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Volumn 3, Issue 2, 2011, Pages 1-22

Genetic analyses of integrin signaling

Author keywords

[No Author keywords available]

Indexed keywords

EUKARYOTA; MUS;

EID: 84857400630     PISSN: None     EISSN: 19430264     Source Type: Journal    
DOI: 10.1101/cshperspect.a005116     Document Type: Review
Times cited : (76)

References (156)
  • 1
    • 34547757016 scopus 로고    scopus 로고
    • Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects
    • Ackerl R, Walko G, Fuchs P, Fischer I, Schmuth M, Wiche G. 2007. Conditional targeting of plectin in prenatal and adult mouse stratified epithelia causes keratinocyte fragility and lesional epidermal barrier defects. J Cell Sci 120: 2435-2443.
    • (2007) J Cell Sci , vol.120 , pp. 2435-2443
    • Ackerl, R.1    Walko, G.2    Fuchs, P.3    Fischer, I.4    Schmuth, M.5    Wiche, G.6
  • 2
    • 0141670816 scopus 로고    scopus 로고
    • LAD-III, a novel group of leukocyte integrin activation deficiencies
    • Alon R, Etzioni A. 2003. LAD-III, a novel group of leukocyte integrin activation deficiencies. Trends Immunol 24: 561-566.
    • (2003) Trends Immunol , vol.24 , pp. 561-566
    • Alon, R.1    Etzioni, A.2
  • 3
    • 0035354189 scopus 로고    scopus 로고
    • Protein kinase Cd-mediated phosphorylation of α6β4 is associated with reduced integrin localization to the hemidesmosome and decreased keratinocyte attachment
    • Alt A, Ohba M, Li L, Gartsbein M, Belanger A, Denning MF, Kuroki T, Yuspa SH, TennenbaumT. 2001. Protein kinase Cd-mediated phosphorylation of α6β4 is associated with reduced integrin localization to the hemidesmosome and decreased keratinocyte attachment. Cancer Res 61: 4591-4598.
    • (2001) Cancer Res , vol.61 , pp. 4591-4598
    • Alt, A.1    Ohba, M.2    Li, L.3    Gartsbein, M.4    Belanger, A.5    Denning, M.F.6    Kuroki, T.7    Yuspa, S.H.8    Tennenbaum, T.9
  • 4
    • 0030721040 scopus 로고    scopus 로고
    • Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture
    • Andra K, Lassmann H, Bittner R, Shorny S, Fässler R, Propst F, Wiche G. 1997. Targeted inactivation of plectin reveals essential function in maintaining the integrity of skin, muscle, and heart cytoarchitecture. Genes Dev 11: 3143-3156.
    • (1997) Genes Dev , vol.11 , pp. 3143-3156
    • Andra, K.1    Lassmann, H.2    Bittner, R.3    Shorny, S.4    Fässler, R.5    Propst, F.6    Wiche, G.7
  • 5
    • 0031577559 scopus 로고    scopus 로고
    • Targeted disruption of exon 52 in the mouse dystrophin gene induced muscle degeneration similar to that observed in Duchenne muscular dystrophy
    • Araki E, Nakamura K, Nakao K, Kameya S, Kobayashi O, Nonaka I, Kobayashi T, Katsuki M. 1997. Targeted disruption of exon 52 in the mouse dystrophin gene induced muscle degeneration similar to that observed in Duchenne muscular dystrophy. Biochem Biophys Res Commun 238: 492-497.
    • (1997) Biochem Biophys Res Commun , vol.238 , pp. 492-497
    • Araki, E.1    Nakamura, K.2    Nakao, K.3    Kameya, S.4    Kobayashi, O.5    Nonaka, I.6    Kobayashi, T.7    Katsuki, M.8
  • 6
    • 35348890874 scopus 로고    scopus 로고
    • Multiple cardiovascular defects caused by the absence of alternatively spliced segments of fibronectin
    • Astrof S, Crowley D, Hynes RO. 2007. Multiple cardiovascular defects caused by the absence of alternatively spliced segments of fibronectin. Dev Biol 311: 11-24.
