Chem. 273 (1998) 6446-6451
    • (1998) J. Biol. Chem. , vol.273 , pp. 6446-6451
    • Ohashi, Y.1    Tachibana, K.2    Kamiguchi, K.3    Fujita, H.4    Morimoto, C.5
  • 15
    • 1542289021 scopus 로고    scopus 로고
    • Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor
    • Ren Y., Meng S., Mei L., Zhao Z.J., Jove R., and Wu J. Roles of Gab1 and SHP2 in paxillin tyrosine dephosphorylation and Src activation in response to epidermal growth factor. J. Biol. Chem. 279 (2004) 8497-8505
    • (2004) J. Biol. Chem. , vol.279 , pp. 8497-8505
    • Ren, Y.1    Meng, S.2    Mei, L.3    Zhao, Z.J.4    Jove, R.5    Wu, J.6
  • 16
    • 0039441744 scopus 로고    scopus 로고
    • Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility
    • Manes S., Mira E., Gomez-Mouton C., Zhao Z.J., Lacalle R.A., and Martinez A.C. Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility. Mol. Cell Biol. 19 (1999) 3125-3135
    • (1999) Mol. Cell Biol. , vol.19 , pp. 3125-3135
    • Manes, S.1    Mira, E.2    Gomez-Mouton, C.3    Zhao, Z.J.4    Lacalle, R.A.5    Martinez, A.C.6
  • 17
    • 34547610472 scopus 로고    scopus 로고
    • Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase
    • Guo H.B., Randolph M., and Pierce M. Inhibition of a specific N-glycosylation activity results in attenuation of breast carcinoma cell invasiveness-related phenotypes: inhibition of epidermal growth factor-induced dephosphorylation of focal adhesion kinase. J. Biol. Chem. 282 (2007) 22150-22162
    • (2007) J. Biol. Chem. , vol.282 , pp. 22150-22162
    • Guo, H.B.1    Randolph, M.2    Pierce, M.3
  • 18
    • 33744764925 scopus 로고    scopus 로고
    • A discoidin domain receptor 1/SHP-2 signaling complex inhibits alpha2beta1-integrin-mediated signal transducers and activators of transcription 1/3 activation and cell migration
    • Wang C.Z., Su H.W., Hsu Y.C., Shen M.R., and Tang M.J. A discoidin domain receptor 1/SHP-2 signaling complex inhibits alpha2beta1-integrin-mediated signal transducers and activators of transcription 1/3 activation and cell migration. Mol. Biol. Cell 17 (2006) 2839-2852
    • (2006) Mol. Biol. Cell , vol.17 , pp. 2839-2852
    • Wang, C.Z.1    Su, H.W.2    Hsu, Y.C.3    Shen, M.R.4    Tang, M.J.5
  • 19
    • 53049096122 scopus 로고    scopus 로고
    • Potential molecular mechanism for c-Src kinase-mediated regulation of intestinal cell migration
    • Mathew S., George S.P., Wang Y., Siddiqui M.R., Srinivasan K., Tan L., and Khurana S. Potential molecular mechanism for c-Src kinase-mediated regulation of intestinal cell migration. J. Biol. Chem. 283 (2008) 22709-22722
    • (2008) J. Biol. Chem. , vol.283 , pp. 22709-22722
    • Mathew, S.1    George, S.P.2    Wang, Y.3    Siddiqui, M.R.4    Srinivasan, K.5    Tan, L.6    Khurana, S.7
  • 21
    • 0028136280 scopus 로고
    • Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin
    • Milarski K.L., and Saltiel A.R. Expression of catalytically inactive Syp phosphatase in 3T3 cells blocks stimulation of mitogen-activated protein kinase by insulin. J. Biol. Chem. 269 (1994) 21239-21243
    • (1994) J. Biol. Chem. , vol.269 , pp. 21239-21243
    • Milarski, K.L.1    Saltiel, A.R.2
  • 22
    • 0038190924 scopus 로고    scopus 로고
    • Development of an efficient "Substrate-trapping" mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates
    • Agazie Y.M., and Hayman M.J. Development of an efficient "Substrate-trapping" mutant of Src homology phosphotyrosine phosphatase 2 and identification of the epidermal growth factor receptor, Gab1, and three other proteins as target substrates. J. Biol. Chem. 278 (2003) 13952-13958
    • (2003) J. Biol. Chem. , vol.278 , pp. 13952-13958
    • Agazie, Y.M.1    Hayman, M.J.2
  • 23
    • 3142751435 scopus 로고    scopus 로고
    • The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling
    • Kolli S., Zito C.I., Mossink M.H., Wiemer E.A., and Bennett A.M. The major vault protein is a novel substrate for the tyrosine phosphatase SHP-2 and scaffold protein in epidermal growth factor signaling. J. Biol. Chem. 279 (2004) 29374-29385
    • (2004) J. Biol. Chem. , vol.279 , pp. 29374-29385
    • Kolli, S.1    Zito, C.I.2    Mossink, M.H.3    Wiemer, E.A.4    Bennett, A.M.5
  • 24
    • 0029891787 scopus 로고    scopus 로고
    • Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae
    • Law S.F., Estojak J., Wang B., Mysliwiec T., Kruh G., and Golemis E.A. Human enhancer of filamentation 1, a novel p130cas-like docking protein, associates with focal adhesion kinase and induces pseudohyphal growth in Saccharomyces cerevisiae. Mol. Cell Biol. 16 (1996) 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
  • 25
    • 3543036342 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion
    • Yu D.H., Qu C.K., Henegariu O., Lu X., and Feng G.S. Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J. Biol. Chem. 273 (1998) 21125-21131
    • (1998) J. Biol. Chem. , vol.273 , pp. 21125-21131
    • Yu, D.H.1    Qu, C.K.2    Henegariu, O.3    Lu, X.4    Feng, G.S.5
  • 27
    • 0029826289 scopus 로고    scopus 로고
    • Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST
    • Garton A.J., Flint A.J., and Tonks N.K. Identification of p130(cas) as a substrate for the cytosolic protein tyrosine phosphatase PTP-PEST. Mol. Cell Biol. 16 (1996) 6408-6418
    • (1996) Mol. Cell Biol. , vol.16 , pp. 6408-6418
    • Garton, A.J.1    Flint, A.J.2    Tonks, N.K.3
  • 30
    • 33645745233 scopus 로고    scopus 로고
    • Enhanced sensitivity to inhibition of SHP2, STAT5, and Gab2 expression in chronic myeloid leukemia (CML)
    • Scherr M., Chaturvedi A., Battmer K., Dallmann I., Schultheis B., Ganser A., and Eder M. Enhanced sensitivity to inhibition of SHP2, STAT5, and Gab2 expression in chronic myeloid leukemia (CML). Blood 107 (2006) 3279-3287
    • (2006) Blood , vol.107 , pp. 3279-3287
    • Scherr, M.1    Chaturvedi, A.2    Battmer, K.3    Dallmann, I.4    Schultheis, B.5    Ganser, A.6    Eder, M.7
  • 31
    • 33846223147 scopus 로고    scopus 로고
    • SHP-2 phosphatase is required for hematopoietic cell transformation by Bcr-Abl
    • Chen J., Yu W.M., Daino H., Broxmeyer H.E., Druker B.J., and Qu C.K. SHP-2 phosphatase is required for hematopoietic cell transformation by Bcr-Abl. Blood 109 (2007) 778-785
    • (2007) Blood , vol.109 , pp. 778-785
    • Chen, J.1    Yu, W.M.2    Daino, H.3    Broxmeyer, H.E.4    Druker, B.J.5    Qu, C.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.