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Volumn 288, Issue 52, 2013, Pages 36926-36935

Receptor protein-tyrosine phosphatase α regulates focal adhesion kinase phosphorylation and ErbB2 oncoproteinmediated mammary epithelial cell motility

Author keywords

[No Author keywords available]

Indexed keywords

BREAST CANCER; BREAST CANCER CELLS; FOCAL ADHESION KINASE; MAMMARY EPITHELIAL CELLS; PROTEIN-TYROSINE PHOSPHATASE; SIGNALING EVENTS;

EID: 84891397565     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M113.527564     Document Type: Article
Times cited : (18)

References (78)
  • 1
    • 63749113783 scopus 로고    scopus 로고
    • Tyrosine phosphorylation. Thirty years and counting
    • Hunter, T. (2009) Tyrosine phosphorylation. Thirty years and counting. Curr. Opin. Cell Biol. 21, 140-146
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 140-146
    • Hunter, T.1
  • 2
    • 0035902180 scopus 로고    scopus 로고
    • Oncogenic kinase signalling
    • Blume-Jensen, P., and Hunter, T. (2001) Oncogenic kinase signalling. Nature 411, 355-365
    • (2001) Nature , vol.411 , pp. 355-365
    • Blume-Jensen, P.1    Hunter, T.2
  • 4
  • 5
    • 77952887713 scopus 로고    scopus 로고
    • The SYK tyrosine kinase. A crucial player in diverse biological functions
    • Mócsai, A., Ruland, J., and Tybulewicz, V. L. (2010) The SYK tyrosine kinase. A crucial player in diverse biological functions. Nat. Rev. Immunol. 10, 387-402
    • (2010) Nat. Rev. Immunol. , vol.10 , pp. 387-402
    • Mócsai, A.1    Ruland, J.2    Tybulewicz, V.L.3
  • 6
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases. From genes, to function, to disease
    • Tonks, N. K. (2006) Protein tyrosine phosphatases. From genes, to function, to disease. Nat. Rev. Mol. Cell Biol. 7, 833-846
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 7
  • 8
    • 0025049129 scopus 로고
    • Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine-phosphatases expressed in brain
    • Kaplan, R., Morse, B., Huebner, K., Croce, C., Howk, R., Ravera, M., Ricca, G., Jaye, M., and Schlessinger, J. (1990) Cloning of three human tyrosine phosphatases reveals a multigene family of receptor-linked protein-tyrosine- phosphatases expressed in brain. Proc. Natl. Acad. Sci. U.S.A. 87, 7000-7004
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 7000-7004
    • Kaplan, R.1    Morse, B.2    Huebner, K.3    Croce, C.4    Howk, R.5    Ravera, M.6    Ricca, G.7    Jaye, M.8    Schlessinger, J.9
  • 9
    • 0025146562 scopus 로고
    • Structural diversity and evolution of human receptor-like protein tyrosine phosphatases
    • Krueger, N. X., Streuli, M., and Saito, H. (1990) Structural diversity and evolution of human receptor-like protein tyrosine phosphatases. EMBO J. 9, 3241-3252
    • (1990) EMBO J. , vol.9 , pp. 3241-3252
    • Krueger, N.X.1    Streuli, M.2    Saito, H.3
  • 10
    • 0025376471 scopus 로고
    • Identification of an additional member of the protein-tyrosine- phosphatase family. Evidence for alternative splicing in the tyrosine phosphatase domain
    • Matthews, R. J., Cahir, E. D., and Thomas, M. L. (1990) Identification of an additional member of the protein-tyrosine-phosphatase family. Evidence for alternative splicing in the tyrosine phosphatase domain. Proc. Natl. Acad. Sci. U.S.A. 87, 4444-4448
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 4444-4448
    • Matthews, R.J.1    Cahir, E.D.2    Thomas, M.L.3
  • 11
    • 0035503358 scopus 로고    scopus 로고
    • Two mechanisms activate PTPα during mitosis
    • Zheng, X. M., and Shalloway, D. (2001) Two mechanisms activate PTPα during mitosis. EMBO J. 20, 6037-6049
    • (2001) EMBO J. , vol.20 , pp. 6037-6049
    • Zheng, X.M.1    Shalloway, D.2
  • 13
    • 0037647185 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase α (PTPα). A Src family kinase activator and mediator of multiple biological effects
