메뉴 건너뛰기




Volumn 24, Issue 5, 2013, Pages 447-458

Dynamic Regulation of the Structure and Functions of Integrin Adhesions

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; ALPHA INTEGRIN; BETA INTEGRIN; FIBRONECTIN; PROTEIN CDC42; RHO KINASE;

EID: 84875273788     PISSN: 15345807     EISSN: 18781551     Source Type: Journal    
DOI: 10.1016/j.devcel.2013.02.012     Document Type: Review
Times cited : (216)

References (142)
  • 1
    • 0016489782 scopus 로고
    • Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy
    • Abercrombie M., Dunn G.A. Adhesions of fibroblasts to substratum during contact inhibition observed by interference reflection microscopy. Exp. Cell Res. 1975, 92:57-62.
    • (1975) Exp. Cell Res. , vol.92 , pp. 57-62
    • Abercrombie, M.1    Dunn, G.A.2
  • 2
    • 0010613696 scopus 로고
    • Invasiveness of sarcoma cells
    • Abercrombie M., Heaysman J.E. Invasiveness of sarcoma cells. Nature 1954, 174:697-698.
    • (1954) Nature , vol.174 , pp. 697-698
    • Abercrombie, M.1    Heaysman, J.E.2
  • 3
    • 0015104295 scopus 로고
    • The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella
    • Abercrombie M., Heaysman J.E., Pegrum S.M. The locomotion of fibroblasts in culture. IV. Electron microscopy of the leading lamella. Exp. Cell Res. 1971, 67:359-367.
    • (1971) Exp. Cell Res. , vol.67 , pp. 359-367
    • Abercrombie, M.1    Heaysman, J.E.2    Pegrum, S.M.3
  • 4
    • 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., Arnold K., Schaub S., Vasiliev J.M., Meister J.J., Bershadsky A.D., Verkhovsky A.B. Comparative dynamics of retrograde actin flow and focal adhesions: formation of nascent adhesions triggers transition from fast to slow flow. PLoS ONE 2008, 3:e3234.
    • (2008) PLoS ONE , vol.3
    • Alexandrova, A.Y.1    Arnold, K.2    Schaub, S.3    Vasiliev, J.M.4    Meister, J.J.5    Bershadsky, A.D.6    Verkhovsky, A.B.7
  • 5
    • 33749091631 scopus 로고
    • Morphology and migratory behavior of embryonic pigment cells studied by phase microscopy
    • Algard F.T. Morphology and migratory behavior of embryonic pigment cells studied by phase microscopy. J. Exp. Zool. 1953, 123:499-521.
    • (1953) J. Exp. Zool. , vol.123 , pp. 499-521
    • Algard, F.T.1
  • 6
    • 24644471128 scopus 로고    scopus 로고
    • Src and FAK signalling controls adhesion fate and the epithelial-to-mesenchymal transition
    • Avizienyte E., Frame M.C. Src and FAK signalling controls adhesion fate and the epithelial-to-mesenchymal transition. Curr. Opin. Cell Biol. 2005, 17:542-547.
    • (2005) Curr. Opin. Cell Biol. , vol.17 , pp. 542-547
    • Avizienyte, E.1    Frame, M.C.2
  • 8
    • 84875258534 scopus 로고    scopus 로고
    • Cell-matrix adhesions
    • in MBInfo.
    • Bershadsky, A. (2012). Cell-matrix adhesions. Cellular structures in mechanosensing and cell motility, in MBInfo. https://sites.google.com/a/mechanobio.info/mbinfo/Home/Dynamic-Structures-in-Mechanosensing/cell-matrix-adhesions.
    • (2012) Cellular structures in mechanosensing and cell motility
    • Bershadsky, A.1
  • 9
    • 33646183674 scopus 로고    scopus 로고
    • Force-induced adsorption and anisotropic growth of focal adhesions
    • Besser A., Safran S.A. Force-induced adsorption and anisotropic growth of focal adhesions. Biophys. J. 2006, 90:3469-3484.
    • (2006) Biophys. J. , vol.90 , pp. 3469-3484
    • Besser, A.1    Safran, S.A.2
  • 10
    • 0023663872 scopus 로고
    • The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments
    • Bogaert T., Brown N., Wilcox M. The Drosophila PS2 antigen is an invertebrate integrin that, like the fibronectin receptor, becomes localized to muscle attachments. Cell 1987, 51:929-940.
    • (1987) Cell , vol.51 , pp. 929-940
    • Bogaert, T.1    Brown, N.2    Wilcox, M.3
  • 11
    • 0036745861 scopus 로고    scopus 로고
    • Integrins in development: moving on, responding to, and sticking to the extracellular matrix
    • Bökel C., Brown N.H. Integrins in development: moving on, responding to, and sticking to the extracellular matrix. Dev. Cell 2002, 3:311-321.
    • (2002) Dev. Cell , vol.3 , pp. 311-321
    • Bökel, C.1    Brown, N.H.2
  • 14
    • 0024972501 scopus 로고
    • Requirement for integrins during Drosophila wing development
    • Brower D.L., Jaffe S.M. Requirement for integrins during Drosophila wing development. Nature 1989, 342:285-287.
