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Volumn 159, Issue 6, 2002, Pages 1071-1086

The fibronectin-binding integrins α5β1 and αvβ3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis

Author keywords

Cell matrix adhesion; Fibronectin; Integrin; Matrix assembly; Rho GTPase

Indexed keywords

BINDING PROTEIN; FIBRONECTIN; ISOPROTEIN; PROTEIN SUBUNIT; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; UNCLASSIFIED DRUG; VERY LATE ACTIVATION ANTIGEN 5; VITRONECTIN RECEPTOR;

EID: 0037164867     PISSN: 00219525     EISSN: None     Source Type: Journal    
DOI: 10.1083/jcb.200205014     Document Type: Article
Times cited : (285)

References (76)
  • 1
    • 0027971378 scopus 로고
    • The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function
    • Aota, S., M. Nomizu, and K. Yamada. 1994. The short amino acid sequence Pro-His-Ser-Arg-Asn in human fibronectin enhances cell-adhesive function. J. Biol. Chem. 269:24756-24761.
    • (1994) J. Biol. Chem. , vol.269 , pp. 24756-24761
    • Aota, S.1    Nomizu, M.2    Yamada, K.3
  • 2
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur, W., L. Petch, and K. Burridge. 2000. Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10:719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.1    Petch, L.2    Burridge, K.3
  • 3
    • 0035807873 scopus 로고    scopus 로고
    • Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer
    • Baneyx, G., L. Baugh, and V. Vogel. 2001. Coexisting conformations of fibronectin in cell culture imaged using fluorescence resonance energy transfer. Proc. Natl. Acad. Sci. USA. 98:14464-14468.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 14464-14468
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 6
    • 0028245615 scopus 로고
    • Identification of a novel integrin binding site in fibronectin. Differential utilization by beta 3 integrins
    • Bowditch, R., M. Hariharan, E. Tominna, J. Smith, K. Yamada, E. Getzoff, and M. Ginsberg. 1994. Identification of a novel integrin binding site in fibronectin. Differential utilization by beta 3 integrins. J. Biol. Chem. 269:10856-10863.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10856-10863
    • Bowditch, R.1    Hariharan, M.2    Tominna, E.3    Smith, J.4    Yamada, K.5    Getzoff, E.6    Ginsberg, M.7
  • 7
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga, V., L. Machesky, A. Hall, and N. Hotchin. 1997. The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137:1421-1431.
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.1    Machesky, L.2    Hall, A.3    Hotchin, N.4
  • 8
    • 0023234083 scopus 로고
    • Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130-kDa alpha subunit
    • Cheresh, D., and J. Harper. 1987. Arg-Gly-Asp recognition by a cell adhesion receptor requires its 130-kDa alpha subunit. J. Biol. Chem. 262:1434-1437.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1434-1437
    • Cheresh, D.1    Harper, J.2
  • 9
    • 0030943367 scopus 로고    scopus 로고
    • Localization of fibronectin matrix assembly sites on fibroblasts and endothelial cells
    • Christopher, R., A. Kowalczyk, and P. McKeown-Longo. 1997. Localization of fibronectin matrix assembly sites on fibroblasts and endothelial cells. J. Cell Sci. 110:569-581.
    • (1997) J. Cell Sci. , vol.110 , pp. 569-581
    • Christopher, R.1    Kowalczyk, A.2    McKeown-Longo, P.3
  • 10
    • 0035941075 scopus 로고    scopus 로고
    • Taking cell-matrix adhesions to the third dimension
    • Cukierman, E., R. Pankov, D. Stevens, and K. Yamada. 2001. Taking cell-matrix adhesions to the third dimension. Science. 294:1708-1712.
    • (2001) Science , vol.294 , pp. 1708-1712
    • Cukierman, E.1    Pankov, R.2    Stevens, D.3    Yamada, K.4
  • 11
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins, and growth control
    • Danen, E., and K. Yamada. 2001. Fibronectin, integrins, and growth control. J. Cell. Physiol. 189:1-13.