    • Pallen, C. J. (2003) Protein tyrosine phosphatase α (PTPα). A Src family kinase activator and mediator of multiple biological effects. Curr. Top. Med. Chem. 3, 821-835
    • (2003) Curr. Top. Med. Chem. , vol.3 , pp. 821-835
    • Pallen, C.J.1
  • 14
    • 1242342002 scopus 로고    scopus 로고
    • Preferential oxidation of the second phosphatase domain of receptor-like PTP-α revealed by an antibody against oxidized protein tyrosine phosphatases
    • Persson, C., Sjöblom, T., Groen, A., Kappert, K., Engström, U., Hellman, U., Heldin, C. H., den Hertog, J., and Ostman, A. (2004) Preferential oxidation of the second phosphatase domain of receptor-like PTP-α revealed by an antibody against oxidized protein tyrosine phosphatases. Proc. Natl. Acad. Sci. U.S.A. 101, 1886-1891
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 1886-1891
    • Persson, C.1    Sjöblom, T.2    Groen, A.3    Kappert, K.4    Engström, U.5    Hellman, U.6    Heldin, C.H.7    Den Hertog, J.8    Ostman, A.9
  • 15
    • 33846456252 scopus 로고    scopus 로고
    • Reversible oxidation of the membrane distal domain of receptor PTPα is mediated by a cyclic sulfenamide
    • Yang, J., Groen, A., Lemeer, S., Jans, A., Slijper, M., Roe, S. M., den Hertog, J., and Barford, D. (2007) Reversible oxidation of the membrane distal domain of receptor PTPα is mediated by a cyclic sulfenamide. Biochemistry 46, 709-719
    • (2007) Biochemistry , vol.46 , pp. 709-719
    • Yang, J.1    Groen, A.2    Lemeer, S.3    Jans, A.4    Slijper, M.5    Roe, S.M.6    Den Hertog, J.7    Barford, D.8
  • 16
    • 0037561996 scopus 로고    scopus 로고
    • Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase α dimers
    • van der Wijk, T., Blanchetot, C., Overvoorde, J., and den Hertog, J. (2003) Redox-regulated rotational coupling of receptor protein-tyrosine phosphatase α dimers. J. Biol. Chem. 278, 13968-13974
    • (2003) J. Biol. Chem. , vol.278 , pp. 13968-13974
    • Van Der-Wijk, T.1    Blanchetot, C.2    Overvoorde, J.3    Den Hertog, J.4
  • 17
    • 0026705734 scopus 로고
    • c-src by overexpression of a protein tyrosine phosphatase
    • c-src by overexpression of a protein tyrosine phosphatase. Nature 359, 336-339
    • (1992) Nature , vol.359 , pp. 336-339
    • Zheng, X.M.1    Wang, Y.2    Pallen, C.J.3
  • 18
    • 0033587177 scopus 로고    scopus 로고
    • Targeted disruption of the tyrosine phosphatase PTPα leads to constitutive downregulation of the kinases Src and Fyn
    • Ponniah, S., Wang, D. Z., Lim, K. L., and Pallen, C. J. (1999) Targeted disruption of the tyrosine phosphatase PTPα leads to constitutive downregulation of the kinases Src and Fyn. Curr. Biol. 9, 535-538
    • (1999) Curr. Biol. , vol.9 , pp. 535-538
    • Ponniah, S.1    Wang, D.Z.2    Lim, K.L.3    Pallen, C.J.4
  • 19
    • 0033587069 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase α activates Src-family kinases and controls integrin-mediated responses in fibroblasts
    • Su, J., Muranjan, M., and Sap, J. (1999) Receptor protein tyrosine phosphatase α activates Src-family kinases and controls integrin-mediated responses in fibroblasts. Curr. Biol. 9, 505-511
    • (1999) Curr. Biol. , vol.9 , pp. 505-511
    • Su, J.1    Muranjan, M.2    Sap, J.3
  • 20
    • 33847391938 scopus 로고    scopus 로고
    • A brake becomes an accelerator. PTP1B. A new therapeutic target for breast cancer
    • Tonks, N. K., and Muthuswamy, S. K. (2007) A brake becomes an accelerator. PTP1B. A new therapeutic target for breast cancer. Cancer Cell 11, 214-216
    • (2007) Cancer Cell , vol.11 , pp. 214-216
    • Tonks, N.K.1    Muthuswamy, S.K.2
  • 21
    • 0034616884 scopus 로고    scopus 로고
    • Identification of p130cas as an in vivo substrate of receptor protein-tyrosine phosphatase α
    • Buist, A., Blanchetot, C., Tertoolen, L. G., and den Hertog, J. (2000) Identification of p130cas as an in vivo substrate of receptor protein-tyrosine phosphatase α. J. Biol. Chem. 275, 20754-20761
