메뉴 건너뛰기




Volumn 6, Issue , 2016, Pages

Substrate engagement of integrins α5 β1 and αv β3 is necessary, but not sufficient, for high directional persistence in migration on fibronectin

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; MOLECULAR LIBRARY; VERY LATE ACTIVATION ANTIGEN 5; VITRONECTIN RECEPTOR;

EID: 84962515390     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep23258     Document Type: Article
Times cited : (49)

References (110)
  • 1
    • 77956064817 scopus 로고    scopus 로고
    • Cell adhesion: Integrating cytoskeletal dynamics and cellular tension
    • Parsons, J. T., Horwitz, A. R., Schwartz, M. A. Cell adhesion: integrating cytoskeletal dynamics and cellular tension. Nat. Rev. Mol. Cell Biol. 11, 633-643 (2010).
    • (2010) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 633-643
    • Parsons, J.T.1    Horwitz, A.R.2    Schwartz, M.A.3
  • 2
    • 0344305784 scopus 로고    scopus 로고
    • Cell migration: Integrating signals from front to back
    • Ridley, A. J. et al. Cell migration: integrating signals from front to back. Science 302, 1704-1709 (2003).
    • (2003) Science , vol.302 , pp. 1704-1709
    • Ridley, A.J.1
  • 3
    • 84855208997 scopus 로고    scopus 로고
    • Bio-inspired materials for parsing matrix physicochemical control of cell migration: A Review
    • Kim, H.-D., Peyton, S. R. Bio-inspired materials for parsing matrix physicochemical control of cell migration: A Review. Integr. Biol. 4, 37-52 (2012).
    • (2012) Integr. Biol. , vol.4 , pp. 37-52
    • Kim, H.-D.1    Peyton, S.R.2
  • 6
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687 (2002).
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 7
    • 78649867535 scopus 로고    scopus 로고
    • Unique and redundant functions of integrins in the epidermis
    • Margadant, C., Charafeddine, R. A., Sonnenberg, A. Unique and redundant functions of integrins in the epidermis. FASEB J. 24, 4133-4152 (2010).
    • (2010) FASEB J. , vol.24 , pp. 4133-4152
    • Margadant, C.1    Charafeddine, R.A.2    Sonnenberg, A.3
  • 8
    • 72949119124 scopus 로고    scopus 로고
    • Integrins in cancer: Biological implications and therapeutic opportunities
    • Desgrosellier, J. S., Cheresh, D. A. Integrins in cancer: biological implications and therapeutic opportunities. Nat. Rev. Cancer 10, 9-22 (2010).
    • (2010) Nat. Rev. Cancer , vol.10 , pp. 9-22
    • Desgrosellier, J.S.1    Cheresh, D.A.2
  • 9
    • 33748637333 scopus 로고    scopus 로고
    • Integrin signalling in directed cell migration
    • Moissoglu, K., Schwartz, M. A. Integrin signalling in directed cell migration. Biol. Cell 98, 547-555 (2006).
    • (2006) Biol. Cell , vol.98 , pp. 547-555
    • Moissoglu, K.1    Schwartz, M.A.2
  • 10
  • 11
    • 69249235440 scopus 로고    scopus 로고
    • Giving off mixed signals-distinct functions of alpha5beta1 and alphavbeta3 integrins in regulating cell behaviour
    • Morgan, M. R., Byron, A., Humphries, M. J., Bass, M. D. Giving off mixed signals-distinct functions of alpha5beta1 and alphavbeta3 integrins in regulating cell behaviour. IUBMB Life 61, 731-738 (2009).
    • (2009) IUBMB Life , vol.61 , pp. 731-738
    • Morgan, M.R.1    Byron, A.2    Humphries, M.J.3    Bass, M.D.4
  • 12
    • 18844424325 scopus 로고    scopus 로고
    • Integrins control motile strategy through a Rho-cofilin pathway
    • Danen, E. H. J. et al. Integrins control motile strategy through a Rho-cofilin pathway. J. Cell Biol. 169, 515-526 (2005).
    • (2005) J. Cell Biol. , vol.169 , pp. 515-526
    • Danen, E.H.J.1
  • 13
    • 84878598076 scopus 로고    scopus 로고
    • 1-and ?v-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments
    • Schiller, H. B. et al. ?1-and ?v-class integrins cooperate to regulate myosin II during rigidity sensing of fibronectin-based microenvironments. Nat. Cell Biol. 15, 625-636 (2013).
    • (2013) Nat. Cell Biol. , vol.15 , pp. 625-636
    • Schiller, H.B.1
  • 14
    • 84934275754 scopus 로고    scopus 로고
    • Segregation versus colocalization: Orthogonally functionalized binary micropatterned substrates regulate the molecular distribution in focal adhesions
    • Guasch, J. et al. Segregation versus colocalization: orthogonally functionalized binary micropatterned substrates regulate the molecular distribution in focal adhesions. Adv. Mater. 27, 3737-3747 (2015).
    • (2015) Adv. Mater. , vol.27 , pp. 3737-3747
    • Guasch, J.1
  • 15
    • 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. J., 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. 159, 1071-1086 (2002).
    • (2002) J. Cell Biol. , vol.159 , pp. 1071-1086
    • Danen, E.H.J.1    Sonneveld, P.2    Brakebusch, C.3    Fassler, R.4    Sonnenberg, A.5
  • 16
    • 0040106980 scopus 로고
    • The distribution of distinct integrins in focal contacts is determined by the substratum composition
    • Fath, K. R., Edgell, C. J., Burridge, K. The distribution of distinct integrins in focal contacts is determined by the substratum composition. J. Cell Sci. 92 (Pt 1), 67-75 (1989).
