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Volumn 90, Issue 2-3, 2011, Pages 261-269

Specificities of β1 integrin signaling in the control of cell adhesion and adhesive strength

Author keywords

Adhesion strength; Fibrillogenesis; Integrin activation

Indexed keywords

BETA1 INTEGRIN; GUANOSINE TRIPHOSPHATASE; RAP1 PROTEIN; TALIN; VERY LATE ACTIVATION ANTIGEN 5;

EID: 79151482019     PISSN: 01719335     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ejcb.2010.09.006     Document Type: Short Survey
Times cited : (15)

References (137)
  • 1
    • 33846246384 scopus 로고    scopus 로고
    • Force as a facilitator of integrin conformational changes during leukocyte arrest on blood vessels and antigen-presenting cells
    • Alon R., Dustin M.L. Force as a facilitator of integrin conformational changes during leukocyte arrest on blood vessels and antigen-presenting cells. Immunity 2007, 26:17-27.
    • (2007) Immunity , vol.26 , pp. 17-27
    • Alon, R.1    Dustin, M.L.2
  • 3
    • 77955413407 scopus 로고    scopus 로고
    • Transient frictional slip between integrin and the ECM in focal adhesions under myosin II tension
    • Aratyn-Schaus Y., Gardel M.L. Transient frictional slip between integrin and the ECM in focal adhesions under myosin II tension. Curr. Biol. 2010, 20:1145-1153.
    • (2010) Curr. Biol. , vol.20 , pp. 1145-1153
    • Aratyn-Schaus, Y.1    Gardel, M.L.2
  • 4
    • 23844457919 scopus 로고    scopus 로고
    • Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain
    • Arias-Salgado E.G., Lizano S., Shattil S.J., Ginsberg M.H. Specification of the direction of adhesive signaling by the integrin beta cytoplasmic domain. J. Biol. Chem. 2005, 280:29699-29707.
    • (2005) J. Biol. Chem. , vol.280 , pp. 29699-29707
    • Arias-Salgado, E.G.1    Lizano, S.2    Shattil, S.J.3    Ginsberg, M.H.4
  • 5
    • 33845566257 scopus 로고    scopus 로고
    • Importance of force linkage in mechanochemistry of adhesion receptors
    • Astrof N.S., Salas A., Shimaoka M., Chen J., Springer T.A. Importance of force linkage in mechanochemistry of adhesion receptors. Biochemistry 2006, 45:15020-15028.
    • (2006) Biochemistry , vol.45 , pp. 15020-15028
    • Astrof, N.S.1    Salas, A.2    Shimaoka, M.3    Chen, J.4    Springer, T.A.5
  • 7
    • 0037117522 scopus 로고    scopus 로고
    • Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension
    • Baneyx G., Baugh L., Vogel V. Fibronectin extension and unfolding within cell matrix fibrils controlled by cytoskeletal tension. Proc. Natl. Acad. Sci. U.S.A. 2002, 99:5139-5143.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 5139-5143
    • Baneyx, G.1    Baugh, L.2    Vogel, V.3
  • 9
    • 0029671374 scopus 로고    scopus 로고
    • Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells
    • Belkin A.M., Zhidkova N.I., Balzac F., Altruda F., Tomatis D., Maier A., Tarone G., Koteliansky V.E., Burridge K. Beta 1D integrin displaces the beta 1A isoform in striated muscles: localization at junctional structures and signaling potential in nonmuscle cells. J. Cell Biol. 1996, 132:211-226.
    • (1996) J. Cell Biol. , vol.132 , pp. 211-226
    • Belkin, A.M.1    Zhidkova, N.I.2    Balzac, F.3    Altruda, F.4    Tomatis, D.5    Maier, A.6    Tarone, G.7    Koteliansky, V.E.8    Burridge, K.9
  • 11
    • 70349335654 scopus 로고    scopus 로고
    • Control of cell adhesion dynamics by Rap1 signaling
    • Boettner B., Van Aelst L. Control of cell adhesion dynamics by Rap1 signaling. Curr. Opin. Cell Biol. 2009, 21:684-693.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 684-693
    • Boettner, B.1    Van Aelst, L.2
  • 12
    • 15044359236 scopus 로고    scopus 로고
    • Linking Rap to cell adhesion
    • Bos J.L. Linking Rap to cell adhesion. Curr. Opin. Cell Biol. 2005, 17:123-128.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 123-128
    • Bos, J.L.1
  • 13
    • 44449148944 scopus 로고    scopus 로고
    • The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins
    • Bouaouina M., Lad Y., Calderwood D.A. The N-terminal domains of talin cooperate with the phosphotyrosine binding-like domain to activate beta1 and beta3 integrins. J. Biol. Chem. 2008, 283:6118-6125.