    • (2007) Dev Biol , vol.311 , pp. 11-24
    • Astrof, S.1    Crowley, D.2    Hynes, R.O.3
  • 7
    • 0032514841 scopus 로고    scopus 로고
    • Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all αv integrins
    • Bader BL, Rayburn H, Crowley D, Hynes RO. 1998. Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all αv integrins. Cell 95: 507-519.
    • (1998) Cell , vol.95 , pp. 507-519
    • Bader, B.L.1    Rayburn, H.2    Crowley, D.3    Hynes, R.O.4
  • 8
    • 60549086393 scopus 로고    scopus 로고
    • Beta1 integrins differentially control extravasation of inflammatory cell subsets into the CNS during autoimmunity
    • Bauer M, Brakebusch C, Coisne C, Sixt M, Wekerle H, Engelhardt B, Fässler R. 2009. Beta1 integrins differentially control extravasation of inflammatory cell subsets into the CNS during autoimmunity. Proc Natl Acad Sci 106: 1920-1925.
    • (2009) Proc Natl Acad Sci , vol.106 , pp. 1920-1925
    • Bauer, M.1    Brakebusch, C.2    Coisne, C.3    Sixt, M.4    Wekerle, H.5    Engelhardt, B.6    Fässler, R.7
  • 10
    • 33845697707 scopus 로고    scopus 로고
    • β4 integrin activates a Shp2-Src signaling pathway that sustains HGF-induced anchorage-independent growth
    • Bertotti A, Comoglio PM, Trusolino L. 2006. β4 integrin activates a Shp2-Src signaling pathway that sustains HGF-induced anchorage-independent growth. J Cell Biol 175: 993-1003.
    • (2006) J Cell Biol , vol.175 , pp. 993-1003
    • Bertotti, A.1    Comoglio, P.M.2    Trusolino, L.3
  • 12
    • 0031760509 scopus 로고    scopus 로고
    • Collagen VI deficiency induces early onset myopathy in the mouse: An animal model for Bethlem myopathy
    • Bonaldo P, Braghetta P, Zanetti M, Piccolo S, VolpinD, Bressan GM. 1998. Collagen VI deficiency induces early onset myopathy in the mouse: An animal model for Bethlem myopathy. Hum Mol Genet 7: 2135-2140.
    • (1998) Hum Mol Genet , vol.7 , pp. 2135-2140
    • Bonaldo, P.1    Braghetta, P.2    Zanetti, M.3    Piccolo, S.4    Volpin, D.5    Bressan, G.M.6
  • 17
    • 84863900703 scopus 로고    scopus 로고
    • Integrin structure, activation, and interactions
    • doi: 10.1101/cshperspect.a004994
    • Campbell ID, Humphries MJ. 2011. Integrin structure, activation, and interactions. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a004994.
    • (2011) Cold Spring Harb Perspect Biol
    • Campbell, I.D.1    Humphries, M.J.2
  • 18
    • 0035809198 scopus 로고    scopus 로고
    • An inducible mouse model for epidermolysis bullosa simplex: Implications for gene therapy
    • Cao T, Longley MA, Wang XJ, Roop DR. 2001. An inducible mouse model for epidermolysis bullosa simplex: Implications for gene therapy. J Cell Biol 152: 651-656.
    • (2001) J Cell Biol , vol.152 , pp. 651-656
    • Cao, T.1    Longley, M.A.2    Wang, X.J.3    Roop, D.R.4
  • 19
    • 0024580709 scopus 로고
    • Recovery of induced mutations for X chromosomelinked muscular dystrophy in mice
    • Chapman VM, Miller DR, Armstrong D, Caskey CT. 1989. Recovery of induced mutations for X chromosomelinked muscular dystrophy in mice. Proc Natl Acad Sci 86: 1292-1296.
    • (1989) Proc Natl Acad Sci , vol.86 , pp. 1292-1296
    • Chapman, V.M.1    Miller, D.R.2    Armstrong, D.3    Caskey, C.T.4
  • 24
    • 67349092209 scopus 로고    scopus 로고
    • Structural basis of the interaction between integrin α6β4 and plectin at the hemidesmosomes
    • de Pereda JM, Lillo MP, Sonnenberg A. 2009. Structural basis of the interaction between integrin α6β4 and plectin at the hemidesmosomes. EMBO J 28: 1180-1190.