    • (2000) J. Biol. Chem. , vol.275 , pp. 20754-20761
    • Buist, A.1    Blanchetot, C.2    Tertoolen, L.G.3    Den Hertog, J.4
  • 22
    • 0033521647 scopus 로고    scopus 로고
    • Receptor protein tyrosine phosphatase α participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity
    • Tsai, W., Morielli, A. D., Cachero, T. G., and Peralta, E. G. (1999) Receptor protein tyrosine phosphatase α participates in the m1 muscarinic acetylcholine receptor-dependent regulation of Kv1.2 channel activity. EMBO J. 18, 109-118
    • (1999) EMBO J. , vol.18 , pp. 109-118
    • Tsai, W.1    Morielli, A.D.2    Cachero, T.G.3    Peralta, E.G.4
  • 24
    • 0028981510 scopus 로고
    • Increased mRNA expression of the receptor-like protein tyrosine phosphatase α in late stage colon carcinomas
    • Tabiti, K., Smith, D. R., Goh, H. S., and Pallen, C. J. (1995) Increased mRNA expression of the receptor-like protein tyrosine phosphatase α in late stage colon carcinomas. Cancer Lett. 93, 239-248
    • (1995) Cancer Lett. , vol.93 , pp. 239-248
    • Tabiti, K.1    Smith, D.R.2    Goh, H.S.3    Pallen, C.J.4
  • 25
    • 0033031099 scopus 로고    scopus 로고
    • Expression of the transmembrane protein tyrosine phosphatase RPTPα in human oral squamous cell carcinoma
    • Berndt, A., Luo, X., Böhmer, F. D., and Kosmehl, H. (1999) Expression of the transmembrane protein tyrosine phosphatase RPTPα in human oral squamous cell carcinoma. Histochem. Cell Biol. 111, 399-403
    • (1999) Histochem. Cell Biol. , vol.111 , pp. 399-403
    • Berndt, A.1    Luo, X.2    Böhmer, F.D.3    Kosmehl, H.4
  • 26
    • 33749267414 scopus 로고    scopus 로고
    • Protein tyrosine-phosphatase expression profiling in gastric cancer tissues
    • Wu, C. W., Kao, H. L., Li, A. F., Chi, C. W., and Lin, W. C. (2006) Protein tyrosine-phosphatase expression profiling in gastric cancer tissues. Cancer Lett. 242, 95-103
    • (2006) Cancer Lett. , vol.242 , pp. 95-103
    • Wu, C.W.1    Kao, H.L.2    Li, A.F.3    Chi, C.W.4    Lin, W.C.5
  • 27
    • 0034641876 scopus 로고    scopus 로고
    • Expression of protein tyrosine phosphatase α (RPTPα) in human breast cancer correlates with low tumor grade, and inhibits tumor cell growth in vitro and in vivo
    • Ardini, E., Agresti, R., Tagliabue, E., Greco, M., Aiello, P., Yang, L. T., Ménard, S., and Sap, J. (2000) Expression of protein tyrosine phosphatase α (RPTPα) in human breast cancer correlates with low tumor grade, and inhibits tumor cell growth in vitro and in vivo. Oncogene 19, 4979-4987
    • (2000) Oncogene , vol.19 , pp. 4979-4987
    • Ardini, E.1    Agresti, R.2    Tagliabue, E.3    Greco, M.4    Aiello, P.5    Yang, L.T.6    Ménard, S.7    Sap, J.8
  • 29
    • 0037023768 scopus 로고    scopus 로고
    • Identification of novel non-phosphorylated ligands, which bind selectively to the SH2 domain of Grb7
    • Pero, S. C., Oligino, L., Daly, R. J., Soden, A. L., Liu, C., Roller, P. P., Li, P., and Krag, D. N. (2002) Identification of novel non-phosphorylated ligands, which bind selectively to the SH2 domain of Grb7. J. Biol. Chem. 277, 11918-11926
    • (2002) J. Biol. Chem. , vol.277 , pp. 11918-11926
    • Pero, S.C.1    Oligino, L.2    Daly, R.J.3    Soden, A.L.4    Liu, C.5    Roller, P.P.6    Li, P.7    Krag, D.N.8
  • 31
    • 79958072314 scopus 로고    scopus 로고
    • Analysis of the redox regulation of protein tyrosine phosphatase superfamily members utilizing a cysteinyllabeling assay
    • Boivin, B., and Tonks, N. K. (2010) Analysis of the redox regulation of protein tyrosine phosphatase superfamily members utilizing a cysteinyllabeling assay. Methods Enzymol. 474, 35-50
    • (2010) Methods Enzymol. , vol.474 , pp. 35-50
    • Boivin, B.1    Tonks, N.K.2
  • 33
    • 79959959024 scopus 로고    scopus 로고
    • Identification of PTPN23 as a novel regulator of cell invasion in mammary epithelial cells from a loss-of-function screen of the "PTP-ome."