    • (2008) J. Biol. Chem. , vol.283 , pp. 6118-6125
    • Bouaouina, M.1    Lad, Y.2    Calderwood, D.A.3
  • 15
    • 0032501044 scopus 로고    scopus 로고
    • Calcium/calmodulin-dependent protein kinase II controls integrin alpha5beta1-mediated cell adhesion through the integrin cytoplasmic domain associated protein-1alpha
    • Bouvard D., Block M.R. Calcium/calmodulin-dependent protein kinase II controls integrin alpha5beta1-mediated cell adhesion through the integrin cytoplasmic domain associated protein-1alpha. Biochem. Biophys. Res. Commun. 1998, 252:46-50.
    • (1998) Biochem. Biophys. Res. Commun. , vol.252 , pp. 46-50
    • Bouvard, D.1    Block, M.R.2
  • 18
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood D.A. Integrin activation. J. Cell Sci. 2004, 117:657-666.
    • (2004) J. Cell Sci. , vol.117 , pp. 657-666
    • Calderwood, D.A.1
  • 19
    • 3042609771 scopus 로고    scopus 로고
    • Talin controls integrin activation
    • Calderwood D.A. Talin controls integrin activation. Biochem. Soc. Trans. 2004, 32:434-437.
    • (2004) Biochem. Soc. Trans. , vol.32 , pp. 434-437
    • Calderwood, D.A.1
  • 21
    • 3142706142 scopus 로고    scopus 로고
    • Competition for talin results in trans-dominant inhibition of integrin activation
    • Calderwood D.A., Tai V., Di Paolo G., De Camilli P., Ginsberg M.H. Competition for talin results in trans-dominant inhibition of integrin activation. J. Biol. Chem. 2004, 279:28889-28895.
    • (2004) J. Biol. Chem. , vol.279 , pp. 28889-28895
    • Calderwood, D.A.1    Tai, V.2    Di Paolo, G.3    De Camilli, P.4    Ginsberg, M.H.5
  • 23
    • 0030924021 scopus 로고    scopus 로고
    • ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin
    • Chang D.D., Wong C., Smith H., Liu J. ICAP-1, a novel beta1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin. J. Cell Biol. 1997, 138:1149-1157.
    • (1997) J. Cell Biol. , vol.138 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 25
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet D., Felsenfeld D.P., Sheetz M.P. Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 1997, 88:39-48.
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 26
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka M., Burridge K. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 1996, 133:1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 29
    • 27544442354 scopus 로고    scopus 로고
    • The mechanisms and dynamics of (alpha)v(beta)3 integrin clustering in living cells
    • Cluzel C., Saltel F., Lussi J., Paulhe F., Imhof B.A., Wehrle-Haller B. The mechanisms and dynamics of (alpha)v(beta)3 integrin clustering in living cells. J. Cell Biol. 2005, 171:383-392.
    • (2005) J. Cell Biol. , vol.171 , pp. 383-392
    • Cluzel, C.1    Saltel, F.2    Lussi, J.3    Paulhe, F.4    Imhof, B.A.5    Wehrle-Haller, B.6
  • 31
    • 1342333140 scopus 로고    scopus 로고
    • Integrins in regulation of tissue development and function
    • Danen E.H., Sonnenberg A. Integrins in regulation of tissue development and function. J. Pathol. 2003, 201:632-641.
    • (2003) J. Pathol. , vol.201 , pp. 632-641
    • Danen, E.H.1    Sonnenberg, A.2
  • 32
    • 0037164867 scopus 로고    scopus 로고
    • The fibronectin-binding integrins alpha5beta1 and alphavbeta3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis
    • Danen E.H., Sonneveld P., Brakebusch C., Fassler R., Sonnenberg A. The fibronectin-binding integrins alpha5beta1 and alphavbeta3 differentially modulate RhoA-GTP loading, organization of cell matrix adhesions, and fibronectin fibrillogenesis. J. Cell Biol. 2002, 159:1071-1086.
    • (2002) J. Cell Biol. , vol.159 , pp. 1071-1086
    • Danen, E.H.1    Sonneveld, P.2    Brakebusch, C.3    Fassler, R.4    Sonnenberg, A.5
  • 34
  • 35
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher D.E., Janmey P., Wang Y.L. Tissue cells feel and respond to the stiffness of their substrate. Science 2005, 310:1139-1143.
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.L.3
  • 36
    • 33747152561 scopus 로고    scopus 로고
    • Matrix elasticity directs stem cell lineage specification
    • Engler A.J., Sen S., Sweeney H.L., Discher D.E. Matrix elasticity directs stem cell lineage specification. Cell 2006, 126:677-689.