    • (1989) Nature , vol.342 , pp. 285-287
    • Brower, D.L.1    Jaffe, S.M.2
  • 17
    • 0018905464 scopus 로고
    • Microinjection and localization of a 130K protein in living fibroblasts: a relationship to actin and fibronectin
    • Burridge K., Feramisco J.R. Microinjection and localization of a 130K protein in living fibroblasts: a relationship to actin and fibronectin. Cell 1980, 19:587-595.
    • (1980) Cell , vol.19 , pp. 587-595
    • Burridge, K.1    Feramisco, J.R.2
  • 18
    • 0024150623 scopus 로고
    • Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge K., Fath K., Kelly T., Nuckolls G., Turner C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell Biol. 1988, 4:487-525.
    • (1988) Annu. Rev. Cell Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, G.4    Turner, C.5
  • 19
    • 0041924982 scopus 로고    scopus 로고
    • A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src
    • Carragher N.O., Westhoff M.A., Fincham V.J., Schaller M.D., Frame M.C. A novel role for FAK as a protease-targeting adaptor protein: regulation by p42 ERK and Src. Curr. Biol. 2003, 13:1442-1450.
    • (2003) Curr. Biol. , vol.13 , pp. 1442-1450
    • Carragher, N.O.1    Westhoff, M.A.2    Fincham, V.J.3    Schaller, M.D.4    Frame, M.C.5
  • 21
    • 0342275046 scopus 로고
    • Micro-operations on cells in tissue cultures
    • Chambers R., Fell H.B. Micro-operations on cells in tissue cultures. Proc. Roy. Soc. Ser. B 1931, 109:380-403.
    • (1931) Proc. Roy. Soc. Ser. B , vol.109 , pp. 380-403
    • Chambers, R.1    Fell, H.B.2
  • 23
    • 56349169536 scopus 로고    scopus 로고
    • Mechanotransduction - a field pulling together?
    • Chen C.S. Mechanotransduction - a field pulling together?. J. Cell Sci. 2008, 121:3285-3292.
    • (2008) J. Cell Sci. , vol.121 , pp. 3285-3292
    • Chen, C.S.1
  • 24
    • 51049104617 scopus 로고    scopus 로고
    • Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner
    • Choi C.K., Vicente-Manzanares M., Zareno J., Whitmore L.A., Mogilner A., Horwitz A.R. Actin and alpha-actinin orchestrate the assembly and maturation of nascent adhesions in a myosin II motor-independent manner. Nat. Cell Biol. 2008, 10:1039-1050.
    • (2008) Nat. Cell Biol. , vol.10 , pp. 1039-1050
    • Choi, C.K.1    Vicente-Manzanares, M.2    Zareno, J.3    Whitmore, L.A.4    Mogilner, A.5    Horwitz, A.R.6
  • 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
    • 0038409304 scopus 로고    scopus 로고
    • Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes
    • Clark K.A., McGrail M., Beckerle M.C. Analysis of PINCH function in Drosophila demonstrates its requirement in integrin-dependent cellular processes. Development 2003, 130:2611-2621.
    • (2003) Development , vol.130 , pp. 2611-2621
    • Clark, K.A.1    McGrail, M.2    Beckerle, M.C.3
  • 27
    • 0001275564 scopus 로고
    • The mechanism of adhesion of cells to glass. A study by interference reflection microscopy
    • Curtis A.S. The mechanism of adhesion of cells to glass. A study by interference reflection microscopy. J. Cell Biol. 1964, 20:199-215.
    • (1964) J. Cell Biol. , vol.20 , pp. 199-215
    • Curtis, A.S.1
  • 29
    • 41649110901 scopus 로고    scopus 로고
    • Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy
    • Digman M.A., Brown C.M., Horwitz A.R., Mantulin W.W., Gratton E. Paxillin dynamics measured during adhesion assembly and disassembly by correlation spectroscopy. Biophys. J. 2008, 94:2819-2831.
    • (2008) Biophys. J. , vol.94 , pp. 2819-2831
    • Digman, M.A.1    Brown, C.M.2    Horwitz, A.R.3    Mantulin, W.W.4    Gratton, E.5
  • 32
    • 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
  • 33
    • 0028979154 scopus 로고
    • Consequences of lack of beta 1 integrin gene expression in mice
    • Fässler R., Meyer M. Consequences of lack of beta 1 integrin gene expression in mice. Genes Dev. 1995, 9:1896-1908.
    • (1995) Genes Dev. , vol.9 , pp. 1896-1908
    • Fässler, R.1    Meyer, M.2
  • 35
    • 0018692430 scopus 로고
    • A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells
    • Geiger B. A 130K protein from chicken gizzard: its localization at the termini of microfilament bundles in cultured chicken cells. Cell 1979, 18:193-205.