    • (1989) J. Cell Sci. , vol.92 , pp. 67-75
    • Fath, K.R.1    Edgell, C.J.2    Burridge, K.3
  • 17
    • 0024074965 scopus 로고
    • Fibronectin and vitronectin regulate the organization of their respective Arg-Gly-Asp adhesion receptors in cultured human endothelial cells
    • Dejana, E. et al. Fibronectin and vitronectin regulate the organization of their respective Arg-Gly-Asp adhesion receptors in cultured human endothelial cells. J. Cell Biol. 107, 1215-1223 (1988).
    • (1988) J. Cell Biol. , vol.107 , pp. 1215-1223
    • Dejana, E.1
  • 18
    • 0024440425 scopus 로고
    • A Comparison of the Biological-Activities of the Cell-Adhesive Proteins Vitronectin and Fibronectin
    • Underwood, P. A., Bennett, F. A. A Comparison of the Biological-Activities of the Cell-Adhesive Proteins Vitronectin and Fibronectin. J. Cell Sci. 93, 641-649 (1989).
    • (1989) J. Cell Sci. , vol.93 , pp. 641-649
    • Underwood, P.A.1    Bennett, F.A.2
  • 19
    • 0026501109 scopus 로고
    • Motility of fibronectin receptor-deficient cells on fibronectin and vitronectin: Collaborative interactions among integrins
    • Bauer, J. S., Schreiner, C. L., Giancotti, F. G., Ruoslahti, E., Juliano, R. L. Motility of fibronectin receptor-deficient cells on fibronectin and vitronectin: collaborative interactions among integrins. J. Cell Biol. 116, 477-487 (1992).
    • (1992) J. Cell Biol. , vol.116 , pp. 477-487
    • Bauer, J.S.1    Schreiner, C.L.2    Giancotti, F.G.3    Ruoslahti, E.4    Juliano, R.L.5
  • 20
    • 84883272113 scopus 로고    scopus 로고
    • Syndecan-4 signaling at a glance
    • Elfenbein, A., Simons, M. Syndecan-4 signaling at a glance. J. Cell Sci. 126, 3799-3804 (2013).
    • (2013) J. Cell Sci. , vol.126 , pp. 3799-3804
    • Elfenbein, A.1    Simons, M.2
  • 21
    • 84922246831 scopus 로고    scopus 로고
    • The interaction between uPAR and vitronectin triggers ligand-independent adhesion signalling by integrins
    • Ferraris, G. M. S. et al. The interaction between uPAR and vitronectin triggers ligand-independent adhesion signalling by integrins. EMBO J. doi: 10.15252/embj.201387611 (2014).
    • (2014) EMBO J
    • Ferraris, G.M.S.1
  • 22
    • 0032935413 scopus 로고    scopus 로고
    • Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation
    • Garcia, A. J., Vega, M. D., Boettiger, D. Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation. Mol. Biol. Cell 10, 785-798 (1999).
    • (1999) Mol. Biol. Cell , vol.10 , pp. 785-798
    • Garcia, A.J.1    Vega, M.D.2    Boettiger, D.3
  • 23
    • 0027624239 scopus 로고
    • Polystyrene chemistry affects vitronectin activity: An explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene
    • Steele, J. G., Dalton, B. A., Johnson, G., Underwood, P. A. Polystyrene chemistry affects vitronectin activity: an explanation for cell attachment to tissue culture polystyrene but not to unmodified polystyrene. J. Biomed. Mater. Res. 27, 927-940 (1993).
    • (1993) J. Biomed. Mater. Res. , vol.27 , pp. 927-940
    • Steele, J.G.1    Dalton, B.A.2    Johnson, G.3    Underwood, P.A.4
  • 24
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • Palecek, S. P., Loftus, J. C., Ginsberg, M. H., Lauffenburger, D. A., Horwitz, A. F. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature 385, 537-540 (1997).
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 25
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton, S. L., Waterman-Storer, C. M. Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 125, 1361-1374 (2006).
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 26
    • 84856134600 scopus 로고    scopus 로고
    • Fibroblast polarization is a matrix-rigidity-dependent process controlled by focal adhesion mechanosensing
    • Prager-Khoutorsky, M. et al. Fibroblast polarization is a matrix-rigidity-dependent process controlled by focal adhesion mechanosensing. Nat. Cell Biol. 13, 1457-1465 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 1457-1465
    • Prager-Khoutorsky, M.1
  • 27
    • 77953130411 scopus 로고    scopus 로고
    • Optimal matrix rigidity for stress fiber polarization in stem cells
    • Zemel, A., Rehfeldt, F., Brown, A. E. X., Discher, D. E., Safran, S. A. Optimal matrix rigidity for stress fiber polarization in stem cells. Nat. Phys. 6, 468-473 (2010).
    • (2010) Nat. Phys. , vol.6 , pp. 468-473
    • Zemel, A.1    Rehfeldt, F.2    Brown, A.E.X.3    Discher, D.E.4    Safran, S.A.5
  • 28
    • 51049104617 scopus 로고    scopus 로고
    • Actin and ?-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motorindependent manner
    • Choi, C. K. et al. Actin and ?-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motorindependent manner. Nat. Cell Biol. 10, 1039-1050 (2008).
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1
  • 29
    • 3042723613 scopus 로고    scopus 로고
    • Early molecular events in the assembly of the focal adhesion-stress fiber complex during fibroblast spreading
    • Zimerman, B., Volberg, T., Geiger, B. Early molecular events in the assembly of the focal adhesion-stress fiber complex during fibroblast spreading. Cell Motil. Cytoskeleton 58, 143-159 (2004).
    • (2004) Cell Motil. Cytoskeleton , vol.58 , pp. 143-159
    • Zimerman, B.1    Volberg, T.2    Geiger, B.3
  • 30
    • 84906314998 scopus 로고    scopus 로고
    • Integrin-associated complexes form hierarchically with variable stoichiometry in nascent adhesions
    • Bachir, A. I. et al. Integrin-associated complexes form hierarchically with variable stoichiometry in nascent adhesions. Curr. Biol. 24, 1845-1853 (2014).