    • (2009) EMBO J , vol.28 , pp. 1180-1190
    • de Pereda, J.M.1    Lillo, M.P.2    Sonnenberg, A.3
  • 25
    • 0033828682 scopus 로고    scopus 로고
    • αa3β1 and α6β4 integrin receptors for laminin-5 are not essential for epidermal morphogenesis and homeostasis during skin development
    • DiPersio CM, van der Neut R, Georges-Labouesse E, Kreidberg JA, Sonnenberg A, Hynes RO. 2000. αa3β1 and α6β4 integrin receptors for laminin-5 are not essential for epidermal morphogenesis and homeostasis during skin development. J Cell Sci 113: 3051-3062.
    • (2000) J Cell Sci , vol.113 , pp. 3051-3062
    • DiPersio, C.M.1    van der Neut, R.2    Georges-Labouesse, E.3    Kreidberg, J.A.4    Sonnenberg, A.5    Hynes, R.O.6
  • 26
    • 0029666420 scopus 로고    scopus 로고
    • βa4 integrin is required for hemidesmosome formation, cell adhesion and cell survival
    • Dowling J, Yu QC, Fuchs E. 1996. βa4 integrin is required for hemidesmosome formation, cell adhesion and cell survival. J Cell Biol 134: 559-572.
    • (1996) J Cell Biol , vol.134 , pp. 559-572
    • Dowling, J.1    Yu, Q.C.2    Fuchs, E.3
  • 29
    • 0033808066 scopus 로고    scopus 로고
    • Still more complexity in mammalian basement membranes
    • Erickson AC, Couchman JR. 2000. Still more complexity in mammalian basement membranes. J Histochem Cytochem 48: 1291-1306.
    • (2000) J Histochem Cytochem , vol.48 , pp. 1291-1306
    • Erickson, A.C.1    Couchman, J.R.2
  • 31
    • 0345803932 scopus 로고    scopus 로고
    • PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival
    • Fukuda T, Chen K, Shi X, Wu C. 2003. PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival. J Biol Chem 278: 51324-51333.
    • (2003) J Biol Chem , vol.278 , pp. 51324-51333
    • Fukuda, T.1    Chen, K.2    Shi, X.3    Wu, C.4
  • 35
    • 80053298724 scopus 로고    scopus 로고
    • Molecular architecture and function of matrix adhesions
    • doi: 10.1101/cshperspect.a005033
    • Geiger B, Yamada KM. 2011. Molecular architecture and function of matrix adhesions. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a005033.
    • (2011) Cold Spring Harb Perspect Biol
    • Geiger, B.1    Yamada, K.M.2
  • 36
    • 0030818072 scopus 로고    scopus 로고
    • Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells
    • George EL, Baldwin HS, Hynes RO. 1997. Fibronectins are essential for heart and blood vessel morphogenesis but are dispensable for initial specification of precursor cells. Blood 90: 3073-3081.
    • (1997) Blood , vol.90 , pp. 3073-3081
    • George, E.L.1    Baldwin, H.S.2    Hynes, R.O.3
  • 37
    • 0027379724 scopus 로고
    • Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin
    • George EL, Georges-Labouesse EN, Patel-King RS, Rayburn H, Hynes RO. 1993. Defects in mesoderm, neural tube and vascular development in mouse embryos lacking fibronectin. Development 119: 1079-1091.
    • (1993) Development , vol.119 , pp. 1079-1091
    • George, E.L.1    Georges-Labouesse, E.N.2    Patel-King, R.S.3    Rayburn, H.4    Hynes, R.O.5
  • 38
  • 40
    • 0036854284 scopus 로고    scopus 로고
    • Dynamics of the alpha6-beta4 integrin in keratinocytes
    • Geuijen CA, Sonnenberg A. 2002. Dynamics of the alpha6-beta4 integrin in keratinocytes. Mol Biol Cell 13: 3845-3858.