    • (1979) Cell , vol.18 , pp. 193-205
    • Geiger, B.1
  • 36
    • 80053298724 scopus 로고    scopus 로고
    • Molecular architecture and function of matrix adhesions
    • Geiger B., Yamada K.M. Molecular architecture and function of matrix adhesions. Cold Spring Harb. Perspect. Biol. 2011, 3:201-221.
    • (2011) Cold Spring Harb. Perspect. Biol. , vol.3 , pp. 201-221
    • Geiger, B.1    Yamada, K.M.2
  • 37
    • 84867841256 scopus 로고    scopus 로고
    • Opening the floodgates: proteomics and the integrin adhesome
    • Geiger T., Zaidel-Bar R. Opening the floodgates: proteomics and the integrin adhesome. Curr. Opin. Cell Biol. 2012, 24:562-568.
    • (2012) Curr. Opin. Cell Biol. , vol.24 , pp. 562-568
    • Geiger, T.1    Zaidel-Bar, R.2
  • 40
    • 0342712965 scopus 로고
    • Cell behavior in tissue cultures
    • Goodrich H.B. Cell behavior in tissue cultures. Biol. Bull. 1924, 46:252-262.
    • (1924) Biol. Bull. , vol.46 , pp. 252-262
    • Goodrich, H.B.1
  • 42
    • 0034715896 scopus 로고    scopus 로고
    • Insights into extracellular matrix functions from mutant mouse models
    • Gustafsson E., Fässler R. Insights into extracellular matrix functions from mutant mouse models. Exp. Cell Res. 2000, 261:52-68.
    • (2000) Exp. Cell Res. , vol.261 , pp. 52-68
    • Gustafsson, E.1    Fässler, R.2
  • 43
    • 0015862922 scopus 로고
    • Location of cellular adhesions to solid substrata
    • Harris A. Location of cellular adhesions to solid substrata. Dev. Biol. 1973, 35:97-114.
    • (1973) Dev. Biol. , vol.35 , pp. 97-114
    • Harris, A.1
  • 44
    • 0000822531 scopus 로고
    • On the stereotropism of embryonic cells
    • Harrison R.G. On the stereotropism of embryonic cells. Science 1911, 34:279-281.
    • (1911) Science , vol.34 , pp. 279-281
    • Harrison, R.G.1
  • 45
    • 0019779921 scopus 로고
    • Extracellular matrix
    • Hay E.D. Extracellular matrix. J. Cell Biol. 1981, 91:205s-223s.
    • (1981) J. Cell Biol. , vol.91
    • Hay, E.D.1
  • 46
    • 78649807120 scopus 로고    scopus 로고
    • Tissue elongation requires oscillating contractions of a basal actomyosin network
    • He L., Wang X., Tang H.L., Montell D.J. Tissue elongation requires oscillating contractions of a basal actomyosin network. Nat. Cell Biol. 2010, 12:1133-1142.
    • (2010) Nat. Cell Biol. , vol.12 , pp. 1133-1142
    • He, L.1    Wang, X.2    Tang, H.L.3    Montell, D.J.4
  • 47
    • 0017904573 scopus 로고
    • Cell to substratum contacts of chick fibroblasts and their relation to the microfilament system. A correlated interference-reflexion and high-voltage electron-microscope study
    • Heath J.P., Dunn G.A. Cell to substratum contacts of chick fibroblasts and their relation to the microfilament system. A correlated interference-reflexion and high-voltage electron-microscope study. J. Cell Sci. 1978, 29:197-212.
    • (1978) J. Cell Sci. , vol.29 , pp. 197-212
    • Heath, J.P.1    Dunn, G.A.2
  • 48
    • 0017904907 scopus 로고
    • Transmembrane linkage of fibronectin to intracellular actin-containing filaments in cultured human fibroblasts
    • Heggeness M.H., Ash J.F., Singer S.J. Transmembrane linkage of fibronectin to intracellular actin-containing filaments in cultured human fibroblasts. Ann. N Y Acad. Sci. 1978, 312:414-417.
    • (1978) Ann. N Y Acad. Sci. , vol.312 , pp. 414-417
    • Heggeness, M.H.1    Ash, J.F.2    Singer, S.J.3
  • 50
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage
    • Horwitz A., Duggan K., Buck C., Beckerle M.C., Burridge K. Interaction of plasma membrane fibronectin receptor with talin-a transmembrane linkage. Nature 1986, 320:531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 51
    • 33646386142 scopus 로고    scopus 로고
    • Stress fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen P., Lappalainen P. Stress fibers are generated by two distinct actin assembly mechanisms in motile cells. J. Cell Biol. 2006, 173:383-394.
    • (2006) J. Cell Biol. , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 52
    • 0033982574 scopus 로고    scopus 로고
    • Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice
    • Huang X., Griffiths M., Wu J., Farese R.V., Sheppard D. Normal development, wound healing, and adenovirus susceptibility in beta5-deficient mice. Mol. Cell. Biol. 2000, 20:755-759.
