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Volumn 302, Issue 2, 2005, Pages 253-269

The proto-oncogene Fgr regulates cell migration and this requires its plasma membrane localization

Author keywords

Cell migration; Fgr; Focal adhesion kinase; Rhogtpases; Src family kinases

Indexed keywords

CORTACTIN; FIBRONECTIN; FOCAL ADHESION KINASE; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN P85; PROTEIN SUBUNIT; RAC PROTEIN;

EID: 9244248650     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.09.005     Document Type: Article
Times cited : (17)

References (73)
  • 1
    • 0031439247 scopus 로고    scopus 로고
    • Cellular functions regulated by Src family kinases
    • S.M. Thomas, and J.S. Brugge Cellular functions regulated by Src family kinases Annu. Rev. Cell Dev. Biol. 13 1997 513 609
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 513-609
    • Thomas, S.M.1    Brugge, J.S.2
  • 4
    • 0027080147 scopus 로고
    • The Src family of tyrosine protein kinases in hemopoietic signal transduction
    • J.B. Bolen, R.B. Rowley, C. Spana, and A.Y. Tsygankov The Src family of tyrosine protein kinases in hemopoietic signal transduction FASEB J. 6 1992 3403 3409
    • (1992) FASEB J. , vol.6 , pp. 3403-3409
    • Bolen, J.B.1    Rowley, R.B.2    Spana, C.3    Tsygankov, A.Y.4
  • 5
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • T.D. Pollard, and G.G. Borisy Cellular motility driven by assembly and disassembly of actin filaments Cell 112 2003 453 465
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 6
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • R.A. Klinghoffer, C. Sachsenmaier, J.A. Cooper, and P. Soriano Src family kinases are required for integrin but not PDGFR signal transduction EMBO J. 18 1999 2459 2471
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 7
    • 0036205320 scopus 로고    scopus 로고
    • SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • L.A. Cary, R.A. Klinghoffer, C. Sachsenmaier, and J.A. Cooper SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading Mol. Cell. Biol. 22 2002 2427 2440
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 8
    • 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
    • K.B. Kaplan, K.B. Bibbins, J.R. Swedlow, M. Arnaud, D.O. Morgan, and H.E. Varmus 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 1994 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
  • 9
    • 0032472411 scopus 로고    scopus 로고
    • The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility
    • V.J. Fincham, and M.C. Frame The catalytic activity of Src is dispensable for translocation to focal adhesions but controls the turnover of these structures during cell motility EMBO J. 17 1998 81 92
    • (1998) EMBO J. , vol.17 , pp. 81-92
    • Fincham, V.J.1    Frame, M.C.2
  • 10
    • 0033175564 scopus 로고    scopus 로고
    • Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase Src
    • D.P. Felsenfeld, P.L. Schwartzberg, A. Venegas, R. Tse, and M.P. Sheetz Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase Src Nat. Cell Biol. 1 1999 200 206
    • (1999) Nat. Cell Biol. , vol.1 , pp. 200-206
    • Felsenfeld, D.P.1    Schwartzberg, P.L.2    Venegas, A.3    Tse, R.4    Sheetz, M.P.5
  • 11
    • 0034941053 scopus 로고    scopus 로고
    • Pp60(c-src) and related tyrosine kinases: A role in the assembly and reorganization of matrix adhesions
    • T. Volberg, L. Romer, E. Zamir, and B. Geiger pp60(c-src) and related tyrosine kinases: a role in the assembly and reorganization of matrix adhesions J. Cell Sci. 114 2001 2279 2289
    • (2001) J. Cell Sci. , vol.114 , pp. 2279-2289
    • Volberg, T.1    Romer, L.2    Zamir, E.3    Geiger, B.4
  • 12
    • 0032959561 scopus 로고    scopus 로고
    • Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation
    • V.J. Fincham, A. Chudleigh, and M.C. Frame Regulation of p190 Rho-GAP by v-Src is linked to cytoskeletal disruption during transformation J. Cell Sci. 112 Pt 6 1999 947 956
    • (1999) J. Cell Sci. , vol.112 , Issue.6 , pp. 947-956
    • Fincham, V.J.1    Chudleigh, A.2    Frame, M.C.3
  • 13
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • W.T. Arthur, L.A. Petch, and K. Burridge Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism Curr. Biol. 10 2000 719 722
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 14
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • W.T. Arthur, and K. Burridge RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity Mol. Biol. Cell 12 2001 2711 2720
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 15
    • 0035071323 scopus 로고    scopus 로고
    • P190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation
    • M.R. Brouns, S.F. Matheson, and J. Settleman p190 RhoGAP is the principal Src substrate in brain and regulates axon outgrowth, guidance and fasciculation Nat. Cell Biol. 3 2001 361 367
    • (2001) Nat. Cell Biol. , vol.3 , pp. 361-367
    • Brouns, M.R.1    Matheson, S.F.2    Settleman, J.3
  • 16
    • 0037036373 scopus 로고    scopus 로고
    • Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway
    • D. Brandt, M. Gimona, M. Hillmann, H. Haller, and H. Mischak Protein kinase C induces actin reorganization via a Src- and Rho-dependent pathway J. Biol. Chem. 277 2002 20903 20910
    • (2002) J. Biol. Chem. , vol.277 , pp. 20903-20910
    • Brandt, D.1    Gimona, M.2    Hillmann, M.3    Haller, H.4    Mischak, H.5
  • 18
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • S. Etienne-Manneville, and A. Hall Rho GTPases in cell biology Nature 420 2002 629 635
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 19
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • C.D. Nobes, and A. Hall Rho GTPases control polarity, protrusion, and adhesion during cell movement J. Cell Biol. 144 1999 1235 1244
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 21
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • A.J. Ridley Rho GTPases and cell migration J. Cell Sci. 114 2001 2713 2722
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 22
    • 0034978163 scopus 로고    scopus 로고
    • Regulation of c-myc expression by PDGF through Rho GTPases
    • M. Chiariello, M.J. Marinissen, and J.S. Gutkind Regulation of c-myc expression by PDGF through Rho GTPases Nat. Cell Biol. 3 2001 580 586
    • (2001) Nat. Cell Biol. , vol.3 , pp. 580-586
    • Chiariello, M.1    Marinissen, M.J.2    Gutkind, J.S.3
  • 23
    • 0141668894 scopus 로고    scopus 로고
    • Rac1 function is required for Src-induced transformation. Evidence of a role for Tiam1 and Vav2 in Rac activation by Src
    • J.M. Servitja, M.J. Marinissen, A. Sodhi, X.R. Bustelo, and J.S. Gutkind Rac1 function is required for Src-induced transformation. Evidence of a role for Tiam1 and Vav2 in Rac activation by Src J. Biol. Chem. 278 2003 34339 34346
    • (2003) J. Biol. Chem. , vol.278 , pp. 34339-34346
    • Servitja, J.M.1    Marinissen, M.J.2    Sodhi, A.3    Bustelo, X.R.4    Gutkind, J.S.5
  • 25
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: The first ten years
    • J.T. Parsons Focal adhesion kinase: the first ten years J. Cell Sci. 116 2003 1409 1416
    • (2003) J. Cell Sci. , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 27
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • L.A. Cary, J.F. Chang, and J.L. Guan Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn J. Cell Sci. 109 1996 1787 1794
    • (1996) J. Cell Sci. , vol.109 , pp. 1787-1794
