메뉴 건너뛰기




Volumn 6, Issue 2, 2004, Pages 154-161

FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; FOCAL ADHESION KINASE; MITOGEN ACTIVATED PROTEIN KINASE; MYOSIN LIGHT CHAIN KINASE; PAXILLIN; PHOSPHOTRANSFERASE; PROTEIN P130; BCAR1 PROTEIN, MOUSE; CRK ASSOCIATED SUBSTRATE PROTEIN; CYTOSKELETON PROTEIN; FOCAL ADHESION KINASE 1; HYBRID PROTEIN; PHOSPHOPROTEIN; PROTEIN; PROTEIN TYROSINE KINASE; PTK2 PROTEIN, MOUSE; PXN PROTEIN, MOUSE; VESICULAR TRANSPORT ADAPTOR PROTEIN;

EID: 1642586962     PISSN: 14657392     EISSN: None     Source Type: Journal    
DOI: 10.1038/ncb1094     Document Type: Article
Times cited : (1134)

References (41)
  • 1
    • 0030045346 scopus 로고    scopus 로고
    • Cell migration: A physically integrated molecular process
    • Lauffenburger, D. A. & Horwitz, A. F. Cell migration: A physically integrated molecular process. Cell 84, 359-369 (1996).
    • (1996) Cell , vol.84 , pp. 359-369
    • Lauffenburger, D.A.1    Horwitz, A.F.2
  • 2
    • 0036222784 scopus 로고    scopus 로고
    • Adhesion assembly, disassembly and turnover in migrating cells - Over and over and over again
    • Webb, D. J., Parsons, J. T. & Horwitz, A. F. Adhesion assembly, disassembly and turnover in migrating cells - over and over and over again. Nature Cell Biol. 4, E97-E100 (2002).
    • (2002) Nature Cell Biol. , vol.4
    • Webb, D.J.1    Parsons, J.T.2    Horwitz, A.F.3
  • 3
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Ilic, D. et al. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 377, 539-544 (1995).
    • (1995) Nature , vol.377 , pp. 539-544
    • Ilic, D.1
  • 4
    • 0033522510 scopus 로고    scopus 로고
    • Src family kinases are required for integrin but not PDGFR signal transduction
    • Klinghoffer, R. A., Sachsenmaier, C., Cooper, J. A. & Soriano, P. Src family kinases are required for integrin but not PDGFR signal transduction. EMBO J. 18, 2459-2471 (1999).
    • (1999) EMBO J. , vol.18 , pp. 2459-2471
    • Klinghoffer, R.A.1    Sachsenmaier, C.2    Cooper, J.A.3    Soriano, P.4
  • 5
    • 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
    • Fincham, V. J. & Frame, M. C. 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, 81-92 (1998).
    • (1998) EMBO J. , vol.17 , pp. 81-92
    • Fincham, V.J.1    Frame, M.C.2
  • 6
    • 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. & Feng, G.-S. Protein-tyrosine phosphatase Shp-2 regulates cell spreading, migration, and focal adhesion. J. Biol. Chem. 273, 21125-21131 (1998).
    • (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
  • 7
    • 0345593816 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts
    • Angers-Loustau, A. et al. Protein tyrosine phosphatase-PEST regulates focal adhesion disassembly, migration, and cytokinesis in fibroblasts. J. Cell Biol. 144, 1019-1031 (1999).
    • (1999) J. Cell Biol. , vol.144 , pp. 1019-1031
    • Angers-Loustau, A.1
  • 8
    • 0029166094 scopus 로고
    • Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase
    • Bellis, S. L., Miller, J. T. & Turner, C. E. Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase. J. Biol. Chem. 270, 17437-17441 (1995).
    • (1995) J. Biol. Chem. , vol.270 , pp. 17437-17441
    • Bellis, S.L.1    Miller, J.T.2    Turner, C.E.3
  • 9
    • 0028986116 scopus 로고
    • pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk
    • Schaller, M. D. & Parsons, J. T. pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high-affinity binding site for Crk. Mol. Cell. Biol. 15, 2635-2645 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 2635-2645
    • Schaller, M.D.1    Parsons, J.T.2
  • 11
    • 0036142219 scopus 로고    scopus 로고
    • The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling
    • Hagel, M. et al. The adaptor protein paxillin is essential for normal development in the mouse and is a critical transducer of fibronectin signaling. Mol. Cell. Biol. 22, 901-915 (2002).
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 901-915
    • Hagel, M.1
  • 12
    • 0033584466 scopus 로고    scopus 로고
    • p130(Cas), an assembling molecule of actin filaments, promotes cell movement, cell migration, and cell spreading in fibroblasts
    • Honda, H., Nakamoto, T., Sakai, R. & Hirai, H. p130(Cas), an assembling molecule of actin filaments, promotes cell movement, cell migration, and cell spreading in fibroblasts. Biochem. Biophys. Res. Commun. 262, 25-30 (1999).