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 755-759
    • Huang, X.1    Griffiths, M.2    Wu, J.3    Farese, R.V.4    Sheppard, D.5
  • 56
    • 0023666065 scopus 로고
    • Integrins: a family of cell surface receptors
    • Hynes R.O. Integrins: a family of cell surface receptors. Cell 1987, 48:549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 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
    • 0018036788 scopus 로고
    • Relationships between fibronectin (LETS protein) and actin
    • Hynes R.O., Destree A.T. Relationships between fibronectin (LETS protein) and actin. Cell 1978, 15:875-886.
    • (1978) Cell , vol.15 , pp. 875-886
    • Hynes, R.O.1    Destree, A.T.2
  • 59
    • 0017143820 scopus 로고
    • Cell-to-substrate contacts in living fibroblasts: an interference reflexion study with an evaluation of the technique
    • Izzard C.S., Lochner L.R. Cell-to-substrate contacts in living fibroblasts: an interference reflexion study with an evaluation of the technique. J. Cell Sci. 1976, 21:129-159.
    • (1976) J. Cell Sci. , vol.21 , pp. 129-159
    • Izzard, C.S.1    Lochner, L.R.2
  • 60
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: biochemistry and biology
    • Jaffe A.B., Hall A. Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 2005, 21:247-269.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 61
    • 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
  • 62
    • 0028836195 scopus 로고
    • F-actin binding site masked by the intramolecular association of vinculin head and tail domains
    • Johnson R.P., Craig S.W. F-actin binding site masked by the intramolecular association of vinculin head and tail domains. Nature 1995, 373:261-264.
    • (1995) Nature , vol.373 , pp. 261-264
    • Johnson, R.P.1    Craig, S.W.2
  • 65
    • 34548403115 scopus 로고    scopus 로고
    • Mammary epithelial cell: influence of extracellular matrix composition and organization during development and tumorigenesis
    • Kass L., Erler J.T., Dembo M., Weaver V.M. Mammary epithelial cell: influence of extracellular matrix composition and organization during development and tumorigenesis. Int. J. Biochem. Cell Biol. 2007, 39:1987-1994.
    • (2007) Int. J. Biochem. Cell Biol. , vol.39 , pp. 1987-1994
    • Kass, L.1    Erler, J.T.2    Dembo, M.3    Weaver, V.M.4
  • 66
    • 0032872870 scopus 로고    scopus 로고
    • Microtubule targeting of substrate contacts promotes their relaxation and dissociation
    • Kaverina I., Krylyshkina O., Small J.V. Microtubule targeting of substrate contacts promotes their relaxation and dissociation. J. Cell Biol. 1999, 146:1033-1044.
    • (1999) J. Cell Biol. , vol.146 , pp. 1033-1044
    • Kaverina, I.1    Krylyshkina, O.2    Small, J.V.3
  • 67
    • 0042681786 scopus 로고    scopus 로고
    • Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins
    • Kim M., Carman C.V., Springer T.A. Bidirectional transmembrane signaling by cytoplasmic domain separation in integrins. Science 2003, 301:1720-1725.
    • (2003) Science , vol.301 , pp. 1720-1725
    • Kim, M.1    Carman, C.V.2    Springer, T.A.3
  • 68
    • 0018649896 scopus 로고
    • In vivo distribution and turnover of fluorescently labeled actin microinjected into human fibroblasts
    • Kreis T.E., Winterhalter K.H., Birchmeier W. In vivo distribution and turnover of fluorescently labeled actin microinjected into human fibroblasts. Proc. Natl. Acad. Sci. USA 1979, 76:3814-3818.
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 3814-3818
    • Kreis, T.E.1    Winterhalter, K.H.2    Birchmeier, W.3
  • 69
    • 78650457713 scopus 로고    scopus 로고
    • Reducing background fluorescence reveals adhesions in 3D matrices
    • author reply 5-7
    • Kubow K.E., Horwitz A.R. Reducing background fluorescence reveals adhesions in 3D matrices. Nat. Cell Biol. 2011, 13:3-5. author reply 5-7.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 3-5
    • Kubow, K.E.1    Horwitz, A.R.2
  • 70
    • 79953303384 scopus 로고    scopus 로고
    • Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation
    • Kuo J.C., Han X., Hsiao C.T., Yates J.R., Waterman C.M. Analysis of the myosin-II-responsive focal adhesion proteome reveals a role for β-Pix in negative regulation of focal adhesion maturation. Nat. Cell Biol. 2011, 13:383-393.
    • (2011) Nat. Cell Biol. , vol.13 , pp. 383-393
    • Kuo, J.C.1    Han, X.2    Hsiao, C.T.3    Yates, J.R.4    Waterman, C.M.5
  • 71
    • 0007617079 scopus 로고
    • The adhesive quality of cells
    • Lewis W.H. The adhesive quality of cells. Anat. Rec. 1922, 23:387-392.
    • (1922) Anat. Rec. , vol.23 , pp. 387-392
    • Lewis, W.H.1
  • 72
  • 73
    • 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
  • 75
    • 84855163922 scopus 로고    scopus 로고
    • Mechanotransduction in vivo by repeated talin stretch-relaxation events depends upon vinculin
    • Margadant F., Chew L.L., Hu X., Yu H., Bate N., Zhang X., Sheetz M. Mechanotransduction in vivo by repeated talin stretch-relaxation events depends upon vinculin. PLoS Biol. 2011, 9:e1001223.