    • (2006) Cell , vol.126 , pp. 677-689
    • Engler, A.J.1    Sen, S.2    Sweeney, H.L.3    Discher, D.E.4
  • 37
    • 0033175564 scopus 로고    scopus 로고
    • Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase Src
    • Felsenfeld D.P., Schwartzberg P.L., Venegas A., Tse R., Sheetz M.P. Selective regulation of integrin-cytoskeleton interactions by the tyrosine kinase Src. Nat. Cell Biol. 1999, 1:200-206.
    • (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
  • 38
    • 67349161798 scopus 로고    scopus 로고
    • Regulation of fibronectin matrix assembly and capillary morphogenesis in endothelial cells by Rho family GTPases
    • Fernandez-Sauze S., Grall D., Cseh B., Van Obberghen-Schilling E. Regulation of fibronectin matrix assembly and capillary morphogenesis in endothelial cells by Rho family GTPases. Exp. Cell Res. 2009, 315:2092-2104.
    • (2009) Exp. Cell Res. , vol.315 , pp. 2092-2104
    • Fernandez-Sauze, S.1    Grall, D.2    Cseh, B.3    Van Obberghen-Schilling, E.4
  • 39
    • 0037036371 scopus 로고    scopus 로고
    • Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement
    • Fournier H.N., Dupe-Manet S., Bouvard D., Lacombe M.L., Marie C., Block M.R., Albiges-Rizo C. Integrin cytoplasmic domain-associated protein 1alpha (ICAP-1alpha) interacts directly with the metastasis suppressor nm23-H2, and both proteins are targeted to newly formed cell adhesion sites upon integrin engagement. J. Biol. Chem. 2002, 277:20895-20902.
    • (2002) J. Biol. Chem. , vol.277 , pp. 20895-20902
    • Fournier, H.N.1    Dupe-Manet, S.2    Bouvard, D.3    Lacombe, M.L.4    Marie, C.5    Block, M.R.6    Albiges-Rizo, C.7
  • 40
    • 59149097344 scopus 로고    scopus 로고
    • Mechanically activated integrin switch controls alpha5beta1 function
    • Friedland J.C., Lee M.H., Boettiger D. Mechanically activated integrin switch controls alpha5beta1 function. Science 2009, 323:642-644.
    • (2009) Science , vol.323 , pp. 642-644
    • Friedland, J.C.1    Lee, M.H.2    Boettiger, D.3
  • 41
    • 36749013537 scopus 로고    scopus 로고
    • Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells
    • Gaggioli C., Hooper S., Hidalgo-Carcedo C., Grosse R., Marshall J.F., Harrington K., Sahai E. Fibroblast-led collective invasion of carcinoma cells with differing roles for RhoGTPases in leading and following cells. Nat. Cell Biol. 2007, 9:1392-1400.
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1392-1400
    • Gaggioli, C.1    Hooper, S.2    Hidalgo-Carcedo, C.3    Grosse, R.4    Marshall, J.F.5    Harrington, K.6    Sahai, E.7
  • 42
    • 0030829357 scopus 로고    scopus 로고
    • A micromachined device provides a new bend on fibroblast traction forces
    • Galbraith C.G., Sheetz M.P. A micromachined device provides a new bend on fibroblast traction forces. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:9114-9118.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 9114-9118
    • Galbraith, C.G.1    Sheetz, M.P.2
  • 43
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith C.G., Yamada K.M., Sheetz M.P. The relationship between force and focal complex development. J. Cell Biol. 2002, 159:695-705.
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 44
    • 24344434553 scopus 로고    scopus 로고
    • Cell adhesion strengthening: contributions of adhesive area, integrin binding, and focal adhesion assembly
    • Gallant N.D., Michael K.E., Garcia A.J. Cell adhesion strengthening: contributions of adhesive area, integrin binding, and focal adhesion assembly. Mol. Biol. Cell 2005, 16:4329-4340.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4329-4340
    • Gallant, N.D.1    Michael, K.E.2    Garcia, A.J.3
  • 48
    • 0242361579 scopus 로고    scopus 로고
    • Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation
    • Giannone G., Jiang G., Sutton D.H., Critchley D.R., Sheetz M.P. Talin1 is critical for force-dependent reinforcement of initial integrin-cytoskeleton bonds but not tyrosine kinase activation. J. Cell Biol. 2003, 163:409-419.
    • (2003) J. Cell Biol. , vol.163 , pp. 409-419
    • Giannone, G.1    Jiang, G.2    Sutton, D.H.3    Critchley, D.R.4    Sheetz, M.P.5
  • 49
    • 69549110995 scopus 로고    scopus 로고
    • Multi-level molecular clutches in motile cell processes
    • Giannone G., Mege R.M., Thoumine O. Multi-level molecular clutches in motile cell processes. Trends Cell Biol. 2009, 19:475-486.