    • Cary, L.A.1    Chang, J.F.2    Guan, J.L.3
  • 28
    • 0033002997 scopus 로고    scopus 로고
    • Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2
    • J.D. Owen, P.J. Ruest, D.W. Fry, and S.K. Hanks Induced focal adhesion kinase (FAK) expression in FAK-null cells enhances cell spreading and migration requiring both auto- and activation loop phosphorylation sites and inhibits adhesion-dependent tyrosine phosphorylation of Pyk2 Mol. Cell. Biol. 19 1999 4806 4818
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4806-4818
    • Owen, J.D.1    Ruest, P.J.2    Fry, D.W.3    Hanks, S.K.4
  • 29
    • 0032820782 scopus 로고    scopus 로고
    • Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration
    • D.J. Sieg, C.R. Hauck, and D.D. Schlaepfer Required role of focal adhesion kinase (FAK) for integrin-stimulated cell migration J. Cell Sci. 112 1999 2677 2691
    • (1999) J. Cell Sci. , vol.112 , pp. 2677-2691
    • Sieg, D.J.1    Hauck, C.R.2    Schlaepfer, D.D.3
  • 30
    • 0033617357 scopus 로고    scopus 로고
    • Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration
    • H.R. Reiske, S.C. Kao, L.A. Cary, J.L. Guan, J.F. Lai, and H.C. Chen Requirement of phosphatidylinositol 3-kinase in focal adhesion kinase-promoted cell migration J. Biol. Chem. 274 1999 12361 12366
    • (1999) J. Biol. Chem. , vol.274 , pp. 12361-12366
    • Reiske, H.R.1    Kao, S.C.2    Cary, L.A.3    Guan, J.L.4    Lai, J.F.5    Chen, H.C.6
  • 31
    • 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
    • D.D. Schlaepfer, M.A. Broome, and T. Hunter Fibronectin-stimulated signaling from a focal adhesion kinase-c-Src complex: involvement of the Grb2, p130cas, and Nck adaptor proteins Mol. Cell. Biol. 17 1997 1702 1713
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1702-1713
    • Schlaepfer, D.D.1    Broome, M.A.2    Hunter, T.3
  • 32
    • 0032509565 scopus 로고    scopus 로고
    • Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration
    • L.A. Cary, D.C. Han, T.R. Polte, S.K. Hanks, and J.L. Guan Identification of p130Cas as a mediator of focal adhesion kinase-promoted cell migration J. Cell Biol. 140 1998 211 221
    • (1998) J. Cell Biol. , vol.140 , pp. 211-221
    • Cary, L.A.1    Han, D.C.2    Polte, T.R.3    Hanks, S.K.4    Guan, J.L.5
  • 33
  • 35
    • 0344406976 scopus 로고    scopus 로고
    • Translocation of CrkL to focal adhesions mediates integrin-induced migration downstream of Src family kinases
    • L. Li, D.L. Guris, M. Okura, and A. Imamoto Translocation of CrkL to focal adhesions mediates integrin-induced migration downstream of Src family kinases Mol. Cell. Biol. 23 2003 2883 2892
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 2883-2892
    • Li, L.1    Guris, D.L.2    Okura, M.3    Imamoto, A.4
  • 36
    • 0032213953 scopus 로고    scopus 로고
    • Myoblast city, the Drosophila homolog of DOCK180/CED-5, is required in a Rac signaling pathway utilized for multiple developmental processes
    • K.M. Nolan, K. Barrett, Y. Lu, K.Q. Hu, S. Vincent, and J. Settleman Myoblast city, the Drosophila homolog of DOCK180/CED-5, is required in a Rac signaling pathway utilized for multiple developmental processes Genes Dev. 12 1998 3337 3342
    • (1998) Genes Dev. , vol.12 , pp. 3337-3342
    • Nolan, K.M.1    Barrett, K.2    Lu, Y.3    Hu, K.Q.4    Vincent, S.5    Settleman, J.6
  • 39
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • S.Y. Cho, and R.L. Klemke Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold J. Cell Biol. 156 2002 725 736
    • (2002) J. Cell Biol. , vol.156 , pp. 725-736
    • Cho, S.Y.1    Klemke, R.L.2
  • 40
    • 0033490109 scopus 로고    scopus 로고
    • Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages
    • P.W. Suen, D. Ilic, E. Caveggion, G. Berton, C.H. Damsky, and C.A. Lowell Impaired integrin-mediated signal transduction, altered cytoskeletal structure and reduced motility in Hck/Fgr deficient macrophages J. Cell Sci. 112 1999 4067 4078
    • (1999) J. Cell Sci. , vol.112 , pp. 4067-4078
    • Suen, P.W.1    Ilic, D.2    Caveggion, E.3    Berton, G.4    Damsky, C.H.5    Lowell, C.A.6
  • 42
    • 0032479979 scopus 로고    scopus 로고
    • A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration
    • F. Meng, and C.A. Lowell A beta 1 integrin signaling pathway involving Src-family kinases, Cbl and PI-3 kinase is required for macrophage spreading and migration EMBO J. 17 1998 4391 4403
    • (1998) EMBO J. , vol.17 , pp. 4391-4403
    • Meng, F.1    Lowell, C.A.2
  • 43
    • 0028167979 scopus 로고
    • Beta 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils
    • G. Berton, L. Fumagalli, C. Laudanna, and C. Sorio Beta 2 integrin-dependent protein tyrosine phosphorylation and activation of the FGR protein tyrosine kinase in human neutrophils J. Cell Biol. 126 1994 1111 1121
    • (1994) J. Cell Biol. , vol.126 , pp. 1111-1121
    • Berton, G.1    Fumagalli, L.2    Laudanna, C.3    Sorio, C.4
  • 44
    • 0030008394 scopus 로고    scopus 로고
    • Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions
    • C.A. Lowell, L. Fumagalli, and G. Berton Deficiency of Src family kinases p59/61hck and p58c-fgr results in defective adhesion-dependent neutrophil functions J. Cell Biol. 133 1996 895 910
    • (1996) J. Cell Biol. , vol.133 , pp. 895-910
    • Lowell, C.A.1    Fumagalli, L.2    Berton, G.3
  • 45
    • 0033555864 scopus 로고    scopus 로고
    • Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck
    • A. Mocsai, E. Ligeti, C.A. Lowell, and G. Berton Adhesion-dependent degranulation of neutrophils requires the Src family kinases Fgr and Hck J. Immunol. 162 1999 1120 1126
    • (1999) J. Immunol. , vol.162 , pp. 1120-1126
    • Mocsai, A.1    Ligeti, E.2    Lowell, C.A.3    Berton, G.4
  • 46
    • 0001376760 scopus 로고    scopus 로고
    • Regulation of Src family tyrosine kinase activities in adherent human neutrophils. Evidence that reactive oxygen intermediates produced by adherent neutrophils increase the activity of the p58c-fgr and p53/56lyn tyrosine kinases
    • S.R. Yan, and G. Berton Regulation of Src family tyrosine kinase activities in adherent human neutrophils. Evidence that reactive oxygen intermediates produced by adherent neutrophils increase the activity of the p58c-fgr and p53/56lyn tyrosine kinases J. Biol. Chem. 271 1996 23464 23471
    • (1996) J. Biol. Chem. , vol.271 , pp. 23464-23471
    • Yan, S.R.1    Berton, G.2
  • 48
    • 0028293147 scopus 로고
    • Functional overlap in the src gene family: Inactivation of hck and fgr impairs natural immunity
    • C.A. Lowell, P. Soriano, and H.E. Varmus Functional overlap in the src gene family: inactivation of hck and fgr impairs natural immunity Genes Dev. 8 1994 387 398
    • (1994) Genes Dev. , vol.8 , pp. 387-398
    • Lowell, C.A.1    Soriano, P.2    Varmus, H.E.3
  • 49
    • 0032560544 scopus 로고    scopus 로고
    • Resistance to endotoxic shock and reduced neutrophil migration in mice deficient for the Src-family kinases Hck and Fgr
    • C.A. Lowell, and G. Berton Resistance to endotoxic shock and reduced neutrophil migration in mice deficient for the Src-family kinases Hck and Fgr Proc. Natl. Acad. Sci. U. S. A. 95 1998 7580 7584
    • (1998) Proc. Natl. Acad. Sci. U. S. A. , vol.95 , pp. 7580-7584
    • Lowell, C.A.1    Berton, G.2
  • 51
    • 0033153319 scopus 로고    scopus 로고
    • Urokinase receptor-dependent and -independent p56/59(hck) activation state is a molecular switch between myelomonocytic cell motility and adherence