    • (2011) PLoS Biol. , vol.9
    • Margadant, F.1    Chew, L.L.2    Hu, X.3    Yu, H.4    Bate, N.5    Zhang, X.6    Sheetz, M.7
  • 76
    • 0033539916 scopus 로고    scopus 로고
    • Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction
    • McCann R.O., Craig S.W. Functional genomic analysis reveals the utility of the I/LWEQ module as a predictor of protein:actin interaction. Biochem. Biophys. Res. Commun. 1999, 266:135-140.
    • (1999) Biochem. Biophys. Res. Commun. , vol.266 , pp. 135-140
    • McCann, R.O.1    Craig, S.W.2
  • 77
    • 77957237697 scopus 로고    scopus 로고
    • Frontiers of microscopy-based research into cell-matrix adhesions
    • Medalia O., Geiger B. Frontiers of microscopy-based research into cell-matrix adhesions. Curr. Opin. Cell Biol. 2010, 22:659-668.
    • (2010) Curr. Opin. Cell Biol. , vol.22 , pp. 659-668
    • Medalia, O.1    Geiger, B.2
  • 79
    • 77955580383 scopus 로고    scopus 로고
    • Stretchy proteins on stretchy substrates: the important elements of integrin-mediated rigidity sensing
    • Moore S.W., Roca-Cusachs P., Sheetz M.P. Stretchy proteins on stretchy substrates: the important elements of integrin-mediated rigidity sensing. Dev. Cell 2010, 19:194-206.
    • (2010) Dev. Cell , vol.19 , pp. 194-206
    • Moore, S.W.1    Roca-Cusachs, P.2    Sheetz, M.P.3
  • 80
    • 40449133970 scopus 로고    scopus 로고
    • Kindlin-3 is essential for integrin activation and platelet aggregation
    • Moser M., Nieswandt B., Ussar S., Pozgajova M., Fässler R. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat. Med. 2008, 14:325-330.
    • (2008) Nat. Med. , vol.14 , pp. 325-330
    • Moser, M.1    Nieswandt, B.2    Ussar, S.3    Pozgajova, M.4    Fässler, R.5
  • 82
    • 11844259978 scopus 로고    scopus 로고
    • Loss of synchronized retinal phagocytosis and age-related blindness in mice lacking alphavbeta5 integrin
    • Nandrot E.F., Kim Y., Brodie S.E., Huang X., Sheppard D., Finnemann S.C. Loss of synchronized retinal phagocytosis and age-related blindness in mice lacking alphavbeta5 integrin. J. Exp. Med. 2004, 200:1539-1545.
    • (2004) J. Exp. Med. , vol.200 , pp. 1539-1545
    • Nandrot, E.F.1    Kim, Y.2    Brodie, S.E.3    Huang, X.4    Sheppard, D.5    Finnemann, S.C.6
  • 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 1995, 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 85
    • 84859387007 scopus 로고    scopus 로고
    • Tension is required but not sufficient for focal adhesion maturation without a stress fiber template
    • Oakes P.W., Beckham Y., Stricker J., Gardel M.L. Tension is required but not sufficient for focal adhesion maturation without a stress fiber template. J. Cell Biol. 2012, 196:363-374.
    • (2012) J. Cell Biol. , vol.196 , pp. 363-374
    • Oakes, P.W.1    Beckham, Y.2    Stricker, J.3    Gardel, M.L.4
  • 86
    • 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
  • 87
    • 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. 2010, 188:877-890.
    • (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
  • 89
    • 0344912596 scopus 로고    scopus 로고
    • Cell locomotion and focal adhesions are regulated by substrate flexibility
    • Pelham R.J., Wang Yl. Cell locomotion and focal adhesions are regulated by substrate flexibility. Proc. Natl. Acad. Sci. USA 1997, 94:13661-13665.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13661-13665
    • Pelham, R.J.1    Wang, Y.2
  • 93
    • 0014291872 scopus 로고
    • An analysis of cytokinesis in cultured newt cells
    • Rappaport R., Rappaport B.N. An analysis of cytokinesis in cultured newt cells. J. Exp. Zool. 1968, 168:187-195.
    • (1968) J. Exp. Zool. , vol.168 , pp. 187-195
    • Rappaport, R.1    Rappaport, B.N.2
  • 94
    • 0017386479 scopus 로고
    • Control of grip and stick in cell adhesion through lateral relationships of membrane glycoproteins
    • Rees D.A., Lloyd C.W., Thom D. Control of grip and stick in cell adhesion through lateral relationships of membrane glycoproteins. Nature 1977, 267:124-128.
    • (1977) Nature , vol.267 , pp. 124-128
    • Rees, D.A.1    Lloyd, C.W.2    Thom, D.3
  • 95
    • 0015939511 scopus 로고
    • Electronmicroscope investigations of the underside of cells in culture
    • Revel J.P., Wolken K. Electronmicroscope investigations of the underside of cells in culture. Exp. Cell Res. 1973, 78:1-14.
