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Volumn 18, Issue 8, 2007, Pages 3214-3223

E-cadherin adhesion activates c-Src signaling at cell-cell contacts

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; PHOSPHATASE; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOTYROSINE; PROTEIN TYROSINE KINASE; UVOMORULIN;

EID: 34547811984     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-12-1154     Document Type: Article
Times cited : (132)

References (37)
  • 2
    • 0027507028 scopus 로고
    • Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature- sensitive v-SRC gene
    • Behrens, J., Vakaet, L., Friis, R., Winterhager, E., Van Roy, F., Mareel, M. M., and Birchmeier, W. (1993). Loss of epithelial differentiation and gain of invasiveness correlates with tyrosine phosphorylation of the E-cadherin/beta-catenin complex in cells transformed with a temperature- sensitive v-SRC gene. J. Cell Biol. 120, 757-766.
    • (1993) J. Cell Biol , vol.120 , pp. 757-766
    • Behrens, J.1    Vakaet, L.2    Friis, R.3    Winterhager, E.4    Van Roy, F.5    Mareel, M.M.6    Birchmeier, W.7
  • 3
    • 0032526941 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion
    • Calautti, E., Cabodi, S., Stein, P. L., Hatzfeld, M., Kedersha, N., and Paolo Dotto, G. (1998). Tyrosine phosphorylation and src family kinases control keratinocyte cell-cell adhesion. J. Cell Biol. 141, 1449-1465.
    • (1998) J. Cell Biol , vol.141 , pp. 1449-1465
    • Calautti, E.1    Cabodi, S.2    Stein, P.L.3    Hatzfeld, M.4    Kedersha, N.5    Paolo Dotto, G.6
  • 4
    • 0037033804 scopus 로고    scopus 로고
    • Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion
    • Calautti, E., Grossi, M., Mammucari, C., Aoyama, Y., Pirro, M., Ono, Y., Li, J., and Dotto, G. P. (2002). Fyn tyrosine kinase is a downstream mediator of Rho/PRK2 function in keratinocyte cell-cell adhesion. J. Cell Biol. 156, 137-148.
    • (2002) J. Cell Biol , vol.156 , pp. 137-148
    • Calautti, E.1    Grossi, M.2    Mammucari, C.3    Aoyama, Y.4    Pirro, M.5    Ono, Y.6    Li, J.7    Dotto, G.P.8
  • 5
    • 0035020950 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase signalling pathways
    • Cantrell, D. A. (2001). Phosphoinositide 3-kinase signalling pathways. J. Cell Sci. 114, 1439-1445.
    • (2001) J. Cell Sci , vol.114 , pp. 1439-1445
    • Cantrell, D.A.1
  • 6
    • 0022559078 scopus 로고
    • Tyr527 is phosphorylated in pp60c-src: Implications for regulation
    • Cooper, J. A., Gould, K. L., Cartwright, C. A., and Hunter, T. (1986). Tyr527 is phosphorylated in pp60c-src: implications for regulation. Science 231, 1431-1434.
    • (1986) Science , vol.231 , pp. 1431-1434
    • Cooper, J.A.1    Gould, K.L.2    Cartwright, C.A.3    Hunter, T.4
  • 7
    • 1842584776 scopus 로고    scopus 로고
    • Newest findings on the oldest oncogene; how activated src does it
    • Frame, M. C. (2004). Newest findings on the oldest oncogene; how activated src does it. J. Cell Sci. 117, 989-998.
    • (2004) J. Cell Sci , vol.117 , pp. 989-998
    • Frame, M.C.1
  • 8
    • 30044444270 scopus 로고    scopus 로고
    • Activation of Rac by cadherin through the c-Src-Rap1- phosphatidylinositol 3-kinase-Vav2 pathway
    • Fukuyama, T., Ogita, H., Kawakatsu, T., Inagaki, M., and Takai, Y. (2006). Activation of Rac by cadherin through the c-Src-Rap1- phosphatidylinositol 3-kinase-Vav2 pathway. Oncogene 25, 8-19.
    • (2006) Oncogene , vol.25 , pp. 8-19
    • Fukuyama, T.1    Ogita, H.2    Kawakatsu, T.3    Inagaki, M.4    Takai, Y.5
  • 9
    • 0037743623 scopus 로고    scopus 로고
    • Minimal mutation of the cytoplasmic tail inhibits the ability of E-cadherin to activate Rac but not phosphatidylinositol 3-kinase: Direct evidence of a role for cadherin-activated Rac signaling in adhesion and contact formation
    • Goodwin, M., Kovacs, E. M., Thoreson, M. A., Reynolds, A. B., and Yap, A. S. (2003). Minimal mutation of the cytoplasmic tail inhibits the ability of E-cadherin to activate Rac but not phosphatidylinositol 3-kinase: direct evidence of a role for cadherin-activated Rac signaling in adhesion and contact formation. J. Biol. Chem. 278, 20533-20539.