    • Lin, G., Aranda, V., Muthuswamy, S. K., and Tonks, N. K. (2011) Identification of PTPN23 as a novel regulator of cell invasion in mammary epithelial cells from a loss-of-function screen of the "PTP-ome." Genes Dev. 25, 1412-1425
    • (2011) Genes Dev. , vol.25 , pp. 1412-1425
    • Lin, G.1    Aranda, V.2    Muthuswamy, S.K.3    Tonks, N.K.4
  • 34
    • 40749094921 scopus 로고    scopus 로고
    • Apoptosis of estrogenreceptor negative breast cancer and colon cancer cell lines by PTP α and Src RNAi
    • Zheng, X., Resnick, R. J., and Shalloway, D. (2008) Apoptosis of estrogenreceptor negative breast cancer and colon cancer cell lines by PTP α and Src RNAi. Int. J. Cancer 122, 1999-2007
    • (2008) Int. J. Cancer , vol.122 , pp. 1999-2007
    • Zheng, X.1    Resnick, R.J.2    Shalloway, D.3
  • 35
    • 0034854417 scopus 로고    scopus 로고
    • ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial acini
    • Muthuswamy, S. K., Li, D., Lelievre, S., Bissell, M. J., and Brugge, J. S. (2001) ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial acini. Nat. Cell Biol. 3, 785-792
    • (2001) Nat. Cell Biol. , vol.3 , pp. 785-792
    • Muthuswamy, S.K.1    Li, D.2    Lelievre, S.3    Bissell, M.J.4    Brugge, J.S.5
  • 36
    • 0642276003 scopus 로고    scopus 로고
    • Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction
    • Chiarugi, P., and Cirri, P. (2003) Redox regulation of protein tyrosine phosphatases during receptor tyrosine kinase signal transduction. Trends Biochem. Sci. 28, 509-514
    • (2003) Trends Biochem. Sci. , vol.28 , pp. 509-514
    • Chiarugi, P.1    Cirri, P.2
  • 37
    • 4444233558 scopus 로고    scopus 로고
    • Regulation of insulin signaling through reversible oxidation of the proteintyrosine phosphatases TC45 and PTP1B
    • Meng, T. C., Buckley, D. A., Galic, S., Tiganis, T., and Tonks, N. K. (2004) Regulation of insulin signaling through reversible oxidation of the proteintyrosine phosphatases TC45 and PTP1B. J. Biol. Chem. 279, 37716-37725
    • (2004) J. Biol. Chem. , vol.279 , pp. 37716-37725
    • Meng, T.C.1    Buckley, D.A.2    Galic, S.3    Tiganis, T.4    Tonks, N.K.5
  • 38
    • 36549070172 scopus 로고    scopus 로고
    • Fluorescent probes for nitric oxide and hydrogen peroxide in cell signaling
    • Miller, E. W., and Chang, C. J. (2007) Fluorescent probes for nitric oxide and hydrogen peroxide in cell signaling. Curr. Opin, Chem. Biol. 11, 620-625
    • (2007) Curr. Opin, Chem. Biol. , vol.11 , pp. 620-625
    • Miller, E.W.1    Chang, C.J.2
  • 39
    • 79960478547 scopus 로고    scopus 로고
    • Chemistry and biology of reactive oxygen species in signaling or stress responses
    • Dickinson, B. C., and Chang, C. J. (2011) Chemistry and biology of reactive oxygen species in signaling or stress responses. Nat. Chem. Biol. 7, 504-511
    • (2011) Nat. Chem. Biol. , vol.7 , pp. 504-511
    • Dickinson, B.C.1    Chang, C.J.2
  • 40
    • 80053049200 scopus 로고    scopus 로고
    • Boronate oxidation as a bioorthogonal reaction approach for studying the chemistry of hydrogen peroxide in living systems
    • Lippert, A. R., Van de Bittner, G. C., and Chang, C. J. (2011) Boronate oxidation as a bioorthogonal reaction approach for studying the chemistry of hydrogen peroxide in living systems. Acc. Chem. Res. 44, 793-804
    • (2011) Acc. Chem. Res. , vol.44 , pp. 793-804
    • Lippert, A.R.1    Van De-Bittner, G.C.2    Chang, C.J.3
  • 41
    • 84879744031 scopus 로고    scopus 로고
    • Boronate-based fluorescent probes. Imaging hydrogen peroxide in living systems
    • Lin, V. S., Dickinson, B. C., and Chang, C. J. (2013) Boronate-based fluorescent probes. Imaging hydrogen peroxide in living systems. Methods Enzymol. 526, 19-43
    • (2013) Methods Enzymol. , vol.526 , pp. 19-43
    • Lin, V.S.1    Dickinson, B.C.2    Chang, C.J.3
  • 42