    • (2001) J. Cell. Physiol. , vol.189 , pp. 1-13
    • Danen, E.1    Yamada, K.2
  • 12
    • 0029100101 scopus 로고
    • Requirement for the synergy site for cell adhesion to fibronectin depends on the activation state of integrin alpha 5 beta 1
    • Danen, E., S. Aota, A. van Kraats, K. Yamada, D. Ruiter, and G. van Muijen. 1995. Requirement for the synergy site for cell adhesion to fibronectin depends on the activation state of integrin alpha 5 beta 1. J. Biol. Chem. 270:21612-21618.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21612-21618
    • Danen, E.1    Aota, S.2    Van Kraats, A.3    Yamada, K.4    Ruiter, D.5    Van Muijen, G.6
  • 13
    • 0030568857 scopus 로고    scopus 로고
    • Integrin beta 3 cDNA transfection into a highly metastatic alpha v beta 3-negative human melanoma cell line inhibits invasion and experimental metastasis
    • Danen, E., A. van Kraats, I. Cornelissen, D. Ruiter, and G. van Muijen. 1996. Integrin beta 3 cDNA transfection into a highly metastatic alpha v beta 3-negative human melanoma cell line inhibits invasion and experimental metastasis. Biochem. Biophys. Res. Commun. 226:75-81.
    • (1996) Biochem. Biophys. Res. Commun. , vol.226 , pp. 75-81
    • Danen, E.1    Van Kraats, A.2    Cornelissen, I.3    Ruiter, D.4    Van Muijen, G.5
  • 14
    • 0034739844 scopus 로고    scopus 로고
    • Dual stimulation of Ras/mitogen-activated protein kinase and RhoA by cell adhesion to fibronectin supports growth factor-stimulated cell cycle progression
    • Danen, E., P. Sonneveld, A. Sonnenberg, and K. Yamada. 2000. Dual stimulation of Ras/mitogen-activated protein kinase and RhoA by cell adhesion to fibronectin supports growth factor-stimulated cell cycle progression. J. Cell Biol. 151:1413-1422.
    • (2000) J. Cell Biol. , vol.151 , pp. 1413-1422
    • Danen, E.1    Sonneveld, P.2    Sonnenberg, A.3    Yamada, K.4
  • 15
    • 0028979154 scopus 로고
    • Consequences of lack of beta 1 integrin gene expression in mice
    • Fässler, R., and M. Meyer. 1995. Consequences of lack of beta 1 integrin gene expression in mice. Genes Dev. 9:1896-1908.
    • (1995) Genes Dev. , vol.9 , pp. 1896-1908
    • Fässler, R.1    Meyer, M.2
  • 16
    • 0029820859 scopus 로고    scopus 로고
    • Differential utilization of VLA-4 (alpha 4 beta 1) and -5 (alpha 5 beta 1) integrins during the development of mouse bone marrow-derived mast cells
    • Fehlner-Gardiner, C., S. Uniyal, C. von Ballestrem, and B. Chan. 1996. Differential utilization of VLA-4 (alpha 4 beta 1) and -5 (alpha 5 beta 1) integrins during the development of mouse bone marrow-derived mast cells. Differentiation. 60:317-325.
    • (1996) Differentiation , vol.60 , pp. 317-325
    • Fehlner-Gardiner, C.1    Uniyal, S.2    Von Ballestrem, C.3    Chan, B.4
  • 17
    • 0029892628 scopus 로고    scopus 로고
    • Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin
    • Flinn, H., and A. Ridley. 1996. Rho stimulates tyrosine phosphorylation of focal adhesion kinase, p130 and paxillin. J. Cell Sci. 109:1133-1141.