    • (2009) Trends Cell Biol. , vol.19 , pp. 475-486
    • Giannone, G.1    Mege, R.M.2    Thoumine, O.3
  • 54
    • 66449119343 scopus 로고    scopus 로고
    • Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects
    • Harburger D.S., Bouaouina M., Calderwood D.A. Kindlin-1 and -2 directly bind the C-terminal region of beta integrin cytoplasmic tails and exert integrin-specific activation effects. J. Biol. Chem. 2009, 284:11485-11497.
    • (2009) J. Biol. Chem. , vol.284 , pp. 11485-11497
    • Harburger, D.S.1    Bouaouina, M.2    Calderwood, D.A.3
  • 56
    • 50249117119 scopus 로고    scopus 로고
    • Binding of soluble fibronectin to integrin alpha5 beta1 - link to focal adhesion redistribution and contractile shape
    • Huveneers S., Truong H., Fassler R., Sonnenberg A., Danen E.H. Binding of soluble fibronectin to integrin alpha5 beta1 - link to focal adhesion redistribution and contractile shape. J. Cell Sci. 2008, 121:2452-2462.
    • (2008) J. Cell Sci. , vol.121 , pp. 2452-2462
    • Huveneers, S.1    Truong, H.2    Fassler, R.3    Sonnenberg, A.4    Danen, E.H.5
  • 57
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: bidirectional, allosteric signaling machines
    • Hynes R.O. Integrins: bidirectional, allosteric signaling machines. Cell 2002, 110:673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 58
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: not just pretty fibrils
    • Hynes R.O. The extracellular matrix: not just pretty fibrils. Science 2009, 326:1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 60
    • 33646155963 scopus 로고    scopus 로고
    • Rigidity sensing at the leading edge through alphavbeta3 integrins and RPTPalpha
    • Jiang G., Huang A.H., Cai Y., Tanase M., Sheetz M.P. Rigidity sensing at the leading edge through alphavbeta3 integrins and RPTPalpha. Biophys. J. 2006, 90:1804-1809.
    • (2006) Biophys. J. , vol.90 , pp. 1804-1809
    • Jiang, G.1    Huang, A.H.2    Cai, Y.3    Tanase, M.4    Sheetz, M.P.5
  • 63
    • 1342346591 scopus 로고    scopus 로고
    • The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion
    • Kloeker S., Major M.B., Calderwood D.A., Ginsberg M.H., Jones D.A., Beckerle M.C. The Kindler syndrome protein is regulated by transforming growth factor-beta and involved in integrin-mediated adhesion. J. Biol. Chem. 2004, 279:6824-6833.
    • (2004) J. Biol. Chem. , vol.279 , pp. 6824-6833
    • Kloeker, S.1    Major, M.B.2    Calderwood, D.A.3    Ginsberg, M.H.4    Jones, D.A.5    Beckerle, M.C.6
  • 64
    • 67649598285 scopus 로고    scopus 로고
    • Demonstration of catch bonds between an integrin and its ligand
    • Kong F., Garcia A.J., Mould A.P., Humphries M.J., Zhu C. Demonstration of catch bonds between an integrin and its ligand. J. Cell Biol. 2009, 185:1275-1284.
    • (2009) J. Cell Biol. , vol.185 , pp. 1275-1284
    • Kong, F.1    Garcia, A.J.2    Mould, A.P.3    Humphries, M.J.4    Zhu, C.5
  • 67
    • 65649127175 scopus 로고    scopus 로고
    • The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling
    • Lau T.L., Kim C., Ginsberg M.H., Ulmer T.S. The structure of the integrin alphaIIbbeta3 transmembrane complex explains integrin transmembrane signalling. EMBO J. 2009, 28:1351-1361.
    • (2009) EMBO J. , vol.28 , pp. 1351-1361
    • Lau, T.L.1    Kim, C.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 68
    • 41449108071 scopus 로고    scopus 로고
    • Structure of the integrin beta3 transmembrane segment in phospholipid bicelles and detergent micelles
    • Lau T.L., Partridge A.W., Ginsberg M.H., Ulmer T.S. Structure of the integrin beta3 transmembrane segment in phospholipid bicelles and detergent micelles. Biochemistry 2008, 47:4008-4016.
    • (2008) Biochemistry , vol.47 , pp. 4008-4016
    • Lau, T.L.1    Partridge, A.W.2    Ginsberg, M.H.3    Ulmer, T.S.4
  • 69
    • 0030050396 scopus 로고    scopus 로고
    • 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region
    • Leahy D.J., Aukhil I., Erickson H.P. 2.0 A crystal structure of a four-domain segment of human fibronectin encompassing the RGD loop and synergy region. Cell 1996, 84:155-164.
    • (1996) Cell , vol.84 , pp. 155-164
    • Leahy, D.J.1    Aukhil, I.2    Erickson, H.P.3
  • 71
    • 58849162755 scopus 로고    scopus 로고
    • Cell traction forces direct fibronectin matrix assembly
    • Lemmon C.A., Chen C.S., Romer L.H. Cell traction forces direct fibronectin matrix assembly. Biophys. J. 2009, 96:729-738.