    • (2002) Mol Biol Cell , vol.13 , pp. 3845-3858
    • Geuijen, C.A.1    Sonnenberg, A.2
  • 41
    • 34748863597 scopus 로고    scopus 로고
    • Targeting integrin β4 for cancer and anti-angiogenic therapy
    • Giancotti FG. 2007. Targeting integrin β4 for cancer and anti-angiogenic therapy. Trends Pharmacol Sci 28: 506-511.
    • (2007) Trends Pharmacol Sci , vol.28 , pp. 506-511
    • Giancotti, F.G.1
  • 42
    • 0025124607 scopus 로고
    • Lymphoid cells recognize an alternatively spliced segment of fibronectin via the integrin receptor α4 β1
    • Guan JL, Hynes RO. 1990. Lymphoid cells recognize an alternatively spliced segment of fibronectin via the integrin receptor α4 β1. Cell 60: 53-61.
    • (1990) Cell , vol.60 , pp. 53-61
    • Guan, J.L.1    Hynes, R.O.2
  • 43
    • 0029066406 scopus 로고
    • Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration
    • Guo L, Degenstein L, Dowling J, Yu QC, Wollmann R, Perman B, Fuchs E. 1995. Gene targeting of BPAG1: Abnormalities in mechanical strength and cell migration in stratified epithelia and neurologic degeneration. Cell 81: 233-243.
    • (1995) Cell , vol.81 , pp. 233-243
    • Guo, L.1    Degenstein, L.2    Dowling, J.3    Yu, Q.C.4    Wollmann, R.5    Perman, B.6    Fuchs, E.7
  • 45
    • 0032717715 scopus 로고    scopus 로고
    • Targeted inactivation of the type VII collagen gene (Col7a1) in mice results in severe blistering phenotype: A model for recessive dystrophic epidermolysis bullosa
    • Heinonen S, Mannikko M, Klement JF, Whitaker-Menezes D, Murphy GF, Uitto J. 1999. Targeted inactivation of the type VII collagen gene (Col7a1) in mice results in severe blistering phenotype: A model for recessive dystrophic epidermolysis bullosa. J Cell Sci 112: 3641-3648.
    • (1999) J Cell Sci , vol.112 , pp. 3641-3648
    • Heinonen, S.1    Mannikko, M.2    Klement, J.F.3    Whitaker-Menezes, D.4    Murphy, G.F.5    Uitto, J.6
  • 49
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO. 2002. Integrins: Bidirectional, allosteric signaling machines. Cell 110: 673-687.
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 50
    • 70849099495 scopus 로고    scopus 로고
    • The extracellular matrix: Not just pretty fibrils
    • Hynes RO. 2009. The extracellular matrix: Not just pretty fibrils. Science 326: 1216-1219.
    • (2009) Science , vol.326 , pp. 1216-1219
    • Hynes, R.O.1
  • 51
    • 72449124139 scopus 로고    scopus 로고
    • Interplay between cell adhesion and growth factor receptors: From the plasma membrane to the endosomes
    • Ivaska J, Heino J. 2010. Interplay between cell adhesion and growth factor receptors: From the plasma membrane to the endosomes. Cell Tissue Res 339: 111-120.
    • (2010) Cell Tissue Res , vol.339 , pp. 111-120
    • Ivaska, J.1    Heino, J.2
  • 52
    • 33750070428 scopus 로고    scopus 로고
    • The genetic and molecular basis of muscular dystrophy: Roles of cell-matrix linkage in the pathogenesis
    • Kanagawa M, Toda T. 2006. The genetic and molecular basis of muscular dystrophy: Roles of cell-matrix linkage in the pathogenesis. J Hum Genet 51: 915-926.
    • (2006) J Hum Genet , vol.51 , pp. 915-926
    • Kanagawa, M.1    Toda, T.2
  • 53
    • 64549156956 scopus 로고    scopus 로고
    • Glanzmann's thrombasthenia: An overview
    • Kannan M, Saxena R. 2009. Glanzmann's thrombasthenia: An overview. Clin Appl Thromb Hemost 15: 152-165.