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 25-30
    • Honda, H.1    Nakamoto, T.2    Sakai, R.3    Hirai, H.4
  • 14
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of α5 integrin, paxillin, and α-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis, C. M., Webb, D. J., Donais, K. & Horwitz, A. F. Differential dynamics of α5 integrin, paxillin, and α -actinin during formation and disassembly of adhesions in migrating cells. J. Cell Biol. 153, 1427-1440 (2001).
    • (2001) J. Cell Biol. , vol.153 , pp. 1427-1440
    • Laukaitis, C.M.1    Webb, D.J.2    Donais, K.3    Horwitz, A.F.4
  • 15
    • 0028350859 scopus 로고
    • FAK, directs SH2-dependent binding of pp60src
    • FAK, directs SH2-dependent binding of pp60src. Mol. Cell. Biol. 14, 1680-1688 (1994).
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1
  • 16
    • 0029979722 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase
    • Chen, H.-C., Appeddu, P. A., Isoda, H. & Guan, J.-L. Phosphorylation of tyrosine 397 in focal adhesion kinase is required for binding phosphatidylinositol 3-kinase. J. Biol. Chem. 271, 26329-26334 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 26329-26334
    • Chen, H.-C.1    Appeddu, P.A.2    Isoda, H.3    Guan, J.-L.4
  • 18
    • 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. 16, 2606-2613 (1996).
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 2606-2613
    • Vuori, K.1    Hirai, H.2    Aizawa, S.3    Ruoslahti, E.4
  • 19
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • Turner, C. E. Paxillin and focal adhesion signalling. Nature Cell Biol. 2, E231-E236 (2000).
    • (2000) Nature Cell Biol. , vol.2
    • Turner, C.E.1
  • 20
    • 0033577810 scopus 로고    scopus 로고
    • Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankryin repeat, ARF-GAP protein: A role in cytoskeletal remodeling
    • Turner, C. E. et al. Paxillin LD4 motif binds PAK and PIX through a novel 95-kD ankryin repeat, ARF-GAP protein: A role in cytoskeletal remodeling. J. Cell Biol. 145, 851-863 (1999).
    • (1999) J. Cell Biol. , vol.145 , pp. 851-863
    • Turner, C.E.1
  • 21
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • Brown, M. C., Perrotta, J. A. & Turner, C. E. Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J. Cell Biol. 135, 1109-1123 (1996).
    • (1996) J. Cell Biol. , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 22
    • 0033579448 scopus 로고    scopus 로고
    • The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin
    • Thomas, J. W. et al. The role of focal adhesion kinase binding in the regulation of tyrosine phosphorylation of paxillin. J. Biol. Chem. 274, 36684-36692 (1999).
    • (1999) J. Biol. Chem. , vol.274 , pp. 36684-36692
    • Thomas, J.W.1
  • 23
    • 0026445719 scopus 로고
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly. J. Cell Biol. 119, 893-903 (1992).
    • (1992) J. Cell Biol. , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 24
    • 0034610997 scopus 로고    scopus 로고
    • Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells
    • Petit, V. et al. Phosphorylation of tyrosine residues 31 and 118 on paxillin regulates cell migration through an association with CRK in NBT-II cells. J. Cell Biol. 148, 957-969 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 957-969
    • Petit, V.1
  • 25
    • 0034644603 scopus 로고    scopus 로고
    • Localized Rac activation dynamics visualized in living cells
    • Kraynov, V. S. et al. Localized Rac activation dynamics visualized in living cells. Science 290, 333-337 (2000).
    • (2000) Science , vol.290 , pp. 333-337
    • Kraynov, V.S.1
  • 26
    • 0034865456 scopus 로고    scopus 로고
    • Rho GTPases and cell migration
    • Ridley, A. J. Rho GTPases and cell migration. J. Cell Sci. 114, 2713-2722 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 2713-2722
    • Ridley, A.J.1
  • 27
    • 0344845048 scopus 로고    scopus 로고
    • Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis
    • Ishibe, S., Joly, D., Zhu, X. & Cantley, L. G. Phosphorylation-dependent paxillin-ERK association mediates hepatocyte growth factor-stimulated epithelial morphogenesis. Mol. Cell 12, 1275-1285 (2003).