    • (2009) Biophys. J. , vol.96 , pp. 729-738
    • Lemmon, C.A.1    Chen, C.S.2    Romer, L.H.3
  • 73
    • 33846010146 scopus 로고    scopus 로고
    • The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1
    • Liao Y.C., Si L., deVere White R.W., Lo S.H. The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1. J. Cell Biol. 2007, 176:43-49.
    • (2007) J. Cell Biol. , vol.176 , pp. 43-49
    • Liao, Y.C.1    Si, L.2    deVere White, R.W.3    Lo, S.H.4
  • 75
    • 13544270759 scopus 로고    scopus 로고
    • DOK1 mediates SHP-2 binding to the alphaVbeta3 integrin and thereby regulates insulin-like growth factor I signaling in cultured vascular smooth muscle cells
    • Ling Y., Maile L.A., Badley-Clarke J., Clemmons D.R. DOK1 mediates SHP-2 binding to the alphaVbeta3 integrin and thereby regulates insulin-like growth factor I signaling in cultured vascular smooth muscle cells. J. Biol. Chem. 2005, 280:3151-3158.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3151-3158
    • Ling, Y.1    Maile, L.A.2    Badley-Clarke, J.3    Clemmons, D.R.4
  • 76
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo B.H., Carman C.V., Springer T.A. Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 2007, 25:619-647.
    • (2007) Annu. Rev. Immunol. , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 77
    • 16644396938 scopus 로고    scopus 로고
    • A specific interface between integrin transmembrane helices and affinity for ligand
    • Luo B.H., Springer T.A., Takagi J. A specific interface between integrin transmembrane helices and affinity for ligand. PLoS Biol. 2004, 2:e153.
    • (2004) PLoS Biol. , vol.2
    • Luo, B.H.1    Springer, T.A.2    Takagi, J.3
  • 78
    • 43149085289 scopus 로고    scopus 로고
    • Kindlin-2 (Mig-2): a co-activator of beta3 integrins
    • Ma Y.Q., Qin J., Wu C., Plow E.F. Kindlin-2 (Mig-2): a co-activator of beta3 integrins. J. Cell Biol. 2008, 181:439-446.
    • (2008) J. Cell Biol. , vol.181 , pp. 439-446
    • Ma, Y.Q.1    Qin, J.2    Wu, C.3    Plow, E.F.4
  • 79
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon A.C., Qadota H., Norman K.R., Moerman D.G., Williams B.D. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr. Biol. 2002, 12:787-797.
    • (2002) Curr. Biol. , vol.12 , pp. 787-797
    • Mackinnon, A.C.1    Qadota, H.2    Norman, K.R.3    Moerman, D.G.4    Williams, B.D.5
  • 80
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao Y., Schwarzbauer J.E. Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol. 2005, 24:389-399.
    • (2005) Matrix Biol. , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 82
    • 34249821363 scopus 로고    scopus 로고
    • Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions
    • McCleverty C.J., Lin D.C., Liddington R.C. Structure of the PTB domain of tensin1 and a model for its recruitment to fibrillar adhesions. Protein Sci. 2007, 16:1223-1229.
    • (2007) Protein Sci. , vol.16 , pp. 1223-1229
    • McCleverty, C.J.1    Lin, D.C.2    Liddington, R.C.3
  • 83
    • 34548745249 scopus 로고    scopus 로고
    • A catch to integrin activation
    • McEver R.P., Zhu C. A catch to integrin activation. Nat. Immunol. 2007, 8:1035-1037.
    • (2007) Nat. Immunol. , vol.8 , pp. 1035-1037
    • McEver, R.P.1    Zhu, C.2
  • 84
    • 70349312643 scopus 로고    scopus 로고
    • The Kindlin protein family: new members to the club of focal adhesion proteins
    • Meves A., Stremmel C., Gottschalk K., Fassler R. The Kindlin protein family: new members to the club of focal adhesion proteins. Trends Cell Biol. 2009, 19:504-513.
    • (2009) Trends Cell Biol. , vol.19 , pp. 504-513
    • Meves, A.1    Stremmel, C.2    Gottschalk, K.3    Fassler, R.4
  • 85
    • 65649135420 scopus 로고    scopus 로고
    • Focal adhesion kinase modulates cell adhesion strengthening via integrin activation
    • Michael K.E., Dumbauld D.W., Burns K.L., Hanks S.K., Garcia A.J. Focal adhesion kinase modulates cell adhesion strengthening via integrin activation. Mol. Biol. Cell 2009, 20:2508-2519.