    • (2009) Clin Appl Thromb Hemost , vol.15 , pp. 152-165
    • Kannan, M.1    Saxena, R.2
  • 54
    • 0019410292 scopus 로고
    • Analysis of surface proteins of mouse lung carcinomas using monoclonal antibodies
    • Kennel SJ, Foote LJ, Lankford PK. 1981. Analysis of surface proteins of mouse lung carcinomas using monoclonal antibodies. Cancer Res 41: 3465-3470.
    • (1981) Cancer Res , vol.41 , pp. 3465-3470
    • Kennel, S.J.1    Foote, L.J.2    Lankford, P.K.3
  • 55
    • 70349614410 scopus 로고    scopus 로고
    • Integrin-linked kinase controls vascular wall formation by negatively regulating Rho/ROCK-mediated vascular smooth muscle cell contraction
    • Kogata N, Tribe RM, Fässler R, Way M, Adams RH. 2009. Integrin-linked kinase controls vascular wall formation by negatively regulating Rho/ROCK-mediated vascular smooth muscle cell contraction. Genes Dev 23: 2278-2283.
    • (2009) Genes Dev , vol.23 , pp. 2278-2283
    • Kogata, N.1    Tribe, R.M.2    Fässler, R.3    Way, M.4    Adams, R.H.5
  • 56
    • 0035670672 scopus 로고    scopus 로고
    • Two different mutations in the cytoplasmic domain of the integrin β4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of β4 with plectin
    • Koster J, Kuikman I, Kreft M, Sonnenberg A. 2001. Two different mutations in the cytoplasmic domain of the integrin β4 subunit in nonlethal forms of epidermolysis bullosa prevent interaction of β4 with plectin. J Invest Dermatol 117: 1405-1411.
    • (2001) J Invest Dermatol , vol.117 , pp. 1405-1411
    • Koster, J.1    Kuikman, I.2    Kreft, M.3    Sonnenberg, A.4
  • 57
    • 1542344031 scopus 로고    scopus 로고
    • Role of binding of plectin to the integrin β4 subunit in the assembly of hemidesmosomes
    • Koster J, vanWilpe S, Kuikman I, Litjens SH, Sonnenberg A. 2004. Role of binding of plectin to the integrin β4 subunit in the assembly of hemidesmosomes. Mol Biol Cell 15: 1211-1223.
    • (2004) Mol Biol Cell , vol.15 , pp. 1211-1223
    • Koster, J.1    vanWilpe, S.2    Kuikman, I.3    Litjens, S.H.4    Sonnenberg, A.5
  • 58
    • 0032528845 scopus 로고    scopus 로고
    • Merosin-deficient congenital muscular dystrophy. Partial genetic correction in two mouse models
    • Kuang W, Xu H, Vachon PH, Liu L, Loechel F, Wewer UM, Engvall E. 1998. Merosin-deficient congenital muscular dystrophy. Partial genetic correction in two mouse models. J Clin Invest 102: 844-852.
    • (1998) J Clin Invest , vol.102 , pp. 844-852
    • Kuang, W.1    Xu, H.2    Vachon, P.H.3    Liu, L.4    Loechel, F.5    Wewer, U.M.6    Engvall, E.7
  • 59
    • 0030885763 scopus 로고    scopus 로고
    • Leukocyte adhesion deficiency type 1 (LAD-1)/variant. A novel immunodeficiency syndrome characterized by dysfunctional beta2 integrins
    • KuijpersTW, Van Lier RA, HamannD, de Boer M, Thung LY, Weening RS, Verhoeven AJ, Roos D. 1997. Leukocyte adhesion deficiency type 1 (LAD-1)/variant. A novel immunodeficiency syndrome characterized by dysfunctional beta2 integrins. J Clin Invest 100: 1725-1733.
    • (1997) J Clin Invest , vol.100 , pp. 1725-1733
    • Kuijpers, T.W.1    van Lier, R.A.2    Hamann, D.3    de Boer, M.4    Thung, L.Y.5    Weening, R.S.6    Verhoeven, A.J.7    Roos, D.8
  • 61
    • 0031229599 scopus 로고    scopus 로고
    • IAP insertion in the murine LamB3 gene results in junctional epidermolysis bullosa
    • Kuster JE, Guarnieri MH, Ault JG, Flaherty L, Swiatek PJ. 1997. IAP insertion in the murine LamB3 gene results in junctional epidermolysis bullosa. Mamm Genome 8: 673-681.