    • (1973) Exp. Cell Res. , vol.78 , pp. 1-14
    • Revel, J.P.1    Wolken, K.2
  • 96
    • 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
  • 97
    • 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. USA 2009, 106:16245-16250.
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 16245-16250
    • Roca-Cusachs, P.1    Gauthier, N.C.2    Del Rio, A.3    Sheetz, M.P.4
  • 98
    • 0034632070 scopus 로고    scopus 로고
    • The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane
    • Rogalski T.M., Mullen G.P., Gilbert M.M., Williams B.D., Moerman D.G. The UNC-112 gene in Caenorhabditis elegans encodes a novel component of cell-matrix adhesion structures required for integrin localization in the muscle cell membrane. J. Cell Biol. 2000, 150:253-264.
    • (2000) J. Cell Biol. , vol.150 , pp. 253-264
    • Rogalski, T.M.1    Mullen, G.P.2    Gilbert, M.M.3    Williams, B.D.4    Moerman, D.G.5
  • 99
    • 0346481004 scopus 로고
    • Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product
    • Rohrschneider L.R. Adhesion plaques of Rous sarcoma virus-transformed cells contain the src gene product. Proc. Natl. Acad. Sci. USA 1980, 77:3514-3518.
    • (1980) Proc. Natl. Acad. Sci. USA , vol.77 , pp. 3514-3518
    • Rohrschneider, L.R.1
  • 100
    • 0033577975 scopus 로고    scopus 로고
    • Interplay between Rac and Rho in the control of substrate contact dynamics
    • Rottner K., Hall A., Small J.V. Interplay between Rac and Rho in the control of substrate contact dynamics. Curr. Biol. 1999, 9:640-648.
    • (1999) Curr. Biol. , vol.9 , pp. 640-648
    • Rottner, K.1    Hall, A.2    Small, J.V.3
  • 101
    • 84979948588 scopus 로고
    • A sarcoma of the fowl transmissible by an agent separable from the tumor cells
    • Rous P. A sarcoma of the fowl transmissible by an agent separable from the tumor cells. J. Exp. Med. 1911, 13:397-411.
    • (1911) J. Exp. Med. , vol.13 , pp. 397-411
    • Rous, P.1
  • 102
    • 0027990414 scopus 로고
    • A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner
    • Sakai R., Iwamatsu A., Hirano N., Ogawa S., Tanaka T., Mano H., Yazaki Y., Hirai H. A novel signaling molecule, p130, forms stable complexes in vivo with v-Crk and v-Src in a tyrosine phosphorylation-dependent manner. EMBO J. 1994, 13:3748-3756.
    • (1994) EMBO J. , vol.13 , pp. 3748-3756
    • Sakai, R.1    Iwamatsu, A.2    Hirano, N.3    Ogawa, S.4    Tanaka, T.5    Mano, H.6    Yazaki, Y.7    Hirai, H.8
  • 103
    • 79958735965 scopus 로고    scopus 로고
    • Actomyosin-mediated cellular tension drives increased tissue stiffness and β-catenin activation to induce epidermal hyperplasia and tumor growth
    • Samuel M.S., Lopez J.I., McGhee E.J., Croft D.R., Strachan D., Timpson P., Munro J., Schröder E., Zhou J., Brunton V.G., et al. Actomyosin-mediated cellular tension drives increased tissue stiffness and β-catenin activation to induce epidermal hyperplasia and tumor growth. Cancer Cell 2011, 19:776-791.
    • (2011) Cancer Cell , vol.19 , pp. 776-791
    • Samuel, M.S.1    Lopez, J.I.2    McGhee, E.J.3    Croft, D.R.4    Strachan, D.5    Timpson, P.6    Munro, J.7    Schröder, E.8    Zhou, J.9    Brunton, V.G.10
  • 104
    • 0020673112 scopus 로고
    • Roles of extracellular matrix in neural development
    • Sanes J.R. Roles of extracellular matrix in neural development. Annu. Rev. Physiol. 1983, 45:581-600.
    • (1983) Annu. Rev. Physiol. , vol.45 , pp. 581-600
    • Sanes, J.R.1
  • 107
    • 79952283069 scopus 로고    scopus 로고
    • Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins
    • Schiller H.B., Friedel C.C., Boulegue C., Fässler R. Quantitative proteomics of the integrin adhesome show a myosin II-dependent recruitment of LIM domain proteins. EMBO Rep. 2011, 12:259-266.
    • (2011) EMBO Rep. , vol.12 , pp. 259-266
    • Schiller, H.B.1    Friedel, C.C.2    Boulegue, C.3    Fässler, R.4
  • 108
    • 39549084168 scopus 로고    scopus 로고
    • Substrate rigidity modulates cell matrix interactions and protein expression in human trabecular meshwork cells
    • Schlunck G., Han H., Wecker T., Kampik D., Meyer-ter-Vehn T., Grehn F. Substrate rigidity modulates cell matrix interactions and protein expression in human trabecular meshwork cells. Invest. Ophthalmol. Vis. Sci. 2008, 49:262-269.