    • (2014) Curr. Biol. , vol.24 , pp. 1845-1853
    • Bachir, A.I.1
  • 31
    • 77949754056 scopus 로고    scopus 로고
    • Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation
    • Pasapera, A. M., Schneider, I. C., Rericha, E., Schlaepfer, D. D., Waterman, C. M. Myosin II activity regulates vinculin recruitment to focal adhesions through FAK-mediated paxillin phosphorylation. J. Cell Biol. 188, 877-890 (2010).
    • (2010) J. Cell Biol. , vol.188 , pp. 877-890
    • Pasapera, A.M.1    Schneider, I.C.2    Rericha, E.3    Schlaepfer, D.D.4    Waterman, C.M.5
  • 32
    • 84874652706 scopus 로고    scopus 로고
    • Vinculin regulates the recruitment and release of core focal adhesion proteins in a force-dependent manner
    • Carisey, A. et al. Vinculin Regulates the Recruitment and Release of Core Focal Adhesion Proteins in a Force-Dependent Manner. Curr. Biol. 23, 1-11 (2013).
    • (2013) Curr. Biol. , vol.23 , pp. 1-11
    • Carisey, A.1
  • 33
    • 0344465841 scopus 로고    scopus 로고
    • Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells
    • Zaidel-Bar, R., Ballestrem, C., Kam, Z., Geiger, B. Early molecular events in the assembly of matrix adhesions at the leading edge of migrating cells. J. Cell Sci. 116, 4605-4613 (2003).
    • (2003) J. Cell Sci. , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 34
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase
    • Hannigan, G. E. et al. Regulation of cell adhesion and anchorage-dependent growth by a new beta 1-integrin-linked protein kinase. Nature 379, 91-96 (1996).
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1
  • 36
    • 33645234372 scopus 로고    scopus 로고
    • Molecular mapping of tyrosine-phosphorylated proteins in focal adhesions using fluorescence resonance energy transfer
    • Ballestrem, C. et al. Molecular mapping of tyrosine-phosphorylated proteins in focal adhesions using fluorescence resonance energy transfer. J. Cell Sci. 119, 866-875 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 866-875
    • Ballestrem, C.1
  • 37
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cellmatrix adhesions
    • Zaidel-Bar, R., Milo, R., Kam, Z., Geiger, B. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cellmatrix adhesions. J. Cell Sci. 120, 137-148 (2007).
    • (2007) J. Cell Sci. , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 38
    • 83355173170 scopus 로고    scopus 로고
    • Paxillin mediates sensing of physical cues and regulates directional cell motility by controlling lamellipodia positioning
    • Sero, J. E. et al. Paxillin mediates sensing of physical cues and regulates directional cell motility by controlling lamellipodia positioning. PLoS ONE 6, e28303 (2011).
    • (2011) PLoS ONE , vol.6 , pp. e28303
    • Sero, J.E.1
  • 39
    • 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, 957-970 (2000).
    • (2000) J. Cell Biol. , vol.148 , pp. 957-970
    • Petit, V.1
  • 40
    • 0033606767 scopus 로고    scopus 로고
    • Shc and FAK differentially regulate cell motility and directionality modulated by PTEN
    • Gu, J. et al. Shc and FAK differentially regulate cell motility and directionality modulated by PTEN. J. Cell Biol. 146, 389-403 (1999).
    • (1999) J. Cell Biol. , vol.146 , pp. 389-403
    • Gu, J.1
  • 41
    • 84883606862 scopus 로고    scopus 로고
    • Integrin-specific control of focal adhesion kinase and RhoA regulates membrane protrusion and invasion
    • Costa, P., Scales, T. M. E., Ivaska, J., Parsons, M. Integrin-specific control of focal adhesion kinase and RhoA regulates membrane protrusion and invasion. PLoS ONE 8, e74659 (2013).
    • (2013) PLoS ONE , vol.8 , pp. e74659
    • Costa, P.1    Scales, T.M.E.2    Ivaska, J.3    Parsons, M.4
  • 42
    • 67649849871 scopus 로고    scopus 로고
    • Integrin beta1-focal adhesion kinase signaling directs the proliferation of metastatic cancer cells disseminated in the lungs
    • Shibue, T., Weinberg, R. A. Integrin beta1-focal adhesion kinase signaling directs the proliferation of metastatic cancer cells disseminated in the lungs. Proc. Natl. Acad. Sci. USA 106, 10290-10295 (2009).
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 10290-10295
    • Shibue, T.1    Weinberg, R.A.2
  • 43
    • 84860266328 scopus 로고    scopus 로고
    • FAK promotes recruitment of talin to nascent adhesions to control cell motility
    • Lawson, C. et al. FAK promotes recruitment of talin to nascent adhesions to control cell motility. J. Cell Biol. 196, 223-232 (2012).
    • (2012) J. Cell Biol. , vol.196 , pp. 223-232
    • Lawson, C.1
  • 44
    • 79551678536 scopus 로고    scopus 로고
    • Cross-Correlated Fluctuation Analysis Reveals Phosphorylation-RegulatedPaxillin-FAK Complexes in Nascent Adhesions
    • Choi, C. K., Zareno, J., Digman, M. A., Gratton, E., Horwitz, A. R. Cross-Correlated Fluctuation Analysis Reveals Phosphorylation-RegulatedPaxillin-FAK Complexes in Nascent Adhesions. Biophys. J. 100, 583-592 (2011).