    • (1997) Mamm Genome , vol.8 , pp. 673-681
    • Kuster, J.E.1    Guarnieri, M.H.2    Ault, J.G.3    Flaherty, L.4    Swiatek, P.J.5
  • 62
    • 0028952534 scopus 로고
    • Defective development of the embryonic and extraembryonic circulatory systems in vascular cell adhesion molecule (VCAM-1) deficient mice
    • Kwee L, Baldwin HS, Shen HM, Stewart CL, Buck C, Buck CA, Labow MA. 1995. Defective development of the embryonic and extraembryonic circulatory systems in vascular cell adhesion molecule (VCAM-1) deficient mice. Development 121: 489-503.
    • (1995) Development , vol.121 , pp. 489-503
    • Kwee, L.1    Baldwin, H.S.2    Shen, H.M.3    Stewart, C.L.4    Buck, C.5    Buck, C.A.6    Labow, M.A.7
  • 63
    • 61449213806 scopus 로고    scopus 로고
    • Mechanisms that regulate adaptor binding to {β}-integrin cytoplasmic tails
    • Legate KR, Fässler R. 2009. Mechanisms that regulate adaptor binding to {β}-integrin cytoplasmic tails. J Cell Sci 122: 187-198.
    • (2009) J Cell Sci , vol.122 , pp. 187-198
    • Legate, K.R.1    Fässler, R.2
  • 64
    • 61449220945 scopus 로고    scopus 로고
    • Genetic and cell biological analysis of integrin outside-in signaling
    • Legate KR, Wickström SA, Fässler R. 2009. Genetic and cell biological analysis of integrin outside-in signaling. Genes & Dev 23: 397-418.
    • (2009) Genes & Dev , vol.23 , pp. 397-418
    • Legate, K.R.1    Wickström, S.A.2    Fässler, R.3
  • 65
  • 66
    • 23744490092 scopus 로고    scopus 로고
    • PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage
    • Li S, Bordoy R, Stanchi F, Moser M, Braun A, Kudlacek O, Wewer UM, Yurchenco PD, Fässler R. 2005. PINCH1 regulates cell-matrix and cell-cell adhesions, cell polarity and cell survival during the peri-implantation stage. J Cell Sci 118: 2913-2921.
    • (2005) J Cell Sci , vol.118 , pp. 2913-2921
    • Li, S.1    Bordoy, R.2    Stanchi, F.3    Moser, M.4    Braun, A.5    Kudlacek, O.6    Wewer, U.M.7    Yurchenco, P.D.8    Fässler, R.9
  • 67
    • 0037850992 scopus 로고    scopus 로고
    • C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo
    • Lin X, Qadota H, Moerman DG, Williams BD. 2003. C. elegans PAT-6/actopaxin plays a critical role in the assembly of integrin adhesion complexes in vivo. Curr Biol 13: 922-932.
    • (2003) Curr Biol , vol.13 , pp. 922-932
    • Lin, X.1    Qadota, H.2    Moerman, D.G.3    Williams, B.D.4
  • 68
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • Litjens SH, de Pereda JM, Sonnenberg A. 2006. Current insights into the formation and breakdown of hemidesmosomes. Trends Cell Biol 16: 376-383.
    • (2006) Trends Cell Biol , vol.16 , pp. 376-383
    • Litjens, S.H.1    de Pereda, J.M.2    Sonnenberg, A.3
  • 70
    • 0029043889 scopus 로고
    • The basal keratin network of stratified squamous epithelia: Defining K15 function in the absence of K14
    • Lloyd C, Yu QC, Cheng J, Turksen K, Degenstein L, Hutton E, Fuchs E. 1995. The basal keratin network of stratified squamous epithelia: Defining K15 function in the absence of K14. J Cell Biol 129: 1329-1344.