    • (2003) J. Biol. Chem , vol.278 , pp. 20533-20539
    • Goodwin, M.1    Kovacs, E.M.2    Thoreson, M.A.3    Reynolds, A.B.4    Yap, A.S.5
  • 11
    • 0037155159 scopus 로고    scopus 로고
    • E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts
    • Kovacs, E. M., Ali, R. G., McCormack, A. J., and Yap, A. S. (2002a). E-cadherin homophilic ligation directly signals through Rac and phosphatidylinositol 3-kinase to regulate adhesive contacts. J. Biol. Chem. 277, 6708-6718.
    • (2002) J. Biol. Chem , vol.277 , pp. 6708-6718
    • Kovacs, E.M.1    Ali, R.G.2    McCormack, A.J.3    Yap, A.S.4
  • 12
    • 0037022538 scopus 로고    scopus 로고
    • Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts
    • Kovacs, E. M., Goodwin, M., Ali, R. G., Paterson, A. D., and Yap, A. S. (2002b). Cadherin-directed actin assembly: E-cadherin physically associates with the Arp2/3 complex to direct actin assembly in nascent adhesive contacts. Curr. Biol. 12, 379-382.
    • (2002) Curr. Biol , vol.12 , pp. 379-382
    • Kovacs, E.M.1    Goodwin, M.2    Ali, R.G.3    Paterson, A.D.4    Yap, A.S.5
  • 14
    • 0026742310 scopus 로고
    • Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts
    • Matsuyoshi, N., Hamaguchi, M., Taniguchi, S., Nagafuchi, A., Tsukita, S., and Takeichi, M. (1992). Cadherin-mediated cell-cell adhesion is perturbed by v-src tyrosine phosphorylation in metastatic fibroblasts. J. Cell Biol. 118, 703-714.
    • (1992) J. Cell Biol , vol.118 , pp. 703-714
    • Matsuyoshi, N.1    Hamaguchi, M.2    Taniguchi, S.3    Nagafuchi, A.4    Tsukita, S.5    Takeichi, M.6
  • 15
    • 34249891883 scopus 로고    scopus 로고
    • Not so simple: The complexity of phosphotyrosine signaling at cadherin adhesive contacts
    • McLachlan, R. W., and Yap, A. S. (2007). Not so simple: the complexity of phosphotyrosine signaling at cadherin adhesive contacts. J. Mol. Med. 85, 545-554.
    • (2007) J. Mol. Med , vol.85 , pp. 545-554
    • McLachlan, R.W.1    Yap, A.S.2
  • 16
    • 0025881470 scopus 로고
    • Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src
    • Nada, S., Okada, M., MacAuley, A., Cooper, J. A., and Nakagawa, H. (1991). Cloning of a complementary DNA for a protein-tyrosine kinase that specifically phosphorylates a negative regulatory site of p60c-src. Nature 351, 69-72.
    • (1991) Nature , vol.351 , pp. 69-72
    • Nada, S.1    Okada, M.2    MacAuley, A.3    Cooper, J.A.4    Nakagawa, H.5
  • 17
    • 13244267197 scopus 로고    scopus 로고
    • Recruitment of phosphoinositide 3-kinase defines a positive contribution of tyrosine kinase signaling to E-cadherin function
    • Pang, J. H., Kraemer, A., Stehbens, S. J., Frame, M. C., and Yap, A. S. (2005). Recruitment of phosphoinositide 3-kinase defines a positive contribution of tyrosine kinase signaling to E-cadherin function. J. Biol. Chem. 280, 3043-3050.
    • (2005) J. Biol. Chem , vol.280 , pp. 3043-3050
    • Pang, J.H.1    Kraemer, A.2    Stehbens, S.J.3    Frame, M.C.4    Yap, A.S.5
  • 18
    • 0024821548 scopus 로고
    • Genetics of src: Structure and functional organization of a protein tyrosine kinase
    • Parsons, J. T., and Weber, M. J. (1989). Genetics of src: structure and functional organization of a protein tyrosine kinase. Curr. Top. Microbiol. Immunol. 147, 79-127.