    • 79960286223 scopus 로고    scopus 로고
    • Signal transduction by reactive oxygen species
    • Finkel, T. (2011) Signal transduction by reactive oxygen species. J. Cell Biol. 194, 7-15
    • (2011) J. Cell Biol. , vol.194 , pp. 7-15
    • Finkel, T.1
  • 43
    • 77956634584 scopus 로고    scopus 로고
    • Targeting the reversibly oxidized protein tyrosine phosphatase superfamily
    • Boivin, B., Yang, M., and Tonks, N. K. (2010) Targeting the reversibly oxidized protein tyrosine phosphatase superfamily. Sci. Signal. 3, pl2
    • (2010) Sci. Signal. , vol.3
    • Boivin, B.1    Yang, M.2    Tonks, N.K.3
  • 44
    • 27744458852 scopus 로고    scopus 로고
    • FAK signaling is critical for ErbB-2/ErbB-3 receptor cooperation for oncogenic transformation and invasion
    • Benlimame, N., He, Q., Jie, S., Xiao, D., Xu, Y. J., Loignon, M., Schlaepfer, D. D., and Alaoui-Jamali, M. A. (2005) FAK signaling is critical for ErbB-2/ErbB-3 receptor cooperation for oncogenic transformation and invasion. J. Cell Biol. 171, 505-516
    • (2005) J. Cell Biol. , vol.171 , pp. 505-516
    • Benlimame, N.1    He, Q.2    Jie, S.3    Xiao, D.4    Xu, Y.J.5    Loignon, M.6    Schlaepfer, D.D.7    Alaoui-Jamali, M.A.8
  • 45
    • 60349114065 scopus 로고    scopus 로고
    • Regulation of focal adhesion turnover by ErbB signalling in invasive breast cancer cells
    • Xu, Y., Benlimame, N., Su, J., He, Q., and Alaoui-Jamali, M. A. (2009) Regulation of focal adhesion turnover by ErbB signalling in invasive breast cancer cells. Br. J. Cancer 100, 633-643
    • (2009) Br. J. Cancer , vol.100 , pp. 633-643
    • Xu, Y.1    Benlimame, N.2    Su, J.3    He, Q.4    Alaoui-Jamali, M.A.5
  • 47
    • 4644301879 scopus 로고    scopus 로고
    • Regulation of vascular endothelial growth factor receptor 2-mediated phosphorylation of focal adhesion kinase by heat shock protein 90 and Src kinase activities
    • Le Boeuf, F., Houle, F., and Huot, J. (2004) Regulation of vascular endothelial growth factor receptor 2-mediated phosphorylation of focal adhesion kinase by heat shock protein 90 and Src kinase activities. J. Biol. Chem. 279, 39175-39185
    • (2004) J. Biol. Chem. , vol.279 , pp. 39175-39185
    • Le Boeuf, F.1    Houle, F.2    Huot, J.3
  • 48
    • 33746622446 scopus 로고    scopus 로고
    • Phosphorylation of focal adhesion kinase (FAK) on Ser-732 is induced by rho-dependent kinase and is essential for proline-rich tyrosine kinase-2-mediated phosphorylation of FAK on Tyr-407 in response to vascular endothelial growth factor
    • Le Boeuf, F., Houle, F., Sussman, M., and Huot, J. (2006) Phosphorylation of focal adhesion kinase (FAK) on Ser-732 is induced by rho-dependent kinase and is essential for proline-rich tyrosine kinase-2-mediated phosphorylation of FAK on Tyr-407 in response to vascular endothelial growth factor. Mol. Biol. Cell 17, 3508-3520
    • (2006) Mol. Biol. Cell , vol.17 , pp. 3508-3520
    • Le Boeuf, F.1    Houle, F.2    Sussman, M.3    Huot, J.4
  • 49
    • 76849100707 scopus 로고    scopus 로고
    • Focal adhesion kinase. A prominent determinant in breast cancer initiation, progression and metastasis
    • Luo, M., and Guan, J. L. (2010) Focal adhesion kinase. A prominent determinant in breast cancer initiation, progression and metastasis. Cancer Lett. 289, 127-139
    • (2010) Cancer Lett. , vol.289 , pp. 127-139
    • Luo, M.1    Guan, J.L.2
  • 52
    • 84855829745 scopus 로고    scopus 로고
    • β1-integrins signaling and mammary tumor progression in transgenic mouse models. Implications for human breast cancer
    • Lahlou, H., and Muller, W. J. (2011) β1-integrins signaling and mammary tumor progression in transgenic mouse models. Implications for human breast cancer. Breast Cancer Res. 13, 229-239
    • (2011) Breast Cancer Res. , vol.13 , pp. 229-239
    • Lahlou, H.1    Muller, W.J.2
  • 53