    • (2009) Mol. Biol. Cell , vol.20 , pp. 2508-2519
    • Michael, K.E.1    Dumbauld, D.W.2    Burns, K.L.3    Hanks, S.K.4    Garcia, A.J.5
  • 86
    • 38749147215 scopus 로고    scopus 로고
    • Cell adaptive response to extracellular matrix density is controlled by ICAP-1-dependent beta1-integrin affinity
    • Millon-Fremillon A., Bouvard D., Grichine A., Manet-Dupe S., Block M.R., Albiges-Rizo C. Cell adaptive response to extracellular matrix density is controlled by ICAP-1-dependent beta1-integrin affinity. J. Cell Biol. 2008, 180:427-441.
    • (2008) J. Cell Biol. , vol.180 , pp. 427-441
    • Millon-Fremillon, A.1    Bouvard, D.2    Grichine, A.3    Manet-Dupe, S.4    Block, M.R.5    Albiges-Rizo, C.6
  • 89
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M., Legate K.R., Zent R., Fassler R. The tail of integrins, talin, and kindlins. Science 2009, 324:895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fassler, R.4
  • 92
    • 77951189703 scopus 로고    scopus 로고
    • The NPIY motif in the integrin beta1 tail dictates the requirement for talin-1 in outside-in signaling
    • Nieves B., Jones C.W., Ward R., Ohta Y., Reverte C.G., LaFlamme S.E. The NPIY motif in the integrin beta1 tail dictates the requirement for talin-1 in outside-in signaling. J. Cell Sci. 2010, 123:1216-1226.
    • (2010) J. Cell Sci. , vol.123 , pp. 1216-1226
    • Nieves, B.1    Jones, C.W.2    Ward, R.3    Ohta, Y.4    Reverte, C.G.5    LaFlamme, S.E.6
  • 94
    • 41949131361 scopus 로고    scopus 로고
    • An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding
    • Oxley C.L., Anthis N.J., Lowe E.D., Vakonakis I., Campbell I.D., Wegener K.L. An integrin phosphorylation switch: the effect of beta3 integrin tail phosphorylation on Dok1 and talin binding. J. Biol. Chem. 2008, 283:5420-5426.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5420-5426
    • Oxley, C.L.1    Anthis, N.J.2    Lowe, E.D.3    Vakonakis, I.4    Campbell, I.D.5    Wegener, K.L.6
  • 95
    • 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., Cukierman E., Katz B.Z., Matsumoto K., Lin D.C., Lin S., Hahn C., Yamada K.M. Integrin dynamics and matrix assembly: tensin-dependent translocation of alpha(5)beta(1) integrins promotes early fibronectin fibrillogenesis. J. Cell Biol. 2000, 148:1075-1090.
    • (2000) J. Cell Biol. , vol.148 , pp. 1075-1090
    • Pankov, R.1    Cukierman, E.2    Katz, B.Z.3    Matsumoto, K.4    Lin, D.C.5    Lin, S.6    Hahn, C.7    Yamada, K.M.8
  • 98
    • 0344912596 scopus 로고    scopus 로고
    • Cell locomotion and focal adhesions are regulated by substrate flexibility
    • Pelham R.J., Wang Y. Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl. Acad. Sci. U.S.A. 1997, 94:13661-13665.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 13661-13665
    • Pelham, R.J.1    Wang, Y.2
  • 100
    • 66449105246 scopus 로고    scopus 로고
    • Specificity in Ras and Rap signaling
    • Raaijmakers J.H., Bos J.L. Specificity in Ras and Rap signaling. J. Biol. Chem. 2009, 284:10995-10999.
    • (2009) J. Biol. Chem. , vol.284 , pp. 10995-10999
    • Raaijmakers, J.H.1    Bos, J.L.2
  • 101
    • 0035844869 scopus 로고    scopus 로고
    • Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism
    • Riveline D., Zamir E., Balaban N.Q., Schwarz U.S., Ishizaki T., Narumiya S., Kam Z., Geiger B., Bershadsky A.D. Focal contacts as mechanosensors: externally applied local mechanical force induces growth of focal contacts by an mDia1-dependent and ROCK-independent mechanism. J. Cell Biol. 2001, 153:1175-1186.
    • (2001) J. Cell Biol. , vol.153 , pp. 1175-1186
    • Riveline, D.1    Zamir, E.2    Balaban, N.Q.3    Schwarz, U.S.4    Ishizaki, T.5    Narumiya, S.6    Kam, Z.7    Geiger, B.8    Bershadsky, A.D.9
  • 102
    • 70349496205 scopus 로고    scopus 로고
    • Clustering of alpha(5)beta(1) integrins determines adhesion strength whereas alpha(v)beta(3) and talin enable mechanotransduction
    • Roca-Cusachs P., Gauthier N.C., Del Rio A., Sheetz M.P. Clustering of alpha(5)beta(1) integrins determines adhesion strength whereas alpha(v)beta(3) and talin enable mechanotransduction. Proc. Natl. Acad. Sci. U.S.A. 2009, 106:16245-16250.