    • (1996) J. Cell Sci. , vol.109 , pp. 1133-1141
    • Flinn, H.1    Ridley, A.2
  • 18
    • 0026063230 scopus 로고
    • Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function
    • Frelinger, A., III, X. Du, E. Plow, and M. Ginsberg. 1991. Monoclonal antibodies to ligand-occupied conformers of integrin alpha IIb beta 3 (glycoprotein IIb-IIIa) alter receptor affinity, specificity, and function. J. Biol. Chem. 266:17106-17111.
    • (1991) J. Biol. Chem. , vol.266 , pp. 17106-17111
    • Frelinger A. III1    Du, X.2    Plow, E.3    Ginsberg, M.4
  • 19
    • 0035651254 scopus 로고    scopus 로고
    • Rho-family GTPases in cadherin-mediated cell-cell adhesion
    • Fukata, M., and K. Kaibuchi. 2001. Rho-family GTPases in cadherin-mediated cell-cell adhesion. Nat. Rev. Mol. Cell Biol. 2:887-897.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 887-897
    • Fukata, M.1    Kaibuchi, K.2
  • 20
    • 0037189557 scopus 로고    scopus 로고
    • ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin
    • Gaultier, A., H. Cousin, T. Darribere, and D. Alfandari. 2002. ADAM13 disintegrin and cysteine-rich domains bind to the second heparin-binding domain of fibronectin. J. Biol. Chem. 277:23336-23344.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23336-23344
    • Gaultier, A.1    Cousin, H.2    Darribere, T.3    Alfandari, D.4
  • 21
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger, B., A. Bershadsky, R. Pankov, and K. Yamada. 2001. Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2:793-805.
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.4
  • 22
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George, E., E. Georges-Labouesse, R. Patel-King, H. Rayburn, and R. Hynes. 1993. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development. 119:1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.1    Georges-Labouesse, E.2    Patel-King, R.3    Rayburn, H.4    Hynes, R.5
  • 23
    • 0025214421 scopus 로고
    • Elevated levels of the alpha 5 beta 1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells
    • Giancotti, F., and E. Ruoslahti. 1990. Elevated levels of the alpha 5 beta 1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell. 60:849-859.
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.1    Ruoslahti, E.2
  • 24
    • 0033794569 scopus 로고    scopus 로고
    • Complexity and specificity of integrin signalling
    • Giancotti, F. 2000. Complexity and specificity of integrin signalling. Nat. Cell Biol. 2:E13-E14.
    • (2000) Nat. Cell Biol. , vol.2
    • Giancotti, F.1
  • 25
    • 0033552615 scopus 로고    scopus 로고
    • Induction of cell scattering by expression of beta 1 integrins in beta 1-deficient epithelial cells requires activation of members of the rho family of GTPases and downregulation of cadherin and catenin function
    • Gimond, C., A. van der Flier, S. van Delft, C. Brakebusch, I. Kuikman, J. Collard, R. Fassler, and A. Sonnenberg. 1999. Induction of cell scattering by expression of beta 1 integrins in beta 1-deficient epithelial cells requires activation of members of the rho family of GTPases and downregulation of cadherin and catenin function. J. Cell Biol. 147:1325-1340.
    • (1999) J. Cell Biol. , vol.147 , pp. 1325-1340
    • Gimond, C.1    Van der Flier, A.2    Van Delft, S.3    Brakebusch, C.4    Kuikman, I.5    Collard, J.6    Fassler, R.7    Sonnenberg, A.8
  • 26
    • 0025338007 scopus 로고
    • Developmental changes in expression of contractile and cytoskeletal proteins in human aortic smooth muscle
    • Glukhova, M., M. Frid, and V. Koteliansky. 1990. Developmental changes in expression of contractile and cytoskeletal proteins in human aortic smooth muscle. J. Biol. Chem. 265:13042-13046.
    • (1990) J. Biol. Chem. , vol.265 , pp. 13042-13046
    • Glukhova, M.1    Frid, M.2    Koteliansky, V.3
  • 27
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner, B. 1996. Cell adhesion: The molecular basis of tissue architecture and morphogenesis. Cell. 84:345-357.