    • (2011) Biophys. J. , vol.100 , pp. 583-592
    • Choi, C.K.1    Zareno, J.2    Digman, M.A.3    Gratton, E.4    Horwitz, A.R.5
  • 45
    • 84855500059 scopus 로고    scopus 로고
    • Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation
    • Yu, C.-H., Law, J. B. K., Suryana, M., Low, H. Y., Sheetz, M. P. Early integrin binding to Arg-Gly-Asp peptide activates actin polymerization and contractile movement that stimulates outward translocation. Proc. Natl. Acad. Sci. USA 108, 20585-20590 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20585-20590
    • Yu, C.-H.1    Law, J.B.K.2    Suryana, M.3    Low, H.Y.4    Sheetz, M.P.5
  • 46
    • 84921438809 scopus 로고    scopus 로고
    • Rac1-Dependent phosphorylation and focal adhesion recruitment of myosin IIA regulates migration and mechanosensing
    • Pasapera, A. M. et al. Rac1-Dependent Phosphorylation and Focal Adhesion Recruitment of Myosin IIA Regulates Migration and Mechanosensing. Curr. Biol. 25, 175-186 (2015).
    • (2015) Curr. Biol. , vol.25 , pp. 175-186
    • Pasapera, A.M.1
  • 47
    • 34447538483 scopus 로고    scopus 로고
    • Cellular characterization of a novel focal adhesion kinase inhibitor
    • Slack-Davis, J. K. et al. Cellular characterization of a novel focal adhesion kinase inhibitor. J. Biol. Chem. 282, 14845-14852 (2007).
    • (2007) J. Biol. Chem. , vol.282 , pp. 14845-14852
    • Slack-Davis, J.K.1
  • 48
    • 1642586962 scopus 로고    scopus 로고
    • FAK-Src signalling through paxillin ERK and MLCK regulates adhesion disassembly
    • Webb, D. J. et al. FAK-Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly. Nat. Cell Biol. 6, 154-161 (2004).
    • (2004) Nat. Cell Biol. , vol.6 , pp. 154-161
    • Webb, D.J.1
  • 49
    • 33847413148 scopus 로고    scopus 로고
    • Focal adhesion kinase modulates tension signaling to control actin and focal adhesion dynamics
    • Schober, M. et al. Focal adhesion kinase modulates tension signaling to control actin and focal adhesion dynamics. J. Cell Biol. 176, 667-680 (2007).
    • (2007) J. Cell Biol. , vol.176 , pp. 667-680
    • Schober, M.1
  • 50
    • 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. 1, 200-206 (1999).
    • (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
  • 51
    • 0345687176 scopus 로고    scopus 로고
    • Src kinase activation by direct interaction with the integrin beta cytoplasmic domain
    • Arias-Salgado, E. G. et al. Src kinase activation by direct interaction with the integrin beta cytoplasmic domain. Proc. Natl. Acad. Sci. USA 100, 13298-13302 (2003).
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 13298-13302
    • Arias-Salgado, E.G.1
  • 52
    • 34249063885 scopus 로고    scopus 로고
    • Caveolin-1 regulates cell polarization and directional migration through Src kinase and Rho GTPases
    • Grande-Garcia, A. et al. Caveolin-1 regulates cell polarization and directional migration through Src kinase and Rho GTPases. J. Cell Biol. 177, 683-694 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 683-694
    • Grande-Garcia, A.1
  • 53
    • 84867872264 scopus 로고    scopus 로고
    • Assembly and disassembly of cell matrix adhesions
    • Wehrle-Haller, B. Assembly and disassembly of cell matrix adhesions. Curr. Opin. Cell Biol. 24, 569-581 (2012).
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 569-581
    • Wehrle-Haller, B.1
  • 54
    • 84906669290 scopus 로고    scopus 로고
    • Steering cell migration: Lamellipodium dynamics and the regulation of directional persistence
    • Krause, M., Gautreau, A. Steering cell migration: lamellipodium dynamics and the regulation of directional persistence. Nat. Rev. Mol. Cell Biol. 15, 577-590 (2014).
    • (2014) Nat. Rev. Mol. Cell Biol. , vol.15 , pp. 577-590
    • Krause, M.1    Gautreau, A.2
  • 55
    • 79952328998 scopus 로고    scopus 로고
    • Cortactin: A multifunctional regulator of cellular invasiveness
    • Kirkbride, K. C., Sung, B. H., Sinha, S., Weaver, A. M. Cortactin: a multifunctional regulator of cellular invasiveness. Cell Adh. Migr. 5, 187-198 (2011).
    • (2011) Cell Adh. Migr. , vol.5 , pp. 187-198
    • Kirkbride, K.C.1    Sung, B.H.2    Sinha, S.3    Weaver, A.M.4
  • 56
    • 79955516270 scopus 로고    scopus 로고
    • Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells
    • Vicente-Manzanares, M., Newell-Litwa, K., Bachir, A. I., Whitmore, L. A., Horwitz, A. R. Myosin IIA/IIB restrict adhesive and protrusive signaling to generate front-back polarity in migrating cells. J. Cell Biol. 193, 381-396 (2011).
    • (2011) J. Cell Biol. , vol.193 , pp. 381-396
    • Vicente-Manzanares, M.1    Newell-Litwa, K.2    Bachir, A.I.3    Whitmore, L.A.4    Horwitz, A.R.5
  • 57
    • 84892589395 scopus 로고    scopus 로고
    • Combined effects of PEG hydrogel elasticity and cell-adhesive coating on fibroblast adhesion and persistent migration
    • Missirlis, D., Spatz, J. P. Combined effects of PEG hydrogel elasticity and cell-adhesive coating on fibroblast adhesion and persistent migration. Biomacromolecules 15, 195-205 (2014).
    • (2014) Biomacromolecules , vol.15 , pp. 195-205
    • Missirlis, D.1    Spatz, J.P.2
  • 58
    • 84871997465 scopus 로고    scopus 로고
    • Crawling from soft to stiff matrix polarizes the cytoskeleton and phosphoregulates myosin-II heavy chain
    • Raab, M. et al. Crawling from soft to stiff matrix polarizes the cytoskeleton and phosphoregulates myosin-II heavy chain. J. Cell Biol. 199, 669-683 (2012).