    • (2008) Invest. Ophthalmol. Vis. Sci. , vol.49 , pp. 262-269
    • Schlunck, G.1    Han, H.2    Wecker, T.3    Kampik, D.4    Meyer-ter-Vehn, T.5    Grehn, F.6
  • 110
    • 79952580461 scopus 로고    scopus 로고
    • Nanolithographic control of the spatial organization of cellular adhesion receptors at the single-molecule level
    • Schvartzman M., Palma M., Sable J., Abramson J., Hu X., Sheetz M.P., Wind S.J. Nanolithographic control of the spatial organization of cellular adhesion receptors at the single-molecule level. Nano Lett. 2011, 11:1306-1312.
    • (2011) Nano Lett. , vol.11 , pp. 1306-1312
    • Schvartzman, M.1    Palma, M.2    Sable, J.3    Abramson, J.4    Hu, X.5    Sheetz, M.P.6    Wind, S.J.7
  • 114
    • 0018344535 scopus 로고
    • The fibronexus: a transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts
    • Singer I.I. The fibronexus: a transmembrane association of fibronectin-containing fibers and bundles of 5 nm microfilaments in hamster and human fibroblasts. Cell 1979, 16:675-685.
    • (1979) Cell , vol.16 , pp. 675-685
    • Singer, I.I.1
  • 115
    • 0014418101 scopus 로고
    • Anchorage and growth regulation in normal and virus-transformed cells
    • Stoker M., O'Neill C., Berryman S., Waxman V. Anchorage and growth regulation in normal and virus-transformed cells. Int. J. Cancer 1968, 3:683-693.
    • (1968) Int. J. Cancer , vol.3 , pp. 683-693
    • Stoker, M.1    O'Neill, C.2    Berryman, S.3    Waxman, V.4
  • 116
    • 0001726468 scopus 로고
    • Characteristics of an assay for Rous sarcoma virus and Rous sarcoma cells in tissue culture
    • Temin H.M., Rubin H. Characteristics of an assay for Rous sarcoma virus and Rous sarcoma cells in tissue culture. Virology 1958, 6:669-688.
    • (1958) Virology , vol.6 , pp. 669-688
    • Temin, H.M.1    Rubin, H.2
  • 118
    • 0022166122 scopus 로고
    • Cell migration in the vertebrate embryo: role of cell adhesion and tissue environment in pattern formation
    • Thiery J.P., Duband J.L., Tucker G.C. Cell migration in the vertebrate embryo: role of cell adhesion and tissue environment in pattern formation. Annu. Rev. Cell Biol. 1985, 1:91-113.
    • (1985) Annu. Rev. Cell Biol. , vol.1 , pp. 91-113
    • Thiery, J.P.1    Duband, J.L.2    Tucker, G.C.3
  • 119
    • 0018331208 scopus 로고
    • Mechanisms of cellular adhesion. IV. Role of serum glycoproteins in fibroblast spreading on glass
    • Thom D., Powell A.J., Rees D.A. Mechanisms of cellular adhesion. IV. Role of serum glycoproteins in fibroblast spreading on glass. J. Cell Sci. 1979, 35:281-305.
    • (1979) J. Cell Sci. , vol.35 , pp. 281-305
    • Thom, D.1    Powell, A.J.2    Rees, D.A.3
  • 122
    • 84867530808 scopus 로고    scopus 로고
    • Functional analysis of parvin and different modes of IPP-complex assembly at integrin sites during Drosophila development
    • Vakaloglou K.M., Chountala M., Zervas C.G. Functional analysis of parvin and different modes of IPP-complex assembly at integrin sites during Drosophila development. J. Cell Sci. 2012, 125:3221-3232.
    • (2012) J. Cell Sci. , vol.125 , pp. 3221-3232
    • Vakaloglou, K.M.1    Chountala, M.2    Zervas, C.G.3
  • 124
    • 60749130274 scopus 로고    scopus 로고
    • Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways
    • Vogel V., Sheetz M.P. Cell fate regulation by coupling mechanical cycles to biochemical signaling pathways. Curr. Opin. Cell Biol. 2009, 21:38-46.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 38-46
    • Vogel, V.1    Sheetz, M.P.2
  • 125
    • 0025153883 scopus 로고
    • A role for integrin in the formation of sarcomeric cytoarchitecture
    • Volk T., Fessler L.I., Fessler J.H. A role for integrin in the formation of sarcomeric cytoarchitecture. Cell 1990, 63:525-536.
    • (1990) Cell , vol.63 , pp. 525-536
    • Volk, T.1    Fessler, L.I.2    Fessler, J.H.3
  • 126
    • 15144341744 scopus 로고
    • Coincidence of Crossing over in DROSOPHILA MELANOGASTER (AMPELOPHILA)
    • Weinstein A. Coincidence of Crossing over in DROSOPHILA MELANOGASTER (AMPELOPHILA). Genetics 1918, 3:135-172.