    • F. Chiaradonna, L. Fontana, C. Iavarone, M.V. Carriero, G. Scholz, M.V. Barone, and M.P. Stoppelli Urokinase receptor-dependent and -independent p56/59(hck) activation state is a molecular switch between myelomonocytic cell motility and adherence EMBO J. 18 1999 3013 3023
    • (1999) EMBO J. , vol.18 , pp. 3013-3023
    • Chiaradonna, F.1    Fontana, L.2    Iavarone, C.3    Carriero, M.V.4    Scholz, G.5    Barone, M.V.6    Stoppelli, M.P.7
  • 52
    • 0037036415 scopus 로고    scopus 로고
    • P59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42 and Rac-dependent manner
    • S. Carreno, E. Caron, C. Cougoule, L.J. Emorine, and I. Maridonneau-Parini p59Hck isoform induces F-actin reorganization to form protrusions of the plasma membrane in a Cdc42 and Rac-dependent manner J. Biol. Chem. 277 2002 21007 21016
    • (2002) J. Biol. Chem. , vol.277 , pp. 21007-21016
    • Carreno, S.1    Caron, E.2    Cougoule, C.3    Emorine, L.J.4    Maridonneau-Parini, I.5
  • 53
    • 0028173679 scopus 로고
    • Myristylation and palmitylation of Src family members: The fats of the matter
    • M.D. Resh Myristylation and palmitylation of Src family members: the fats of the matter Cell 76 1994 411 413
    • (1994) Cell , vol.76 , pp. 411-413
    • Resh, M.D.1
  • 54
    • 84866476582 scopus 로고    scopus 로고
    • Rapid plasma membrane anchoring of newly synthesized p59fyn: Selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3
    • W. van't Hof, and M.D. Resh Rapid plasma membrane anchoring of newly synthesized p59fyn: selective requirement for NH2-terminal myristoylation and palmitoylation at cysteine-3 J. Cell Biol. 136 1997 1023 1035
    • (1997) J. Cell Biol. , vol.136 , pp. 1023-1035
    • Van'T Hof, W.1    Resh, M.D.2
  • 55
    • 0032746309 scopus 로고    scopus 로고
    • Regulation of the RhoA pathway in human endothelial cell spreading on type IV collagen: Role of calcium influx
    • L. Masiero, K.A. Lapidos, I. Ambudkar, and E.C. Kohn Regulation of the RhoA pathway in human endothelial cell spreading on type IV collagen: role of calcium influx J. Cell Sci. 112 1999 3205 3213
    • (1999) J. Cell Sci. , vol.112 , pp. 3205-3213
    • Masiero, L.1    Lapidos, K.A.2    Ambudkar, I.3    Kohn, E.C.4
  • 56
    • 0034594914 scopus 로고    scopus 로고
    • RAFTK/Pyk2 tyrosine kinase mediates the association of p190 RhoGAP with RasGAP and is involved in breast cancer cell invasion
    • S. Zrihan-Licht, Y. Fu, J. Settleman, K. Schinkmann, L. Shaw, I. Keydar, S. Avraham, and H. Avraham RAFTK/Pyk2 tyrosine kinase mediates the association of p190 RhoGAP with RasGAP and is involved in breast cancer cell invasion Oncogene 19 2000 1318 1328
    • (2000) Oncogene , vol.19 , pp. 1318-1328
    • Zrihan-Licht, S.1    Fu, Y.2    Settleman, J.3    Schinkmann, K.4    Shaw, L.5    Keydar, I.6    Avraham, S.7    Avraham, H.8
  • 58
    • 0033847250 scopus 로고    scopus 로고
    • The SH3 domain directs acto-myosin-dependent targeting of v-Src to focal adhesions via phosphatidylinositol 3-kinase
    • V.J. Fincham, V.G. Brunton, and M.C. Frame The SH3 domain directs acto-myosin-dependent targeting of v-Src to focal adhesions via phosphatidylinositol 3-kinase Mol. Cell. Biol. 20 2000 6518 6536
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 6518-6536
    • Fincham, V.J.1    Brunton, V.G.2    Frame, M.C.3
  • 59
    • 0037440109 scopus 로고    scopus 로고
    • Site-specific phosphorylation of platelet focal adhesion kinaes by low-density lipoprotein
    • I.A. Relou, L.A.B. Bax, H.J.M. van Rijn, and J.W.N. Akkerman Site-specific phosphorylation of platelet focal adhesion kinaes by low-density lipoprotein Biochem. J. 369 2003 407 476