    • (2012) J. Cell Biol. , vol.199 , pp. 669-683
    • Raab, M.1
  • 59
    • 77955914547 scopus 로고    scopus 로고
    • Feedback amplification of fibrosis through matrix stiffening and COX-2 suppression
    • Liu, F. et al. Feedback amplification of fibrosis through matrix stiffening and COX-2 suppression. J. Cell Biol. 190, 693-706 (2010).
    • (2010) J. Cell Biol. , vol.190 , pp. 693-706
    • Liu, F.1
  • 60
    • 1542314212 scopus 로고    scopus 로고
    • Nonmuscle myosin IIb is involved in the guidance of fibroblast migration
    • Lo, C.-M. et al. Nonmuscle myosin IIb is involved in the guidance of fibroblast migration. Mol. Biol. Cell 15, 982-989 (2004).
    • (2004) Mol. Biol. Cell , vol.15 , pp. 982-989
    • Lo, C.-M.1
  • 62
    • 84875216391 scopus 로고    scopus 로고
    • Activation of beta 1 but not beta 3 integrin increases cell traction forces
    • Lin, G. L. et al. Activation of beta 1 but not beta 3 integrin increases cell traction forces. FEBS Lett. 587, 763-769 (2013).
    • (2013) FEBS Lett. , vol.587 , pp. 763-769
    • Lin, G.L.1
  • 63
    • 84887110448 scopus 로고    scopus 로고
    • Hydrogel micropillars with integrin selective peptidomimetic functionalized nanopatterned tops: A new tool for the measurement of cell traction forces transmitted through ?v?3-or ?5?1-integrins
    • Rahmouni, S. et al. Hydrogel micropillars with integrin selective peptidomimetic functionalized nanopatterned tops: a new tool for the measurement of cell traction forces transmitted through ?v?3-or ?5?1-integrins. Adv. Mater. 25, 5869-5874 (2013).
    • (2013) Adv. Mater. , vol.25 , pp. 5869-5874
    • Rahmouni, S.1
  • 64
    • 84865373665 scopus 로고    scopus 로고
    • Decoupling substrate stiffness, spread area, and micropost density: A close spatial relationship between traction forces and focal adhesions
    • Han, S. J., Bielawski, K. S., Ting, L. H., Rodriguez, M. L., Sniadecki, N. J. Decoupling substrate stiffness, spread area, and micropost density: a close spatial relationship between traction forces and focal adhesions. Biophys. J. 103, 640-648 (2012).
    • (2012) Biophys. J. , vol.103 , pp. 640-648
    • Han, S.J.1    Bielawski, K.S.2    Ting, L.H.3    Rodriguez, M.L.4    Sniadecki, N.J.5
  • 65
    • 84872849297 scopus 로고    scopus 로고
    • Functionalizing ?v?3-or ?5?1-Selective Integrin Antagonists for Surface Coating: A Method to Discriminate Integrin Subtypes in Vitro
    • Rechenmacher, F. et al. Functionalizing ?v?3-or ?5?1-Selective Integrin Antagonists for Surface Coating: A Method To Discriminate Integrin Subtypes In Vitro. Angew. Chem. Int. Ed. 52, 1572-1575 (2012).
    • (2012) Angew. Chem. Int. Ed. , vol.52 , pp. 1572-1575
    • Rechenmacher, F.1
  • 66
    • 84899579958 scopus 로고    scopus 로고
    • Pharmacophoric Modifications Lead to Superpotent ?v?3 Integrin Ligands with Suppressed ?5?1 Activity
    • Neubauer, S. et al. Pharmacophoric Modifications Lead to Superpotent ?v?3 Integrin Ligands with Suppressed ?5?1 Activity. J. Med. Chem. 57, 3410-3417 (2014).
    • (2014) J. Med. Chem. , vol.57 , pp. 3410-3417
    • Neubauer, S.1
  • 67
    • 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. 177, 515 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 515
    • White, D.P.1    Caswell, P.T.2    Norman, J.C.3
  • 68
    • 0029671372 scopus 로고    scopus 로고
    • Beta 1 integrin-dependent and-independent polymerization of fibronectin
    • Wennerberg, K. et al. Beta 1 integrin-dependent and-independent polymerization of fibronectin. J. Cell Biol. 132, 227-238 (1996).
    • (1996) J. Cell Biol. , vol.132 , pp. 227-238
    • Wennerberg, K.1
  • 69
    • 2442578523 scopus 로고    scopus 로고
    • Activation of Integrin Function by Nanopatterned Adhesive Interfaces
    • Arnold, M. et al. Activation of Integrin Function by Nanopatterned Adhesive Interfaces. ChemPhysChem 5, 383-388 (2004).
    • (2004) ChemPhysChem , vol.5 , pp. 383-388
    • Arnold, M.1
  • 70
    • 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. J. Binding of soluble fibronectin to integrin alpha5 beta1-link to focal adhesion redistribution and contractile shape. J. Cell Sci. 121, 2452-2462 (2008).
    • (2008) J. Cell Sci. , vol.121 , pp. 2452-2462
    • Huveneers, S.1    Truong, H.2    Fassler, R.3    Sonnenberg, A.4    Danen, E.H.J.5
  • 71
    • 84872084802 scopus 로고    scopus 로고
    • The tension mounts: Stress fibers as force-generating mechanotransducers
    • Burridge, K., Wittchen, E. S. The tension mounts: stress fibers as force-generating mechanotransducers. J. Cell Biol. 200, 9-19 (2013).