    • 0033551899 scopus 로고    scopus 로고
    • Integrin signaling
    • Giancotti, F. G., and Ruoslahti, E. (1999) Integrin signaling. Science 285, 1028-1032
    • (1999) Science , vol.285 , pp. 1028-1032
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 54
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation. Roles of integrin aggregation and occupancy of receptors
    • Miyamoto, S., Teramoto, H., Gutkind, J. S., and Yamada, K. M. (1996) Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation. Roles of integrin aggregation and occupancy of receptors. J. Cell Biol. 135, 1633-1642
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 55
    • 77957283664 scopus 로고    scopus 로고
    • β1-Integrin is dispensable for the induction of ErbB2 mammary tumors but plays a critical role in the metastatic phase of tumor progression
    • Huck, L., Pontier, S. M., Zuo, D. M., and Muller, W. J. (2010) β1-Integrin is dispensable for the induction of ErbB2 mammary tumors but plays a critical role in the metastatic phase of tumor progression. Proc. Natl. Acad. Sci. U.S.A. 107, 15559-15564
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 15559-15564
    • Huck, L.1    Pontier, S.M.2    Zuo, D.M.3    Muller, W.J.4
  • 56
    • 0021228376 scopus 로고
    • Actin-membrane interaction in fibroblasts. What proteins are involved in this association?
    • Mangeat, P., and Burridge, K. (1984) Actin-membrane interaction in fibroblasts. What proteins are involved in this association? J. Cell Biol. 99, 95s-103s
    • (1984) J. Cell Biol. , vol.99
    • Mangeat, P.1    Burridge, K.2
  • 58
    • 2542490290 scopus 로고    scopus 로고
    • Grb7 in intracellular signaling and its role in cell regulation
    • Shen, T. L., and Guan, J. L. (2004) Grb7 in intracellular signaling and its role in cell regulation. Front. Biosci. 9, 192-200
    • (2004) Front. Biosci. , vol.9 , pp. 192-200
    • Shen, T.L.1    Guan, J.L.2
  • 59
    • 67749099777 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis
    • Chu, P. Y., Huang, L. Y., Hsu, C. H., Liang, C. C., Guan, J. L., Hung, T. H., and Shen, T. L. (2009) Tyrosine phosphorylation of growth factor receptor-bound protein-7 by focal adhesion kinase in the regulation of cell migration, proliferation, and tumorigenesis. J. Biol. Chem. 284, 20215-20226
    • (2009) J. Biol. Chem. , vol.284 , pp. 20215-20226
    • Chu, P.Y.1    Huang, L.Y.2    Hsu, C.H.3    Liang, C.C.4    Guan, J.L.5    Hung, T.H.6    Shen, T.L.7
  • 60
    • 33645735705 scopus 로고    scopus 로고
    • Specific peptide ligand for Grb7 signal transduction protein and pancreatic cancer metastasis
    • Tanaka, S., Pero, S. C., Taguchi, K., Shimada, M., Mori, M., Krag, D. N., and Arii, S. (2006) Specific peptide ligand for Grb7 signal transduction protein and pancreatic cancer metastasis. J. Natl. Cancer Inst. 98, 491-498
    • (2006) J. Natl. Cancer Inst. , vol.98 , pp. 491-498
    • Tanaka, S.1    Pero, S.C.2    Taguchi, K.3    Shimada, M.4    Mori, M.5    Krag, D.N.6    Arii, S.7
  • 61
    • 79961021621 scopus 로고    scopus 로고
    • Activation of Src and transformation by an RPTPα splice mutant found in human tumours
    • Huang, J., Yao, L., Xu, R., Wu, H., Wang, M., White, B. S., Shalloway, D., and Zheng, X. (2011) Activation of Src and transformation by an RPTPα splice mutant found in human tumours. EMBO J. 30, 3200-3211
    • (2011) EMBO J. , vol.30 , pp. 3200-3211
    • Huang, J.1    Yao, L.2    Xu, R.3    Wu, H.4    Wang, M.5    White, B.S.6    Shalloway, D.7    Zheng, X.8
  • 62
    • 0141788585 scopus 로고    scopus 로고
    • Aging-related attenuation of EGF receptor signaling is mediated in part by increased protein tyrosine phosphatase activity
    • Tran, K. T., Rusu, S. D., Satish, L., and Wells, A. (2003) Aging-related attenuation of EGF receptor signaling is mediated in part by increased protein tyrosine phosphatase activity. Exp. Cell Res. 289, 359-367