    • (1989) Curr. Top. Microbiol. Immunol , vol.147 , pp. 79-127
    • Parsons, J.T.1    Weber, M.J.2
  • 19
    • 0038418651 scopus 로고    scopus 로고
    • Characterization of E-cadherin endocytosis in isolated MCF-7 and Chinese hamster ovary cells: The initial fate of unbound E-cadherin
    • Paterson, A. D., Parton, R. G., Ferguson, C., Stow, J. L., and Yap, A. S. (2003). Characterization of E-cadherin endocytosis in isolated MCF-7 and Chinese hamster ovary cells: the initial fate of unbound E-cadherin. J. Biol. Chem. 278, 21050-21057.
    • (2003) J. Biol. Chem , vol.278 , pp. 21050-21057
    • Paterson, A.D.1    Parton, R.G.2    Ferguson, C.3    Stow, J.L.4    Yap, A.S.5
  • 20
    • 0033516481 scopus 로고    scopus 로고
    • Activation of the protein kinase Akt/PKB by the formation of E-cadherin-mediated cell-cell junctions. Evidence for the association of phosphatidylinositol 3-kinase with the E-cadherin adhesion complex
    • Pece, S., Chiariello, M., Murga, C., and Gutkind, J. S. (1999). Activation of the protein kinase Akt/PKB by the formation of E-cadherin-mediated cell-cell junctions. Evidence for the association of phosphatidylinositol 3-kinase with the E-cadherin adhesion complex. J. Biol. Chem. 274, 19347-19351.
    • (1999) J. Biol. Chem , vol.274 , pp. 19347-19351
    • Pece, S.1    Chiariello, M.2    Murga, C.3    Gutkind, J.S.4
  • 21
    • 26244455734 scopus 로고    scopus 로고
    • Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts
    • Shewan, A. M., Maddugoda, M., Kraemer, A., Stehbens, S. J., Verma, S., Kovacs, E. M., and Yap, A. S. (2005). Myosin 2 is a key Rho kinase target necessary for the local concentration of E-cadherin at cell-cell contacts. Mol. Biol. Cell 16, 4531-4542.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4531-4542
    • Shewan, A.M.1    Maddugoda, M.2    Kraemer, A.3    Stehbens, S.J.4    Verma, S.5    Kovacs, E.M.6    Yap, A.S.7
  • 23
    • 0029736912 scopus 로고    scopus 로고
    • Regulation of cell-cell contacts in developing Drosophila eyes by Dsrc41, a new, close relative of vertebrate c-src
    • Takahashi, F., Endo, S., Kojima, T., and Saigo, K. (1996). Regulation of cell-cell contacts in developing Drosophila eyes by Dsrc41, a new, close relative of vertebrate c-src. Genes Dev. 10, 1645-1656.
    • (1996) Genes Dev , vol.10 , pp. 1645-1656
    • Takahashi, F.1    Endo, S.2    Kojima, T.3    Saigo, K.4
  • 24
    • 21244459197 scopus 로고    scopus 로고
    • Requirements of genetic interactions between Src42A, armadillo and shotgun, a gene encoding E-cadherin, for normal development in Drosophila
    • Takahashi, M., Takahashi, F., Ui-Tei, K., Kojima, T., and Saigo, K. (2005). Requirements of genetic interactions between Src42A, armadillo and shotgun, a gene encoding E-cadherin, for normal development in Drosophila. Development 132, 2547-2559.
    • (2005) Development , vol.132 , pp. 2547-2559
    • Takahashi, M.1    Takahashi, F.2    Ui-Tei, K.3    Kojima, T.4    Saigo, K.5
  • 25
    • 0023892929 scopus 로고
    • Phosphotyrosine-modified proteins are concentrated at the membranes of epithelial and endothelial cells during tissue development in chick embryos
    • Takata, K., and Singer, S. J. (1988). Phosphotyrosine-modified proteins are concentrated at the membranes of epithelial and endothelial cells during tissue development in chick embryos. J. Cell Biol. 106, 1757-1764.
    • (1988) J. Cell Biol , vol.106 , pp. 1757-1764
    • Takata, K.1    Singer, S.J.2
  • 26
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • Thomas, S. M., and Brugge, J. S. (1997). Cellular functions regulated by Src family kinases. Annu. Rev. Cell Dev. Biol. 13, 513-609.
    • (1997) Annu. Rev. Cell Dev. Biol , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 28
    • 0035960717 scopus 로고    scopus 로고
    • Coordination of cell polarization and migration by the Rho family GTPases requires Src tyrosine kinase activity
    • Timpson, P., Jones, G. E., Frame, M. C., and Brunton, V. G. (2001). Coordination of cell polarization and migration by the Rho family GTPases requires Src tyrosine kinase activity. Curr. Biol. 11, 1836-1846.