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.1
  • 28
    • 0034729916 scopus 로고    scopus 로고
    • Rho GTPases: Molecular switches that control the organization and dynamics of the actin cytoskeleton
    • Hall, A., and C. Nobes. 2000. Rho GTPases: Molecular switches that control the organization and dynamics of the actin cytoskeleton. Philos. Trans. R. Soc. Lond. B Biol. Sci. 355:965-970.
    • (2000) Philos. Trans. R. Soc. Lond. B Biol. Sci. , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.2
  • 29
    • 0017904907 scopus 로고
    • Transmembrane linkage of fibronectin to intracellular actin-containing filaments in cultured human fibroblasts
    • Heggeness, M., J. Ash, and S. Singer. 1978. Transmembrane linkage of fibronectin to intracellular actin-containing filaments in cultured human fibroblasts. Ann. NY Acad. Sci. 312:414-417.
    • (1978) Ann. NY Acad. Sci. , vol.312 , pp. 414-417
    • Heggeness, M.1    Ash, J.2    Singer, S.3
  • 30
    • 0028364087 scopus 로고
    • Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin
    • Hocking, D., J. Sottile, and P. McKeown-Longo. 1994. Fibronectin's III-1 module contains a conformation-dependent binding site for the amino-terminal region of fibronectin. J. Biol. Chem. 269:19183-19187.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19183-19187
    • Hocking, D.1    Sottile, J.2    McKeown-Longo, P.3
  • 31
    • 0004043397 scopus 로고
    • Springer-Verlag New York, Inc., New York. 546 pp
    • Hynes, R.O. 1990. Fibronectins. Springer-Verlag New York, Inc., New York. 546 pp.
    • (1990) Fibronectins
    • Hynes, R.O.1
  • 32
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. 2002. Integrins: Bidirectional, allosteric signaling machines. Cell. 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.1
  • 33
    • 0018036788 scopus 로고
    • Relationships between fibronectin (LETS protein) and actin
    • Hynes, R., and A. Destree. 1978. Relationships between fibronectin (LETS protein) and actin. Cell. 15:875-886.
    • (1978) Cell , vol.15 , pp. 875-886
    • Hynes, R.1    Destree, A.2
  • 34
    • 0034710157 scopus 로고    scopus 로고
    • The evolution of cell adhesion
    • Hynes, R., and Q. Zhao. 2000. The evolution of cell adhesion. J. Cell Biol. 150: F89-F96.
    • (2000) J. Cell Biol. , vol.150
    • Hynes, R.1    Zhao, Q.2
  • 36
    • 0029833422 scopus 로고    scopus 로고
    • Episomal vectors rapidly and stably produce high-titer recombinant retrovirus
    • Kinsella, T., and G. Nolan. 1996. Episomal vectors rapidly and stably produce high-titer recombinant retrovirus. Hum. Gene Ther. 7:1405-1413.
    • (1996) Hum. Gene Ther. , vol.7 , pp. 1405-1413
    • Kinsella, T.1    Nolan, G.2
  • 38
    • 0037092520 scopus 로고    scopus 로고
    • Differential regulation of Rho GTPases by β1 and β3 integrins: The role of the extracellular domain of integrin in intracellular signaling
    • Miao, H., S. Li, Y. Hu, S. Yuan, Y. Zhao, B. Chen, W. Puzon-McLaughlin, T. Tarui, J. Shyy, Y. Takada, and S. Usami. 2002. Differential regulation of Rho GTPases by β1 and β3 integrins: the role of the extracellular domain of integrin in intracellular signaling. J. Cell Sci. 115:2199-2206.