    • (2003) Exp. Cell Res. , vol.289 , pp. 359-367
    • Tran, K.T.1    Rusu, S.D.2    Satish, L.3    Wells, A.4
  • 63
    • 0033610844 scopus 로고    scopus 로고
    • Proteintyrosine phosphatase α regulates Src family kinases and alters cell-substratum adhesion
    • Harder, K. W., Moller, N. P., Peacock, J. W., and Jirik, F. R. (1998) Proteintyrosine phosphatase α regulates Src family kinases and alters cell-substratum adhesion. J. Biol. Chem. 273, 31890-31900
    • (1998) J. Biol. Chem. , vol.273 , pp. 31890-31900
    • Harder, K.W.1    Moller, N.P.2    Peacock, J.W.3    Jirik, F.R.4
  • 64
    • 2342472716 scopus 로고    scopus 로고
    • Focal adhesion and actin dynamics. A place where kinases and proteases meet to promote invasion
    • Carragher, N. O., and Frame, M. C. (2004) Focal adhesion and actin dynamics. A place where kinases and proteases meet to promote invasion. Trends Cell Biol. 14, 241-249
    • (2004) Trends Cell Biol. , vol.14 , pp. 241-249
    • Carragher, N.O.1    Frame, M.C.2
  • 66
    • 0037066778 scopus 로고    scopus 로고
    • V-Src SH3-enhanced interaction with focal adhesion kinase at β 1 integrin-containing invadopodia promotes cell invasion
    • Hauck, C. R., Hsia, D. A., Ilic, D., and Schlaepfer, D. D. (2002) v-Src SH3-enhanced interaction with focal adhesion kinase at β 1 integrin-containing invadopodia promotes cell invasion. J. Biol. Chem. 277, 12487-12490
    • (2002) J. Biol. Chem. , vol.277 , pp. 12487-12490
    • Hauck, C.R.1    Hsia, D.A.2    Ilic, D.3    Schlaepfer, D.D.4
  • 67
    • 0036001167 scopus 로고    scopus 로고
    • The focal adhesion kinase. A regulator of cell migration and invasion
    • Hauck, C. R., Hsia, D. A., and Schlaepfer, D. D. (2002) The focal adhesion kinase. A regulator of cell migration and invasion. IUBMB Life 53, 115-119
    • (2002) IUBMB Life , vol.53 , pp. 115-119
    • Hauck, C.R.1    Hsia, D.A.2    Schlaepfer, D.D.3
  • 68
    • 0037421205 scopus 로고    scopus 로고
    • PTP α regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • Zeng, L., Si, X., Yu, W. P., Le, H. T., Ng, K. P., Teng, R. M., Ryan, K., Wang, D. Z., Ponniah, S., and Pallen, C. J. (2003) PTP α regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J. Cell Biol. 160, 137-146
    • (2003) J. Cell Biol. , vol.160 , pp. 137-146
    • Zeng, L.1    Si, X.2    Yu, W.P.3    Le, H.T.4    Ng, K.P.5    Teng, R.M.6    Ryan, K.7    Wang, D.Z.8    Ponniah, S.9    Pallen, C.J.10
  • 69
    • 33748068089 scopus 로고    scopus 로고
    • New concepts regarding focal adhesion kinase promotion of cell migration and proliferation
    • Cox, B. D., Natarajan, M., Stettner, M. R., and Gladson, C. L. (2006) New concepts regarding focal adhesion kinase promotion of cell migration and proliferation. J. Cell Biochem. 99, 35-52
    • (2006) J. Cell Biochem. , vol.99 , pp. 35-52
    • Cox, B.D.1    Natarajan, M.2    Stettner, M.R.3    Gladson, C.L.4
  • 70
    • 0035837360 scopus 로고    scopus 로고
    • Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2 during epithelial-mesenchymal transdifferentiation and cell migration. Analysis of specific phosphorylation events using site-directed antibodies
    • Nakamura, K., Yano, H., Schaefer, E., and Sabe, H. (2001) Different modes and qualities of tyrosine phosphorylation of Fak and Pyk2 during epithelial-mesenchymal transdifferentiation and cell migration. Analysis of specific phosphorylation events using site-directed antibodies. Oncogene 20, 2626-2635
    • (2001) Oncogene , vol.20 , pp. 2626-2635
    • Nakamura, K.1    Yano, H.2    Schaefer, E.3    Sabe, H.4
  • 71
    • 0041743841 scopus 로고    scopus 로고
    • Expression of GRP and its receptor in well-differentiated colon cancer cells correlates with the presence of focal adhesion kinase phosphorylated at tyrosines 397 and 407