    • (2001) Curr. Biol , vol.11 , pp. 1836-1846
    • Timpson, P.1    Jones, G.E.2    Frame, M.C.3    Brunton, V.G.4
  • 29
    • 0025913788 scopus 로고
    • Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated
    • Tsukita, S., Oishi, K., Akiyama, T., Yamanashi, Y., Yamamoto, T., and Tsukita, S. (1991). Specific proto-oncogenic tyrosine kinases of src family are enriched in cell-to-cell adherens junctions where the level of tyrosine phosphorylation is elevated. J. Cell Biol. 113, 867-879.
    • (1991) J. Cell Biol , vol.113 , pp. 867-879
    • Tsukita, S.1    Oishi, K.2    Akiyama, T.3    Yamanashi, Y.4    Yamamoto, T.5    Tsukita, S.6
  • 31
    • 0347301739 scopus 로고    scopus 로고
    • The v-Src and c-Src tyrosine kinases immunoprecipitated from Rous sarcoma virus-transformed cells display different peptide substrate specificities
    • Vojtechova, M., Tuhackova, Z., Hlavacek, J., Velek, J., and Sovova, V. (2004). The v-Src and c-Src tyrosine kinases immunoprecipitated from Rous sarcoma virus-transformed cells display different peptide substrate specificities. Arch. Biochem. Biophys. 421, 277-282.
    • (2004) Arch. Biochem. Biophys , vol.421 , pp. 277-282
    • Vojtechova, M.1    Tuhackova, Z.2    Hlavacek, J.3    Velek, J.4    Sovova, V.5
  • 32
    • 0026114963 scopus 로고
    • Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells
    • Volberg, T., Geiger, B., Dror, R., and Zick, Y. (1991). Modulation of intercellular adherens-type junctions and tyrosine phosphorylation of their components in RSV-transformed cultured chick lens cells. Cell Regul. 2, 105-120.
    • (1991) Cell Regul , vol.2 , pp. 105-120
    • Volberg, T.1    Geiger, B.2    Dror, R.3    Zick, Y.4
  • 33
    • 0023109112 scopus 로고
    • Nonmitogenic morphoregulatory action of pp60v-src on multicellular epithelial structures
    • Warren, S. L., and Nelson, W. J. (1987). Nonmitogenic morphoregulatory action of pp60v-src on multicellular epithelial structures. Mol. Cell. Biol. 7, 1326-1337.
    • (1987) Mol. Cell. Biol , vol.7 , pp. 1326-1337
    • Warren, S.L.1    Nelson, W.J.2
  • 34
    • 0033594403 scopus 로고    scopus 로고
    • Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction
    • Watton, S. J., and Downward, J. (1999). Akt/PKB localisation and 3′ phosphoinositide generation at sites of epithelial cell-matrix and cell-cell interaction. Curr. Biol. 9, 433-436.
    • (1999) Curr. Biol , vol.9 , pp. 433-436
    • Watton, S.J.1    Downward, J.2
  • 35
    • 0032497832 scopus 로고    scopus 로고
    • Structure and function of phosphoinositide 3-kinases
    • Wymann, M. P., and Pirola, L. (1998). Structure and function of phosphoinositide 3-kinases. Biochim. Biophys. Acta 1436, 127-150.
    • (1998) Biochim. Biophys. Acta , vol.1436 , pp. 127-150
    • Wymann, M.P.1    Pirola, L.2
  • 36
    • 0031149109 scopus 로고    scopus 로고
    • Lateral clustering of the adhesive ectodomain: A fundamental determinant of cadherin function
    • Yap, A. S., Brieher, W. M., Pruschy, M., and Gumbiner, B. M. (1997). Lateral clustering of the adhesive ectodomain: a fundamental determinant of cadherin function. Curr. Biol. 7, 308-315.
    • (1997) Curr. Biol , vol.7 , pp. 308-315
    • Yap, A.S.1    Brieher, W.M.2    Pruschy, M.3    Gumbiner, B.M.4
  • 37
    • 0037421188 scopus 로고    scopus 로고
    • Direct cadherin-activated cell signaling: A view from the plasma membrane
    • Yap, A. S., and Kovacs, E. M. (2003). Direct cadherin-activated cell signaling: a view from the plasma membrane. J. Cell Biol. 160, 11-16.
    • (2003) J. Cell Biol , vol.160 , pp. 11-16
    • Yap, A.S.1    Kovacs, E.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.