    • (1995) J Cell Biol , vol.129 , pp. 1329-1344
    • Lloyd, C.1    Yu, Q.C.2    Cheng, J.3    Turksen, K.4    Degenstein, L.5    Hutton, E.6    Fuchs, E.7
  • 71
    • 0037076211 scopus 로고    scopus 로고
    • C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes
    • Mackinnon AC, Qadota H, Norman KR, Moerman DG, Williams BD. 2002. C. elegans PAT-4/ILK functions as an adaptor protein within integrin adhesion complexes. Curr Biol 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
  • 73
    • 28844459379 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis, a cell-mediated matrix assembly process
    • Mao Y, Schwarzbauer JE. 2005. Fibronectin fibrillogenesis, a cell-mediated matrix assembly process. Matrix Biol 24: 389-399.
    • (2005) Matrix Biol , vol.24 , pp. 389-399
    • Mao, Y.1    Schwarzbauer, J.E.2
  • 75
    • 0035851913 scopus 로고    scopus 로고
    • EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: Role in epithelial cell migration and carcinoma invasion
    • Mariotti A, Kedeshian PA, Dans M, Curatola AM, Gagnoux-Palacios L, Giancotti FG. 2001. EGF-R signaling through Fyn kinase disrupts the function of integrin α6β4 at hemidesmosomes: Role in epithelial cell migration and carcinoma invasion. J Cell Biol 155: 447-458.
    • (2001) J Cell Biol , vol.155 , pp. 447-458
    • Mariotti, A.1    Kedeshian, P.A.2    Dans, M.3    Curatola, A.M.4    Gagnoux-Palacios, L.5    Giancotti, F.G.6
  • 77
    • 77954755706 scopus 로고    scopus 로고
    • Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency-III patient reveal distinct effects on leukocyte function in vitro
    • McDowall A, Svensson L, Stanley P, Patzak I, Chakravarty P, Howarth K, Sabnis H, Briones M, Hogg N. 2010. Two mutations in the KINDLIN3 gene of a new leukocyte adhesion deficiency-III patient reveal distinct effects on leukocyte function in vitro. Blood 115: 4834-4842.
    • (2010) Blood , vol.115 , pp. 4834-4842
    • McDowall, A.1    Svensson, L.2    Stanley, P.3    Patzak, I.4    Chakravarty, P.5    Howarth, K.6    Sabnis, H.7    Briones, M.8    Hogg, N.9
  • 78
    • 33845942225 scopus 로고    scopus 로고
    • The congenital muscular dystrophies: Recent advances and molecular insights
    • Mendell JR, Boue DR, Martin PT. 2006. The congenital muscular dystrophies: Recent advances and molecular insights. Pediatr Dev Pathol 9: 427-443.
    • (2006) Pediatr Dev Pathol , vol.9 , pp. 427-443
    • Mendell, J.R.1    Boue, D.R.2    Martin, P.T.3
  • 80
    • 42949086409 scopus 로고    scopus 로고
    • Laminins and their roles in mammals
    • Miner JH. 2008. Laminins and their roles in mammals. Microsc Res Tech 71: 349-356.
    • (2008) Microsc Res Tech , vol.71 , pp. 349-356
    • Miner, J.H.1
  • 81
    • 3042790010 scopus 로고    scopus 로고
    • Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation
    • Miner JH, Li C, Mudd JL, Go G, Sutherland AE. 2004. Compositional and structural requirements for laminin and basement membranes during mouse embryo implantation and gastrulation. Development 131: 2247-2256.
    • (2004) Development , vol.131 , pp. 2247-2256
    • Miner, J.H.1    Li, C.2    Mudd, J.L.3    Go, G.4    Sutherland, A.E.5
  • 82
    • 0030610896 scopus 로고    scopus 로고
    • Laminin α2 chain-null mutant mice by targeted disruption of the Lama2 gene: A new model of merosin (laminin 2)-deficient congenital muscular dystrophy
    • Miyagoe Y, Hanaoka K, Nonaka I, Hayasaka M, Nabeshima Y, Arahata K, Nabeshima Y, Takeda S. 1997. Laminin α2 chain-null mutant mice by targeted disruption of the Lama2 gene: A new model of merosin (laminin 2)-deficient congenital muscular dystrophy. FEBS Lett 415: 33-39.