    • Matkowskyj, K. A., Keller, K., Glover, S., Kornberg, L., Tran-Son-Tay, R., and Benya, R. V. (2003) Expression of GRP and its receptor in well-differentiated colon cancer cells correlates with the presence of focal adhesion kinase phosphorylated at tyrosines 397 and 407. J. Histochem. Cytochem. 51, 1041-1048
    • (2003) J. Histochem. Cytochem. , vol.51 , pp. 1041-1048
    • Matkowskyj, K.A.1    Keller, K.2    Glover, S.3    Kornberg, L.4    Tran-Son-Tay, R.5    Benya, R.V.6
  • 72
    • 34249851423 scopus 로고    scopus 로고
    • Focal adhesion kinase is negatively regulated by phosphorylation at tyrosine 407
    • Lim, Y., Park, H., Jeon, J., Han, I., Kim, J., Jho, E. H., and Oh, E. S. (2007) Focal adhesion kinase is negatively regulated by phosphorylation at tyrosine 407. J. Biol. Chem. 282, 10398-10404
    • (2007) J. Biol. Chem. , vol.282 , pp. 10398-10404
    • Lim, Y.1    Park, H.2    Jeon, J.3    Han, I.4    Kim, J.5    Jho, E.H.6    Oh, E.S.7
  • 73
    • 22844435175 scopus 로고    scopus 로고
    • Grb7-SH2 domain dimerisation is affected by a single point mutation
    • Porter, C. J., Wilce, M. C., Mackay, J. P., Leedman, P., and Wilce, J. A. (2005) Grb7-SH2 domain dimerisation is affected by a single point mutation. Eur. Biophys. J. 34, 454-460
    • (2005) Eur. Biophys. J. , vol.34 , pp. 454-460
    • Porter, C.J.1    Wilce, M.C.2    MacKay, J.P.3    Leedman, P.4    Wilce, J.A.5
  • 74
    • 0028285788 scopus 로고
    • Phosphorylation of receptor protein-tyrosine phosphatase α on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo
    • den Hertog, J., Tracy, S., and Hunter, T. (1994) Phosphorylation of receptor protein-tyrosine phosphatase α on Tyr789, a binding site for the SH3-SH2-SH3 adaptor protein GRB-2 in vivo. EMBO J. 13, 3020-3032
    • (1994) EMBO J. , vol.13 , pp. 3020-3032
    • Den Hertog, J.1    Tracy, S.2    Hunter, T.3
  • 75
    • 0034603164 scopus 로고    scopus 로고
    • The carboxyl-terminal tyrosine residue of protein-tyrosine phosphatase alpha mediates association with focal adhesion plaques
    • Lammers, R., Lerch, M. M., and Ullrich, A. (2000) The carboxyl-terminal tyrosine residue of protein-tyrosine phosphatase alpha mediates association with focal adhesion plaques. J. Biol. Chem. 275, 3391-3396
    • (2000) J. Biol. Chem. , vol.275 , pp. 3391-3396
    • Lammers, R.1    Lerch, M.M.2    Ullrich, A.3
  • 76
    • 0031696486 scopus 로고    scopus 로고
    • SRC binding to the cytoskeleton, triggered by growth cone attachment to laminin, is protein tyrosine phosphatase-dependent
    • Helmke, S., Lohse, K., Mikule, K., Wood, M. R., and Pfenninger, K. H. (1998) SRC binding to the cytoskeleton, triggered by growth cone attachment to laminin, is protein tyrosine phosphatase-dependent. J. Cell Sci. 111, 2465-2475
    • (1998) J. Cell Sci. , vol.111 , pp. 2465-2475
    • Helmke, S.1    Lohse, K.2    Mikule, K.3    Wood, M.R.4    Pfenninger, K.H.5
  • 77
    • 0034161405 scopus 로고    scopus 로고
    • A phosphotyrosine displacement mechanism for activation of Src by PTPα
    • Zheng, X. M., Resnick, R. J., and Shalloway, D. (2000) A phosphotyrosine displacement mechanism for activation of Src by PTPα. EMBO J. 19, 964-978
    • (2000) EMBO J. , vol.19 , pp. 964-978
    • Zheng, X.M.1    Resnick, R.J.2    Shalloway, D.3
  • 78
    • 67649849871 scopus 로고    scopus 로고
    • Integrin β1-focal adhesion kinase signaling directs the proliferation of metastatic cancer cells disseminated in the lungs
    • Shibue, T., and Weinberg, R. A. (2009) Integrin β1-focal adhesion kinase signaling directs the proliferation of metastatic cancer cells disseminated in the lungs. Proc. Natl. Acad. Sci. U.S.A. 106, 10290-10295
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 10290-10295
    • Shibue, T.1    Weinberg, R.A.2


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