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 16245-16250
    • Roca-Cusachs, P.1    Gauthier, N.C.2    Del Rio, A.3    Sheetz, M.P.4
  • 103
    • 0037128202 scopus 로고    scopus 로고
    • Force transduction by Triton cytoskeletons
    • Sawada Y., Sheetz M.P. Force transduction by Triton cytoskeletons. J. Cell Biol. 2002, 156:609-615.
    • (2002) J. Cell Biol. , vol.156 , pp. 609-615
    • Sawada, Y.1    Sheetz, M.P.2
  • 104
    • 50849083158 scopus 로고    scopus 로고
    • Cell adhesion receptors in mechanotransduction
    • Schwartz M.A., DeSimone D.W. Cell adhesion receptors in mechanotransduction. Curr. Opin. Cell Biol. 2008, 20:551-556.
    • (2008) Curr. Opin. Cell Biol. , vol.20 , pp. 551-556
    • Schwartz, M.A.1    DeSimone, D.W.2
  • 105
    • 0030659845 scopus 로고    scopus 로고
    • Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly
    • Sechler J.L., Corbett S.A., Schwarzbauer J.E. Modulatory roles for integrin activation and the synergy site of fibronectin during matrix assembly. Mol. Biol. Cell 1997, 8:2563-2573.
    • (1997) Mol. Biol. Cell , vol.8 , pp. 2563-2573
    • Sechler, J.L.1    Corbett, S.A.2    Schwarzbauer, J.E.3
  • 108
    • 69449100887 scopus 로고    scopus 로고
    • Molecular dissection of the ILK-PINCH-parvin triad reveals a fundamental role for the ILK kinase domain in the late stages of focal-adhesion maturation
    • Stanchi F., Grashoff C., Nguemeni Yonga C.F., Grall D., Fassler R., Van Obberghen-Schilling E. Molecular dissection of the ILK-PINCH-parvin triad reveals a fundamental role for the ILK kinase domain in the late stages of focal-adhesion maturation. J. Cell Sci. 2009, 122:1800-1811.
    • (2009) J. Cell Sci. , vol.122 , pp. 1800-1811
    • Stanchi, F.1    Grashoff, C.2    Nguemeni Yonga, C.F.3    Grall, D.4    Fassler, R.5    Van Obberghen-Schilling, E.6
  • 110
    • 0036697001 scopus 로고    scopus 로고
    • Integrin activation and structural rearrangement
    • Takagi J., Springer T.A. Integrin activation and structural rearrangement. Immunol. Rev. 2002, 186:141-163.
    • (2002) Immunol. Rev. , vol.186 , pp. 141-163
    • Takagi, J.1    Springer, T.A.2
  • 111
    • 0141625303 scopus 로고    scopus 로고
    • Structure of integrin alpha5beta1 in complex with fibronectin
    • Takagi J., Strokovich K., Springer T.A., Walz T. Structure of integrin alpha5beta1 in complex with fibronectin. EMBO J. 2003, 22:4607-4615.
    • (2003) EMBO J. , vol.22 , pp. 4607-4615
    • Takagi, J.1    Strokovich, K.2    Springer, T.A.3    Walz, T.4
  • 113
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • Tu Y., Wu S., Shi X., Chen K., Wu C. Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 2003, 113:37-47.
    • (2003) Cell , vol.113 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 116
    • 0037437150 scopus 로고    scopus 로고
    • RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages
    • von Wichert G., Jiang G., Kostic A., De Vos K., Sap J., Sheetz M.P. RPTP-alpha acts as a transducer of mechanical force on alphav/beta3-integrin-cytoskeleton linkages. J. Cell Biol. 2003, 161:143-153.
    • (2003) J. Cell Biol. , vol.161 , pp. 143-153
    • von Wichert, G.1    Jiang, G.2    Kostic, A.3    De Vos, K.4    Sap, J.5    Sheetz, M.P.6
  • 117
    • 0027172919 scopus 로고
    • Mechanotransduction across the cell surface and through the cytoskeleton
    • Wang N., Butler J.P., Ingber D.E. Mechanotransduction across the cell surface and through the cytoskeleton. Science 1993, 260:1124-1127.
    • (1993) Science , vol.260 , pp. 1124-1127
    • Wang, N.1    Butler, J.P.2    Ingber, D.E.3
  • 120
    • 52449095904 scopus 로고    scopus 로고
    • Heat stress activates AKT via focal adhesion kinase-mediated pathway in neonatal rat ventricular myocytes
    • Wei H., Vander Heide R.S. Heat stress activates AKT via focal adhesion kinase-mediated pathway in neonatal rat ventricular myocytes. Am. J. Physiol. Heart Circ. Physiol. 2008, 295:H561-H568.