    • (2002) J. Cell Sci. , vol.115 , pp. 2199-2206
    • Miao, H.1    Li, S.2    Hu, Y.3    Yuan, S.4    Zhao, Y.5    Chen, B.6    Puzon-McLaughlin, W.7    Tarui, T.8    Shyy, J.9    Takada, Y.10    Usami, S.11
  • 39
    • 0031002437 scopus 로고    scopus 로고
    • Cross talk between adhesion molecules: Control of N-cadherin activity by intracellular signals elicited by beta1 and beta3 integrins in migrating neural crest cells
    • Monier-Gavelle, F., and J. Duband. 1997. Cross talk between adhesion molecules: Control of N-cadherin activity by intracellular signals elicited by beta1 and beta3 integrins in migrating neural crest cells. J. Cell Biol. 137:1663-1681.
    • (1997) J. Cell Biol. , vol.137 , pp. 1663-1681
    • Monier-Gavelle, F.1    Duband, J.2
  • 40
    • 0029161848 scopus 로고
    • Organization of the provisional fibronectin matrix: Control by products of blood coagulation
    • Mosher, D. 1995. Organization of the provisional fibronectin matrix: Control by products of blood coagulation. Thromb. Haemost. 74:529-533.
    • (1995) Thromb. Haemost. , vol.74 , pp. 529-533
    • Mosher, D.1
  • 41
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C., and A. Hall. 1995. Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.1    Hall, A.2
  • 42
    • 0035823593 scopus 로고    scopus 로고
    • Cadherin engagement regulates Rho family GTPases
    • Noren, N., C. Niessen, B. Gumbiner, and K. Burridge. 2001. Cadherin engagement regulates Rho family GTPases. J. Biol. Chem. 276:33305-33308.
    • (2001) J. Biol. Chem. , vol.276 , pp. 33305-33308
    • Noren, N.1    Niessen, C.2    Gumbiner, B.3    Burridge, K.4
  • 43
    • 0033515070 scopus 로고    scopus 로고
    • Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein
    • Ohashi, T., D. Kiehart, and H. Erickson. 1999. Dynamics and elasticity of the fibronectin matrix in living cell culture visualized by fibronectin-green fluorescent protein. Proc. Natl. Acad. Sci. USA. 96:2153-2158.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 2153-2158
    • Ohashi, T.1    Kiehart, D.2    Erickson, H.3
  • 44
    • 0034611008 scopus 로고    scopus 로고
    • Integrin dynamics and matrix assembly: Tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis
    • Pankov, R., E. Cukierman, B. Katz, K. Matsumoto, D. Lin, S. Lin, C. Hahn, and K. Yamada. 2000. Integrin dynamics and matrix assembly: Tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis. J. Cell Biol. 148:1075-1090.
    • (2000) J. Cell Biol. , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.3    Matsumoto, K.4    Lin, D.5    Lin, S.6    Hahn, C.7    Yamada, K.8
  • 45
    • 0024534377 scopus 로고
    • Changes in integrin receptors on oncogenically transformed cells
    • Plantefaber, L., and R. Hynes. 1989. Changes in integrin receptors on oncogenically transformed cells. Cell. 56:281-290.
    • (1989) Cell , vol.56 , pp. 281-290
    • Plantefaber, L.1    Hynes, R.2
  • 46
    • 0031844821 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 by integrins mediates cell spreading
    • Price, L., J. Leng, M. Schwartz, and G. Bokoch. 1998. Activation of Rac and Cdc42 by integrins mediates cell spreading. Mol. Biol. Cell. 9:1863-1871.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 1863-1871
    • Price, L.1    Leng, J.2    Schwartz, M.3    Bokoch, G.4
  • 47
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X., W. Kiosses, and M. Schwartz. 1999. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.1    Kiosses, W.2    Schwartz, M.3
  • 48
    • 0033731010 scopus 로고    scopus 로고
    • Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover
    • Ren, X., W. Kiosses, D. Sieg, C. Otey, D. Schlaepfer, and M. Schwartz. 2000. Focal adhesion kinase suppresses Rho activity to promote focal adhesion turnover. J. Cell Sci. 113:3673-3678.