    • (2013) J. Cell Biol. , vol.200 , pp. 9-19
    • Burridge, K.1    Wittchen, E.S.2
  • 72
    • 0036325856 scopus 로고    scopus 로고
    • Directional control of lamellipodia extension by constraining cell shape and orienting cell tractional forces
    • Parker, K. K. et al. Directional control of lamellipodia extension by constraining cell shape and orienting cell tractional forces. FASEB J. 16, 1195-1204 (2002).
    • (2002) FASEB J. , vol.16 , pp. 1195-1204
    • Parker, K.K.1
  • 73
    • 33646861953 scopus 로고    scopus 로고
    • Cell distribution of stress fibres in response to the geometry of the adhesive environment
    • Thery, M., Pepin, A., Dressaire, E., Chen, Y., Bornens, M. Cell distribution of stress fibres in response to the geometry of the adhesive environment. Cell Motil. Cytoskeleton 63, 341-355 (2006).
    • (2006) Cell Motil. Cytoskeleton , vol.63 , pp. 341-355
    • Thery, M.1    Pepin, A.2    Dressaire, E.3    Chen, Y.4    Bornens, M.5
  • 74
    • 0033790713 scopus 로고    scopus 로고
    • Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts
    • Zamir, E. et al. Dynamics and segregation of cell-matrix adhesions in cultured fibroblasts. Nat. Cell Biol. 2, 191-196 (2000).
    • (2000) Nat. Cell Biol. , vol.2 , pp. 191-196
    • Zamir, E.1
  • 75
    • 84867084870 scopus 로고    scopus 로고
    • Integrins ?1 and ?3 exhibit distinct dynamic nanoscale organizations inside focal adhesions
    • Rossier, O. et al. Integrins ?1 and ?3 exhibit distinct dynamic nanoscale organizations inside focal adhesions. Nat. Cell Biol. 14, 1057-1067 (2012).
    • (2012) Nat. Cell Biol. , vol.14 , pp. 1057-1067
    • Rossier, O.1
  • 76
    • 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. et al. 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).
    • (2000) J. Cell Biol. , vol.148 , pp. 1075-1090
    • Pankov, R.1
  • 77
    • 34548316989 scopus 로고    scopus 로고
    • Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex
    • Serrels, B. et al. Focal adhesion kinase controls actin assembly via a FERM-mediated interaction with the Arp2/3 complex. Nat. Cell Biol. 9, 1046-1056 (2007).
    • (2007) Nat. Cell Biol. , vol.9 , pp. 1046-1056
    • Serrels, B.1
  • 78
    • 84865579696 scopus 로고    scopus 로고
    • Cortactin as a target for FAK in the regulation of focal adhesion dynamics
    • Tomar, A., Lawson, C., Ghassemian, M., Schlaepfer, D. D. Cortactin as a target for FAK in the regulation of focal adhesion dynamics. PLoS ONE 7, e44041 (2012).
    • (2012) PLoS ONE , vol.7 , pp. e44041
    • Tomar, A.1    Lawson, C.2    Ghassemian, M.3    Schlaepfer, D.D.4
  • 79
    • 84903168767 scopus 로고    scopus 로고
    • A FAK-Cas-Rac-lamellipodin signaling module transduces extracellular matrix stiffness into mechanosensitive cell cycling
    • Bae, Y. H. et al. A FAK-Cas-Rac-lamellipodin signaling module transduces extracellular matrix stiffness into mechanosensitive cell cycling. Sci. Signal. 7, ra57-ra57 (2014).
    • (2014) Sci. Signal. , vol.7 , pp. ra57-ra57
    • Bae, Y.H.1
  • 80
    • 69449103232 scopus 로고    scopus 로고
    • A FAK-p120RasGAP-p190RhoGAP complex regulates polarity in migrating cells
    • Tomar, A., Lim, S.-T., Lim, Y., Schlaepfer, D. D. A FAK-p120RasGAP-p190RhoGAP complex regulates polarity in migrating cells. J. Cell Sci. 122, 1852-1862 (2009).
    • (2009) J. Cell Sci. , vol.122 , pp. 1852-1862
    • Tomar, A.1    Lim, S.-T.2    Lim, Y.3    Schlaepfer, D.D.4
  • 81
    • 84863804465 scopus 로고    scopus 로고
    • Specific ?-containing integrins exert differential control on proliferation and two-dimensional collective cell migration in mammary epithelial cells
    • Jeanes, A. I. et al. Specific ?-containing integrins exert differential control on proliferation and two-dimensional collective cell migration in mammary epithelial cells. J. Biol. Chem. 287, 24103-24112 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 24103-24112
    • Jeanes, A.I.1
  • 82
    • 0034886701 scopus 로고    scopus 로고
    • Integrin-specific activation of Rac controls progression through the G(1) phase of the cell cycle
    • Mettouchi, A. et al. Integrin-specific activation of Rac controls progression through the G(1) phase of the cell cycle. Mol. Cell 8, 115-127 (2001).
    • (2001) Mol. Cell , vol.8 , pp. 115-127
    • Mettouchi, A.1
  • 83
    • 0037092520 scopus 로고    scopus 로고
    • Differential regulation of Rho GTPases by beta 1 and beta 3 integrins: The role of an extracellular domain of integrin in intracellular signaling
    • Miao, H. et al. Differential regulation of Rho GTPases by beta 1 and beta 3 integrins: the role of an extracellular domain of integrin in intracellular signaling. J. Cell Sci. 115, 2199-2206 (2002).
    • (2002) J. Cell Sci. , vol.115 , pp. 2199-2206
    • Miao, H.1
  • 84
    • 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. D., Hall, A. 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).
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 85
    • 33847159264 scopus 로고    scopus 로고
    • Polymerizing actin fibers position integrins primed to probe for adhesion sites
    • Galbraith, C. G., Yamada, K. M., Galbraith, J. A. Polymerizing actin fibers position integrins primed to probe for adhesion sites. Science 315, 992-995 (2007).