    • (2008) Am. J. Physiol. Heart Circ. Physiol. , vol.295
    • Wei, H.1    Vander Heide, R.S.2
  • 123
    • 34248226275 scopus 로고    scopus 로고
    • Alpha v beta3 and alpha5beta1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration
    • White D.P., Caswell P.T., Norman J.C. alpha v beta3 and alpha5beta1 integrin recycling pathways dictate downstream Rho kinase signaling to regulate persistent cell migration. J. Cell Biol. 2007, 177:515-525.
    • (2007) J. Cell Biol. , vol.177 , pp. 515-525
    • White, D.P.1    Caswell, P.T.2    Norman, J.C.3
  • 124
    • 44849142138 scopus 로고    scopus 로고
    • Fibronectin expression modulates mammary epithelial cell proliferation during acinar differentiation
    • Williams C.M., Engler A.J., Slone R.D., Galante L.L., Schwarzbauer J.E. Fibronectin expression modulates mammary epithelial cell proliferation during acinar differentiation. Cancer Res. 2008, 68:3185-3192.
    • (2008) Cancer Res. , vol.68 , pp. 3185-3192
    • Williams, C.M.1    Engler, A.J.2    Slone, R.D.3    Galante, L.L.4    Schwarzbauer, J.E.5
  • 125
    • 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., Hughes P.E., Ginsberg M.H., McDonald J.A. Identification of a new biological function for the integrin alpha v beta 3: initiation of fibronectin matrix assembly. Cell Adhes. Commun. 1996, 4:149-158.
    • (1996) Cell Adhes. Commun. , vol.4 , pp. 149-158
    • Wu, C.1    Hughes, P.E.2    Ginsberg, M.H.3    McDonald, J.A.4
  • 127
    • 33748994597 scopus 로고    scopus 로고
    • Interaction of deleted in liver cancer 1 with tensin2 in caveolae and implications in tumor suppression
    • Yam J.W., Ko F.C., Chan C.Y., Jin D.Y., Ng I.O. Interaction of deleted in liver cancer 1 with tensin2 in caveolae and implications in tumor suppression. Cancer Res. 2006, 66:8367-8372.
    • (2006) Cancer Res. , vol.66 , pp. 8367-8372
    • Yam, J.W.1    Ko, F.C.2    Chan, C.Y.3    Jin, D.Y.4    Ng, I.O.5
  • 128
    • 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.T., Hynes R.O. Fibronectin receptor functions in embryonic cells deficient in alpha 5 beta 1 integrin can be replaced by alpha V integrins. Mol. Biol. Cell 1996, 7:1737-1748.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1737-1748
    • Yang, J.T.1    Hynes, R.O.2
  • 131
  • 132
    • 0032590074 scopus 로고    scopus 로고
    • Interaction of the integrin beta1 cytoplasmic domain with ICAP-1 protein
    • Zhang X.A., Hemler M.E. Interaction of the integrin beta1 cytoplasmic domain with ICAP-1 protein. J. Biol. Chem. 1999, 274:11-19.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11-19
    • Zhang, X.A.1    Hemler, M.E.2
  • 133
    • 0032550177 scopus 로고    scopus 로고
    • Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly
    • Zhong C., Chrzanowska-Wodnicka M., Brown J., Shaub A., Belkin A.M., Burridge K. Rho-mediated contractility exposes a cryptic site in fibronectin and induces fibronectin matrix assembly. J. Cell Biol. 1998, 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.M.5    Burridge, K.6
  • 134
    • 33644650666 scopus 로고    scopus 로고
    • Catch bonds: physical models, structural bases, biological function and rheological relevance
    • Zhu C., Lou J., McEver R.P. Catch bonds: physical models, structural bases, biological function and rheological relevance. Biorheology 2005, 42:443-462.
    • (2005) Biorheology , vol.42 , pp. 443-462
    • Zhu, C.1    Lou, J.2    McEver, R.P.3
  • 135
    • 33744487644 scopus 로고    scopus 로고
    • Catch bonds: physical models and biological functions
    • Zhu C., McEver R.P. Catch bonds: physical models and biological functions. Mol. Cell Biomech. 2005, 2:91-104.
    • (2005) Mol. Cell Biomech. , vol.2 , pp. 91-104
    • Zhu, C.1    McEver, R.P.2
  • 136
    • 64749101260 scopus 로고    scopus 로고
    • The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3
    • Zhu J., Luo B.H., Barth P., Schonbrun J., Baker D., Springer T.A. The structure of a receptor with two associating transmembrane domains on the cell surface: integrin alphaIIbbeta3. Mol. Cell 2009, 34:234-249.
    • (2009) Mol. Cell , vol.34 , pp. 234-249
    • Zhu, J.1    Luo, B.H.2    Barth, P.3    Schonbrun, J.4    Baker, D.5    Springer, T.A.6


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