    • (2000) J. Cell Sci. , vol.113 , pp. 3673-3678
    • Ren, X.1    Kiosses, W.2    Sieg, D.3    Otey, C.4    Schlaepfer, D.5    Schwartz, M.6
  • 50
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factots
    • Ridley, A., and A. Hall. 1992. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factots. Cell. 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.1    Hall, A.2
  • 51
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner, K., A. Hall, and J. Small. 1999. Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 9:640-648.
    • (1999) Curr. Biol. , vol.9 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.3
  • 52
    • 0032584382 scopus 로고    scopus 로고
    • Restoration of beta1A integrins is required for lysophosphatidic acid-induced migration of beta1-null mouse fibroblastic cells
    • Sakai, T., O. Peyruchaud, R. Fassler, and D. Mosher. 1998a. Restoration of beta1A integrins is required for lysophosphatidic acid-induced migration of beta1-null mouse fibroblastic cells. J. Biol. Chem. 273:19378-19382.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19378-19382
    • Sakai, T.1    Peyruchaud, O.2    Fassler, R.3    Mosher, D.4
  • 53
    • 0032549860 scopus 로고    scopus 로고
    • Modulation of beta1A integrin functions by tyrosine residues in the beta1 cytoplasmic domain
    • Sakai, T., Q. Zhang, R. Fassler, and D. Mosher. 1998b. Modulation of beta1A integrin functions by tyrosine residues in the beta1 cytoplasmic domain. J. Cell Biol. 141:527-538.
    • (1998) J. Cell Biol. , vol.141 , pp. 527-538
    • Sakai, T.1    Zhang, Q.2    Fassler, R.3    Mosher, D.4
  • 55
    • 0035575458 scopus 로고    scopus 로고
    • Integrin signaling revisited
    • Schwartz, M. 2001. Integrin signaling revisited. Trends Cell Biol. 11:466-470.
    • (2001) Trends Cell Biol. , vol.11 , pp. 466-470
    • Schwartz, M.1
  • 56
    • 0034256024 scopus 로고    scopus 로고
    • Signaling networks linking integrins and rho family GTPases
    • Schwartz, M., and S. Shattil. 2000. Signaling networks linking integrins and rho family GTPases. Trends Biochem. Sci. 25:388-391.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 388-391
    • Schwartz, M.1    Shattil, S.2
  • 57
    • 0032869760 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis: A paradigm for extracellular matrix assembly
    • Schwarzbauer, J., and J. Sechler. 1999. Fibronectin fibrillogenesis: A paradigm for extracellular matrix assembly. Curr. Opin. Cell Biol. 11:622-627.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 622-627
    • Schwarzbauer, J.1    Sechler, J.2
  • 58
    • 0035802114 scopus 로고    scopus 로고
    • A novel fibronectin binding site required for fibronectin fibril growth during matrix assembly
    • Sechler, J., H. Rao, A. Cumiskey, I. Vega-Colon, M. Smith, T. Murata, and J. Schwarzbauer. 2001. A novel fibronectin binding site required for fibronectin fibril growth during matrix assembly. J. Cell Biol. 154:1081-1088.
    • (2001) J. Cell Biol. , vol.154 , pp. 1081-1088
    • Sechler, J.1    Rao, H.2    Cumiskey, A.3    Vega-Colon, I.4    Smith, M.5    Murata, T.6    Schwarzbauer, J.7
  • 59
    • 0034955193 scopus 로고    scopus 로고
    • Y-27632, an inhibitor of Rho-associated kinases, prevents tyrosine phosphorylation of focal adhesion kinase and paxillin induced by bombesin: Dissociation from tyrosine phosphorylation of p130(CAS)
    • Sinnett-Smith, J., J. Lunn, D. Leopoldt, and E. Rozengurt. 2001. Y-27632, an inhibitor of Rho-associated kinases, prevents tyrosine phosphorylation of focal adhesion kinase and paxillin induced by bombesin: Dissociation from tyrosine phosphorylation of p130(CAS). Exp. Cell Res. 266:292-302.