    • (2007) Science , vol.315 , pp. 992-995
    • Galbraith, C.G.1    Yamada, K.M.2    Galbraith, J.A.3
  • 86
    • 0034745356 scopus 로고    scopus 로고
    • Rac recruits high-affinity integrin alphavbeta3 to lamellipodia in endothelial cell migration
    • Kiosses, W. B., Shattil, S. J., Pampori, N., Schwartz, M. A. Rac recruits high-affinity integrin alphavbeta3 to lamellipodia in endothelial cell migration. Nat. Cell Biol. 3, 316-320 (2001).
    • (2001) Nat. Cell Biol. , vol.3 , pp. 316-320
    • Kiosses, W.B.1    Shattil, S.J.2    Pampori, N.3    Schwartz, M.A.4
  • 87
    • 24144458264 scopus 로고    scopus 로고
    • A Rac switch regulates random versus directionally persistent cell migration
    • Pankov, R. et al. A Rac switch regulates random versus directionally persistent cell migration. J. Cell Biol. 170, 793-802 (2005).
    • (2005) J. Cell Biol. , vol.170 , pp. 793-802
    • Pankov, R.1
  • 88
    • 14744267471 scopus 로고    scopus 로고
    • The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration
    • Pratt, S. J. et al. The LIM protein Ajuba influences p130Cas localization and Rac1 activity during cell migration. J. Cell Biol. 168, 813-824 (2005).
    • (2005) J. Cell Biol. , vol.168 , pp. 813-824
    • Pratt, S.J.1
  • 89
    • 84861926483 scopus 로고    scopus 로고
    • The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration
    • Suraneni, P. et al. The Arp2/3 complex is required for lamellipodia extension and directional fibroblast cell migration. J. Cell Biol. 197, 239-251 (2012).
    • (2012) J. Cell Biol. , vol.197 , pp. 239-251
    • Suraneni, P.1
  • 90
    • 22744434624 scopus 로고    scopus 로고
    • Cortactin promotes cell motility by enhancing lamellipodial persistence
    • Bryce, N. S. et al. Cortactin Promotes Cell Motility by Enhancing Lamellipodial Persistence. Curr. Biol. 15, 1276-1285 (2005).
    • (2005) Curr. Biol. , vol.15 , pp. 1276-1285
    • Bryce, N.S.1
  • 91
    • 84863229890 scopus 로고    scopus 로고
    • Arp2/3 Is critical for lamellipodiaand response to extracellular matrix cues but is dispensable for chemotaxis
    • Wu, C. et al. Arp2/3 Is Critical for Lamellipodiaand Response to Extracellular Matrix Cues but Is Dispensable for Chemotaxis. Cell 148, 973-987 (2012).
    • (2012) Cell , vol.148 , pp. 973-987
    • Wu, C.1
  • 92
    • 52449089651 scopus 로고    scopus 로고
    • Comparative dynamics of retrograde actin flow and focal adhesions: Formation of nascent adhesions triggers transition from fast to slow flow
    • Alexandrova, A. Y. et al. Comparative dynamics of retrograde actin flow and focal adhesions: formation of nascent adhesions triggers transition from fast to slow flow. PLoS ONE 3, e3234 (2008).
    • (2008) PLoS ONE , vol.3 , pp. e3234
    • Alexandrova, A.Y.1
  • 93
    • 79953325280 scopus 로고    scopus 로고
    • A role for actin arcs in the leading-edge advance of migrating cells
    • Burnette, D. T. et al. A role for actin arcs in the leading-edge advance of migrating cells. Nat. Cell Biol. 13, 371-382 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 371-382
    • Burnette, D.T.1
  • 94
    • 33846672361 scopus 로고    scopus 로고
    • Lamellipodial actin mechanically links myosin activity with adhesion-site formation
    • Giannone, G. et al. Lamellipodial actin mechanically links myosin activity with adhesion-site formation. Cell 128, 575 (2007).
    • (2007) Cell , vol.128 , pp. 575
    • Giannone, G.1
  • 95
    • 84952639123 scopus 로고    scopus 로고
    • Persistent cell migration and adhesion rely on retrograde transport of ?1 integrin
    • Shafaq-Zadah, M. et al. Persistent cell migration and adhesion rely on retrograde transport of ?1 integrin. Nat. Cell Biol. 18, 54-64 (2015).
    • (2015) Nat. Cell Biol. , vol.18 , pp. 54-64
    • Shafaq-Zadah, M.1
  • 96
    • 79959572798 scopus 로고    scopus 로고
    • Subcellular spatial segregation of integrin subtypes by patterned multicomponent surfaces
    • Desai, R. A., Khan, M. K., Gopal, S. B., Chen, C. S. Subcellular spatial segregation of integrin subtypes by patterned multicomponent surfaces. Integr. Biol. 3, 560 (2011).
    • (2011) Integr. Biol. , vol.3 , pp. 560
    • Desai, R.A.1    Khan, M.K.2    Gopal, S.B.3    Chen, C.S.4
  • 97
    • 0030613632 scopus 로고    scopus 로고
    • The alphavbeta3 integrin regulates alpha5beta1-mediated cell migration toward fibronectin
    • Simon, K. O., Nutt, E. M., Abraham, D. G., Rodan, G. A., Duong, L. T. The alphavbeta3 integrin regulates alpha5beta1-mediated cell migration toward fibronectin. J. Biol. Chem. 272, 29380-29389 (1997).
    • (1997) J. Biol. Chem. , vol.272 , pp. 29380-29389
    • Simon, K.O.1    Nutt, E.M.2    Abraham, D.G.3    Rodan, G.A.4    Duong, L.T.5
  • 98
    • 77951180336 scopus 로고    scopus 로고
    • Alpha v beta3 integrin spatially regulates VASP and RIAM to control adhesion dynamics and migration
    • Worth, D. C. et al. Alpha v beta3 integrin spatially regulates VASP and RIAM to control adhesion dynamics and migration. J. Cell Biol. 189, 369-383 (2010).