    • (1918) Genetics , vol.3 , pp. 135-172
    • Weinstein, A.1
  • 127
    • 0025610114 scopus 로고
    • Genetic analysis of the Drosophila PS integrins
    • Wilcox M. Genetic analysis of the Drosophila PS integrins. Cell Differ. Dev. 1990, 32:391-399.
    • (1990) Cell Differ. Dev. , vol.32 , pp. 391-399
    • Wilcox, M.1
  • 128
    • 70350235056 scopus 로고    scopus 로고
    • The heel and toe of the cell's foot: a multifaceted approach for understanding the structure and dynamics of focal adhesions
    • Wolfenson H., Henis Y.I., Geiger B., Bershadsky A.D. The heel and toe of the cell's foot: a multifaceted approach for understanding the structure and dynamics of focal adhesions. Cell Motil. Cytoskeleton 2009, 66:1017-1029.
    • (2009) Cell Motil. Cytoskeleton , vol.66 , pp. 1017-1029
    • Wolfenson, H.1    Henis, Y.I.2    Geiger, B.3    Bershadsky, A.D.4
  • 129
    • 59349095056 scopus 로고    scopus 로고
    • A role for the juxtamembrane cytoplasm in the molecular dynamics of focal adhesions
    • Wolfenson H., Lubelski A., Regev T., Klafter J., Henis Y.I., Geiger B. A role for the juxtamembrane cytoplasm in the molecular dynamics of focal adhesions. PLoS ONE 2009, 4:e4304.
    • (2009) PLoS ONE , vol.4
    • Wolfenson, H.1    Lubelski, A.2    Regev, T.3    Klafter, J.4    Henis, Y.I.5    Geiger, B.6
  • 130
    • 79955538660 scopus 로고    scopus 로고
    • Actomyosin-generated tension controls the molecular kinetics of focal adhesions
    • Wolfenson H., Bershadsky A., Henis Y.I., Geiger B. Actomyosin-generated tension controls the molecular kinetics of focal adhesions. J. Cell Sci. 2011, 124:1425-1432.
    • (2011) J. Cell Sci. , vol.124 , pp. 1425-1432
    • Wolfenson, H.1    Bershadsky, A.2    Henis, Y.I.3    Geiger, B.4
  • 132
    • 0035374569 scopus 로고    scopus 로고
    • RhoA inhibits the nerve growth factor-induced Rac1 activation through Rho-associated kinase-dependent pathway
    • Yamaguchi Y., Katoh H., Yasui H., Mori K., Negishi M. RhoA inhibits the nerve growth factor-induced Rac1 activation through Rho-associated kinase-dependent pathway. J. Biol. Chem. 2001, 276:18977-18983.
    • (2001) J. Biol. Chem. , vol.276 , pp. 18977-18983
    • Yamaguchi, Y.1    Katoh, H.2    Yasui, H.3    Mori, K.4    Negishi, M.5
  • 133
    • 0035836726 scopus 로고    scopus 로고
    • Extracellular matrix composition determines the transcriptional response to epidermal growth factor receptor activation
    • Yarwood S.J., Woodgett J.R. Extracellular matrix composition determines the transcriptional response to epidermal growth factor receptor activation. Proc. Natl. Acad. Sci. USA 2001, 98:4472-4477.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 4472-4477
    • Yarwood, S.J.1    Woodgett, J.R.2
  • 134
    • 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., 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 2011, 108:20585-20590.
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20585-20590
    • Yu, C.H.1    Law, J.B.2    Suryana, M.3    Low, H.Y.4    Sheetz, M.P.5
  • 135
    • 77951737987 scopus 로고    scopus 로고
    • The switchable integrin adhesome
    • Zaidel-Bar R., Geiger B. The switchable integrin adhesome. J. Cell Sci. 2010, 123:1385-1388.
    • (2010) J. Cell Sci. , vol.123 , pp. 1385-1388
    • Zaidel-Bar, R.1    Geiger, B.2
  • 136
    • 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. 2003, 116:4605-4613.
    • (2003) J. Cell Sci. , vol.116 , pp. 4605-4613
    • Zaidel-Bar, R.1    Ballestrem, C.2    Kam, Z.3    Geiger, B.4
  • 139
    • 33846781373 scopus 로고    scopus 로고
    • A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions
    • Zaidel-Bar R., Milo R., Kam Z., Geiger B. A paxillin tyrosine phosphorylation switch regulates the assembly and form of cell-matrix adhesions. J. Cell Sci. 2007, 120:137-148.
    • (2007) J. Cell Sci. , vol.120 , pp. 137-148
    • Zaidel-Bar, R.1    Milo, R.2    Kam, Z.3    Geiger, B.4
  • 141
    • 0035809918 scopus 로고    scopus 로고
    • Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane
    • Zervas C.G., Gregory S.L., Brown N.H. Drosophila integrin-linked kinase is required at sites of integrin adhesion to link the cytoskeleton to the plasma membrane. J. Cell Biol. 2001, 152:1007-1018.
    • (2001) J. Cell Biol. , vol.152 , pp. 1007-1018
    • Zervas, C.G.1    Gregory, S.L.2    Brown, N.H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.