    • (2001) Exp. Cell Res. , vol.266 , pp. 292-302
    • Sinnett-Smith, J.1    Lunn, J.2    Leopoldt, D.3    Rozengurt, E.4
  • 60
    • 0032478821 scopus 로고    scopus 로고
    • Characterization of graf, the GTPase-activating protein for rho associated with focal adhesion kinase. Phosphorylation and possible regulation by mitogen-activated protein kinase
    • Taylor, J., J. Hildebrand, C. Mack, M. Cox, and J. Parsons. 1998. Characterization of graf, the GTPase-activating protein for rho associated with focal adhesion kinase. Phosphorylation and possible regulation by mitogen-activated protein kinase. J. Biol. Chem. 273:8063-8070.
    • (1998) J. Biol. Chem. , vol.273 , pp. 8063-8070
    • Taylor, J.1    Hildebrand, J.2    Mack, C.3    Cox, M.4    Parsons, J.5
  • 61
    • 0032991640 scopus 로고    scopus 로고
    • Cytoskeletal changes induced by GRAF, the GTPase regulator associated with focal adhesion kinase, are mediated by Rho
    • Taylor, J., M. Macklem, and J. Parsons. 1999. Cytoskeletal changes induced by GRAF, the GTPase regulator associated with focal adhesion kinase, are mediated by Rho. J. Cell Sci. 112:231-242.
    • (1999) J. Cell Sci. , vol.112 , pp. 231-242
    • Taylor, J.1    Macklem, M.2    Parsons, J.3
  • 62
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • van der Flier, A., and A. Sonnenberg. 2001. Function and interactions of integrins. Cell Tissue Res. 305:285-298.
    • (2001) Cell Tissue Res. , vol.305 , pp. 285-298
    • Van der Flier, A.1    Sonnenberg, A.2
  • 63
    • 0033103763 scopus 로고    scopus 로고
    • Cadherins and tissue formation: Integrating adhesion and signaling
    • Vleminckx, K., and R. Kemler. 1999. Cadherins and tissue formation: Integrating adhesion and signaling. Bioessays. 21:211-220.
    • (1999) Bioessays , vol.21 , pp. 211-220
    • Vleminckx, K.1    Kemler, R.2
  • 64
    • 0034001209 scopus 로고    scopus 로고
    • Functional interaction between E-cadherin and alphav-containing integrins in carcinoma cells
    • von Schlippe, M., J. Marshall, P. Perry, M. Stone, A. Zhu, and I. Hart. 2000. Functional interaction between E-cadherin and alphav-containing integrins in carcinoma cells. J. Cell Sci. 113:425-437.
    • (2000) J. Cell Sci. , vol.113 , pp. 425-437
    • Von Schlippe, M.1    Marshall, J.2    Perry, P.3    Stone, M.4    Zhu, A.5    Hart, I.6
  • 65
    • 0030936450 scopus 로고    scopus 로고
    • Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies
    • Weaver, V., O. Petersen, F. Wang, C. Larabell, P. Briand, C. Damsky, and M. Bissell. 1997. Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies. J. Cell Biol. 137:231-245.
    • (1997) J. Cell Biol. , vol.137 , pp. 231-245
    • Weaver, V.1    Petersen, O.2    Wang, F.3    Larabell, C.4    Briand, P.5    Damsky, C.6    Bissell, M.7
  • 67
    • 0035052095 scopus 로고    scopus 로고
    • Syndecans: Transmembrane modulators of adhesion and matrix assembly
    • Woods, A. 2001. Syndecans: Transmembrane modulators of adhesion and matrix assembly. J. Clin. Invest. 107:935-941.