    • (2010) J. Cell Biol. , vol.189 , pp. 369-383
    • Worth, D.C.1
  • 99
    • 0034142030 scopus 로고    scopus 로고
    • Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts
    • Woods, A., Longley, R. L., Tumova, S., Couchman, J. R. Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts. Arch. Biochem. Biophys. 374, 66-72 (2000).
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 66-72
    • Woods, A.1    Longley, R.L.2    Tumova, S.3    Couchman, J.R.4
  • 100
    • 34248159909 scopus 로고    scopus 로고
    • Syndecan-4-dependent Rac1 regulation determines directional migration in response to the extracellular matrix
    • Bass, M. D. et al. Syndecan-4-dependent Rac1 regulation determines directional migration in response to the extracellular matrix. J. Cell Biol. 177, 527-538 (2007).
    • (2007) J. Cell Biol. , vol.177 , pp. 527-538
    • Bass, M.D.1
  • 101
    • 45349086241 scopus 로고    scopus 로고
    • P190RhoGAP is the convergence point of adhesion signals from alpha 5 beta 1 integrin and syndecan-4
    • Bass, M. D. et al. p190RhoGAP is the convergence point of adhesion signals from alpha 5 beta 1 integrin and syndecan-4. J. Cell Biol. 181, 1013-1026 (2008).
    • (2008) J. Cell Biol. , vol.181 , pp. 1013-1026
    • Bass, M.D.1
  • 102
    • 84875259429 scopus 로고    scopus 로고
    • Syndecan-4 phosphorylation is a control point for integrin recycling
    • Morgan, M. R. et al. Syndecan-4 phosphorylation is a control point for integrin recycling. Dev. Cell 24, 472-485 (2013).
    • (2013) Dev. Cell , vol.24 , pp. 472-485
    • Morgan, M.R.1
  • 103
    • 0041976960 scopus 로고    scopus 로고
    • Spatial restriction of alpha4 integrin phosphorylation regulates lamellipodial stability and alpha4beta1-dependent cell migration
    • Goldfinger, L. E., Han, J., Kiosses, W. B., Howe, A. K., Ginsberg, M. H. Spatial restriction of alpha4 integrin phosphorylation regulates lamellipodial stability and alpha4beta1-dependent cell migration. J. Cell Biol. 162, 731-741 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 731-741
    • Goldfinger, L.E.1    Han, J.2    Kiosses, W.B.3    Howe, A.K.4    Ginsberg, M.H.5
  • 104
    • 17344366888 scopus 로고    scopus 로고
    • An ?4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells
    • Nishiya, N., Kiosses, W. B., Han, J., Ginsberg, M. H. An ?4 integrin-paxillin-Arf-GAP complex restricts Rac activation to the leading edge of migrating cells. Nat. Cell Biol. 7, 343-352 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 343-352
    • Nishiya, N.1    Kiosses, W.B.2    Han, J.3    Ginsberg, M.H.4
  • 105
    • 78649727712 scopus 로고    scopus 로고
    • The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factorbinding domain
    • Martino, M. M., Hubbell, J. A. The 12th-14th type III repeats of fibronectin function as a highly promiscuous growth factorbinding domain. FASEB J. 24, 4711-4721 (2010).
    • (2010) FASEB J. , vol.24 , pp. 4711-4721
    • Martino, M.M.1    Hubbell, J.A.2
  • 106
    • 0035954424 scopus 로고    scopus 로고
    • Differential dynamics of alpha 5 integrin, paxillin, and alpha-actinin during formation and disassembly of adhesions in migrating cells
    • Laukaitis, C. M., Webb, D. J., Donais, K., Horwitz, A. F. Differential dynamics of alpha 5 integrin, paxillin, and alpha-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
  • 107
    • 0036615472 scopus 로고    scopus 로고
    • Microfilament-dependent movement of the beta3 integrin subunit within focal contacts of endothelial cells
    • Tsuruta, D. et al. Microfilament-dependent movement of the beta3 integrin subunit within focal contacts of endothelial cells. FASEB J. 16, 866-868 (2002).
    • (2002) FASEB J. , vol.16 , pp. 866-868
    • Tsuruta, D.1
  • 108
    • 84868089352 scopus 로고    scopus 로고
    • Stiffness-controlled three-dimensional extracellular matrices for high-resolution imaging of cell behavior
    • Fischer, R. S., Myers, K. A., Gardel, M. L., Waterman, C. M. Stiffness-controlled three-dimensional extracellular matrices for high-resolution imaging of cell behavior. Nat. Protoc. 7, 2056-2066 (2012).
    • (2012) Nat. Protoc. , vol.7 , pp. 2056-2066
    • Fischer, R.S.1    Myers, K.A.2    Gardel, M.L.3    Waterman, C.M.4
  • 109
    • 84857132597 scopus 로고    scopus 로고
    • Spatial organization of the extracellular matrix regulates cell-cell junction positioning
    • Tseng, Q. et al. Spatial organization of the extracellular matrix regulates cell-cell junction positioning. Proc. Natl. Acad. Sci. USA 109, 1506-1511 (2012).
    • (2012) Proc. Natl. Acad. Sci. USA , vol.109 , pp. 1506-1511
    • Tseng, Q.1
  • 110
    • 37749000819 scopus 로고    scopus 로고
    • High resolution traction force microscopy based on experimental and computational advances
    • Sabass, B., Gardel, M. L., Waterman, C. M., Schwarz, U. S. High resolution traction force microscopy based on experimental and computational advances. Biophys. J. 94, 207-220 (2008).
    • (2008) Biophys. J. , vol.94 , pp. 207-220
    • Sabass, B.1    Gardel, M.L.2    Waterman, C.M.3    Schwarz, U.S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.