    • (2003) Biochem. J. , vol.369 , pp. 407-476
    • Relou, I.A.1    Bax, L.A.B.2    Van Rijn, H.J.M.3    Akkerman, J.W.N.4
  • 60
    • 0029014901 scopus 로고
    • Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae
    • S.M. Robbins, N.A. Quintrell, and J.M. Bishop Myristoylation and differential palmitoylation of the HCK protein-tyrosine kinases govern their attachment to membranes and association with caveolae Mol. Cell. Biol. 15 1995 3507 3515
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 3507-3515
    • Robbins, S.M.1    Quintrell, N.A.2    Bishop, J.M.3
  • 61
    • 0035903208 scopus 로고    scopus 로고
    • Heterogeneous fatty acylation of Src family kinases with polyunsaturated fatty acids regulates raft localization and signal transduction
    • X. Liang, A. Nazarian, H. Erdjument-Bromage, W. Bornmann, P. Tempst, and M.D. Resh Heterogeneous fatty acylation of Src family kinases with polyunsaturated fatty acids regulates raft localization and signal transduction J. Biol. Chem. 276 2001 30987 30994
    • (2001) J. Biol. Chem. , vol.276 , pp. 30987-30994
    • Liang, X.1    Nazarian, A.2    Erdjument-Bromage, H.3    Bornmann, W.4    Tempst, P.5    Resh, M.D.6
  • 62
    • 0038827018 scopus 로고    scopus 로고
    • A lipid raft environment enhances Lyn kinase activity by protecting the active site tyrosine from dephosphorylation
    • R.M. Young, D. Holowka, and B. Baird A lipid raft environment enhances Lyn kinase activity by protecting the active site tyrosine from dephosphorylation J. Biol. Chem. 278 2003 20746 20752
    • (2003) J. Biol. Chem. , vol.278 , pp. 20746-20752
    • Young, R.M.1    Holowka, D.2    Baird, B.3
  • 64
    • 0029034939 scopus 로고
    • C-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism
    • K.B. Kaplan, J.R. Swedlow, D.O. Morgan, and H.E. Varmus c-Src enhances the spreading of src-/- fibroblasts on fibronectin by a kinase-independent mechanism Genes Dev. 9 1995 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
  • 65
    • 0037205266 scopus 로고    scopus 로고
    • PI 3-kinases and PTEN: How opposites chemoattract
    • F.I. Comer, and C.A. Parent PI 3-kinases and PTEN: how opposites chemoattract Cell 109 2002 541 544
    • (2002) Cell , vol.109 , pp. 541-544
    • Comer, F.I.1    Parent, C.A.2
  • 70
    • 0032566062 scopus 로고    scopus 로고
    • Overexpression of EMS1/cortactin in NIH3T3 fibroblasts causes increased cell motility and invasion in vitro
    • A.S. Patel, G.L. Schechter, W.J. Wasilenko, and K.D. Somers Overexpression of EMS1/cortactin in NIH3T3 fibroblasts causes increased cell motility and invasion in vitro Oncogene 16 1998 3227 3232
    • (1998) Oncogene , vol.16 , pp. 3227-3232
    • Patel, A.S.1    Schechter, G.L.2    Wasilenko, W.J.3    Somers, K.D.4
  • 71
    • 0032476012 scopus 로고    scopus 로고
    • The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells
    • C. Huang, J. Liu, C.C. Haudenschild, and X. Zhan The role of tyrosine phosphorylation of cortactin in the locomotion of endothelial cells J. Biol. Chem. 273 1998 25770 25776
    • (1998) J. Biol. Chem. , vol.273 , pp. 25770-25776
    • Huang, C.1    Liu, J.2    Haudenschild, C.C.3    Zhan, X.4
  • 73
    • 0037072731 scopus 로고    scopus 로고
    • Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells
    • B.H. Chen, J.T. Tzen, A.R. Bresnick, and H.C. Chen Roles of Rho-associated kinase and myosin light chain kinase in morphological and migratory defects of focal adhesion kinase-null cells J. Biol. Chem. 277 2002 33857 33863
    • (2002) J. Biol. Chem. , vol.277 , pp. 33857-33863
    • Chen, B.H.1    Tzen, J.T.2    Bresnick, A.R.3    Chen, H.C.4


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