    • (2001) J. Clin. Invest. , vol.107 , pp. 935-941
    • Woods, A.1
  • 68
    • 0027422170 scopus 로고
    • The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly
    • Wu, C., J. Bauer, R. Juliano, and J. McDonald. 1993. The alpha 5 beta 1 integrin fibronectin receptor, but not the alpha 5 cytoplasmic domain, functions in an early and essential step in fibronectin matrix assembly. J. Biol. Chem. 268:21883-21888.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21883-21888
    • Wu, C.1    Bauer, J.2    Juliano, R.3    McDonald, J.4
  • 69
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu, C., V. Keivens, T. O'Toole, J. McDonald, and M. Ginsberg. 1995. Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell. 83:715-724.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.2    O'Toole, T.3    McDonald, J.4    Ginsberg, M.5
  • 70
    • 0029800576 scopus 로고    scopus 로고
    • Identification of a new biological function for the integrin alpha v beta 3: Initiation of fibronectin matrix assembly
    • Wu, C., P. Hughes, M. Ginsberg, and J. McDonald. 1996. Identification of a new biological function for the integrin alpha v beta 3: Initiation of fibronectin matrix assembly. Cell Adhes. Commun. 4:149-158.
    • (1996) Cell Adhes. Commun. , vol.4 , pp. 149-158
    • Wu, C.1    Hughes, P.2    Ginsberg, M.3    McDonald, J.4
  • 71
    • 0029957287 scopus 로고    scopus 로고
    • Fibronectin receptor functions in embryonic cells deficient in alpha 5 beta 1 integrin can be replaced by alpha V integrins
    • Yang, J., and R. Hynes. 1996. Fibronectin receptor functions in embryonic cells deficient in alpha 5 beta 1 integrin can be replaced by alpha V integrins. Mol. Biol. Cell. 7:1737-1748.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1737-1748
    • Yang, J.1    Hynes, R.2
  • 73
    • 0030928057 scopus 로고    scopus 로고
    • Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction
    • Zhang, Q., M. Magnusson, and D. Mosher. 1997. Lysophosphatidic acid and microtubule-destabilizing agents stimulate fibronectin matrix assembly through Rho-dependent actin stress fiber formation and cell contraction. Mol. Biol. Cell. 8:1415-1425.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 1415-1425
    • Zhang, Q.1    Magnusson, M.2    Mosher, D.3
  • 74
    • 0032590073 scopus 로고    scopus 로고
    • Functional beta1-integrins release the suppression of fibronectin matrix assembly by vitronectin
    • Zhang, Q., T. Sakai, J. Nowlen, I. Hayashi, R. Fassler, and D. Mosher. 1999. Functional beta1-integrins release the suppression of fibronectin matrix assembly by vitronectin. J. Biol. Chem. 274:368-375.
    • (1999) J. Biol. Chem. , vol.274 , pp. 368-375
    • Zhang, Q.1    Sakai, T.2    Nowlen, J.3    Hayashi, I.4    Fassler, R.5    Mosher, D.6
  • 75
    • 0027175838 scopus 로고
    • The alpha v beta 1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin
    • Zhang, Z., A. Morla, K. Vuori, J. Bauer, R. Juliano, and E. Ruoslahti. 1993. The alpha v beta 1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin. J. Cell Biol. 122:235-242.
    • (1993) J. Cell Biol. , vol.122 , pp. 235-242
    • Zhang, Z.1    Morla, A.2    Vuori, K.3    Bauer, J.4    Juliano, R.5    Ruoslahti, E.6
  • 76
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong, C., M. Chrzanowska-Wodnicka, J. Brown, A. Shaub, A. Belkin, and K. Burridge. 1998. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 141:539-551.
    • (1998) J. Cell Biol. , vol.141 , pp. 539-551
    • Zhong, C.1    Chrzanowska-Wodnicka, M.2    Brown, J.3    Shaub, A.4    Belkin, A.5    Burridge, K.6


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