    • (2003) Mol. Cell , vol.12 , pp. 1275-1285
    • Ishibe, S.1    Joly, D.2    Zhu, X.3    Cantley, L.G.4
  • 28
    • 0042672912 scopus 로고    scopus 로고
    • PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK activation
    • Slack-Davis, J. K. et al. PAK1 phosphorylation of MEK1 regulates fibronectin-stimulated MAPK activation. J. Cell Biol. 162, 281-291 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 281-291
    • Slack-Davis, J.K.1
  • 29
    • 0030931217 scopus 로고    scopus 로고
    • Regulation of cell motility by migoten-activated protein kinase
    • Klemke, R. L. et al. Regulation of cell motility by migoten-activated protein kinase. J. Cell Biol. 137, 481-492 (1997).
    • (1997) J. Cell Biol. , vol.137 , pp. 481-492
    • Klemke, R.L.1
  • 30
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir, E. & Geiger, B. Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114, 3583-3590 (2001).
    • (2001) J. Cell Sci. , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 31
    • 0034660524 scopus 로고    scopus 로고
    • Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src
    • Fincham, V., James, M., Frame, M. & Winder, S. Active ERK/MAP kinase is targeted to newly forming cell-matrix adhesions by integrin engagement and v-Src. EMBO J. 19, 2911-2923 (2000).
    • (2000) EMBO J. , vol.19 , pp. 2911-2923
    • Fincham, V.1    James, M.2    Frame, M.3    Winder, S.4
  • 32
    • 0028841220 scopus 로고
    • Tyrosine phosphorylation and cytosketal tension regulate the release of fibroblast adhesions
    • Crowley, E. & Horwitz, A. F. Tyrosine phosphorylation and cytosketal tension regulate the release of fibroblast adhesions. J. Cell Biol. 131, 525-537 (1995).
    • (1995) J. Cell Biol. , vol.131 , pp. 525-537
    • Crowley, E.1    Horwitz, A.F.2
  • 33
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren, X. D. et al. Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113, 3673-3678 (2000).
    • (2000) J. Cell Sci. , vol.113 , pp. 3673-3678
    • Ren, X.D.1
  • 34
    • 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
    • Chen, B.-C., Tzen, J. T., Bresnick, A. R. & Chen, H.-C. 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, 33857-33863 (2002).
    • (2002) J. Biol. Chem. , vol.277 , pp. 33857-33863
    • Chen, B.-C.1    Tzen, J.T.2    Bresnick, A.R.3    Chen, H.-C.4
  • 35
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src
    • Carragher, N. O., Westhoff, M. A., Fincham, V. J., Schaller, M. D. & Frame, M. C. A novel role for FAK as a protease-targeting adaptor protein: Regulation by p42 ERK and Src. Curr. Biol. 13, 1442-1450 (2003).
    • (2003) Curr. Biol. , vol.13 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 36
    • 0029820264 scopus 로고    scopus 로고
    • Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity
    • Huttenlocher, A., Ginsberg, M. H. & Horwitz, A. F. Modulation of cell migration by integrin-mediated cytoskeletal linkages and ligand-binding affinity. J. Cell Biol. 134, 1551-1562 (1996).
    • (1996) J. Cell Biol. , vol.134 , pp. 1551-1562
    • Huttenlocher, A.1    Ginsberg, M.H.2    Horwitz, A.F.3
  • 37
    • 0035930548 scopus 로고    scopus 로고
    • Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts
    • Dourdin, N. et al. Reduced cell migration and disruption of the actin cytoskeleton in calpain-deficient embryonic fibroblasts. J. Biol. Chem. 276, 48382-48388 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 48382-48388
    • Dourdin, N.1
  • 38
    • 0035800777 scopus 로고    scopus 로고
    • The cytoskeletal/non-muscle isoform of α-actinin is phosphorylated on its actin-binding domain by focal adhesion kinase
    • Izaguirre, G. et al. The cytoskeletal/non-muscle isoform of α-actinin is phosphorylated on its actin-binding domain by focal adhesion kinase. J. Biol. Chem. 276, 28676-28685 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 28676-28685
    • Izaguirre, G.1
  • 39
    • 0029153801 scopus 로고
    • c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation
    • Chang, J. H., Settleman, J. & Parsons, S. J. c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation. J. Cell Biol. 130, 355-368 (1995).
    • (1995) J. Cell Biol. , vol.130 , pp. 355-368
    • Chang, J.H.1    Settleman, J.2    Parsons, S.J.3
  • 40
    • 0029164688 scopus 로고
    • A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function
    • Catling, A. D., Schaeffer, H. J., Reuter, C. W., Reddy, G. R. & Weber, M. J. A proline-rich sequence unique to MEK1 and MEK2 is required for raf binding and regulates MEK function. Mol. Cell. Biol. 15, 5214-5225 (1995).
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5214-5225
    • Catling, A.D.1    Schaeffer, H.J.2    Reuter, C.W.3    Reddy, G.R.4    Weber, M.J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.