    • (1997) FEBS Lett , vol.415 , pp. 33-39
    • Miyagoe, Y.1    Hanaoka, K.2    Nonaka, I.3    Hayasaka, M.4    Nabeshima, Y.5    Arahata, K.6    Nabeshima, Y.7    Takeda, S.8
  • 84
    • 70350345546 scopus 로고    scopus 로고
    • αa-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling
    • Montanez E, Wickström SA, Altstätter J, Chu H, Fässler R. 2009. αa-parvin controls vascular mural cell recruitment to vessel wall by regulating RhoA/ROCK signalling. EMBO J 28: 3132-3144.
    • (2009) EMBO J , vol.28 , pp. 3132-3144
    • Montanez, E.1    Wickström, S.A.2    Altstätter, J.3    Chu, H.4    Fässler, R.5
  • 87
    • 66149128873 scopus 로고    scopus 로고
    • The tail of integrins, talin, and kindlins
    • Moser M, Legate KR, Zent R, Fässler R. 2009b. The tail of integrins, talin, and kindlins. Science 324: 895-899.
    • (2009) Science , vol.324 , pp. 895-899
    • Moser, M.1    Legate, K.R.2    Zent, R.3    Fässler, R.4
  • 88
    • 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. 2008. Kindlin-3 is essential for integrin activation and platelet aggregation. Nat Med 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
  • 89
    • 0032528060 scopus 로고    scopus 로고
    • Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin beta4 cytoplasmic domain
    • Murgia C, Blaikie P, Kim N, Dans M, Petrie HT, Giancotti FG. 1998. Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin beta4 cytoplasmic domain. EMBO J 17: 3940-3951.
    • (1998) EMBO J , vol.17 , pp. 3940-3951
    • Murgia, C.1    Blaikie, P.2    Kim, N.3    Dans, M.4    Petrie, H.T.5    Giancotti, F.G.6
  • 90
    • 73449132933 scopus 로고    scopus 로고
    • Blistering skin diseases: A bridge between dermatopathology and molecular biology
    • Nagy N, McGrath JA. 2010. Blistering skin diseases: A bridge between dermatopathology and molecular biology. Histopathology 56 91-99.
    • (2010) Histopathology , vol.56 , pp. 91-99
    • Nagy, N.1    McGrath, J.A.2
  • 92
    • 37549029679 scopus 로고    scopus 로고
    • Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo
    • Nieswandt B, Moser M, Pleines I, Varga-Szabo D, Monkley S, Critchley D, Fässler R. 2007. Loss of talin1 in platelets abrogates integrin activation, platelet aggregation, and thrombus formation in vitro and in vivo. J Exp Med 204: 3113-3118.
    • (2007) J Exp Med , vol.204 , pp. 3113-3118
    • Nieswandt, B.1    Moser, M.2    Pleines, I.3    Varga-Szabo, D.4    Monkley, S.5    Critchley, D.6    Fässler, R.7
  • 93
    • 0034110936 scopus 로고    scopus 로고
    • Formation of hemidesmosome-like structures in the absence of ligand binding by the (α)6(β)4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the (β)4 integrin subunit
    • Nievers MG, Kuikman I, Geerts D, Leigh IM, Sonnenberg A. 2000. Formation of hemidesmosome-like structures in the absence of ligand binding by the (α)6(β)4 integrin requires binding of HD1/plectin to the cytoplasmic domain of the (β)4 integrin subunit. J Cell Sci 113: 963-973.
    • (2000) J Cell Sci , vol.113 , pp. 963-973
    • Nievers, M.G.1    Kuikman, I.2    Geerts, D.3    Leigh, I.M.4    Sonnenberg, A.5
  • 95
    • 0034739856 scopus 로고    scopus 로고
    • Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion
    • Nikolopoulos SN, Turner CE. 2000. Actopaxin, a new focal adhesion protein that binds paxillin LD motifs and actin and regulates cell adhesion. J Cell Biol 151: 1435-1448.
    • (2000) J Cell Biol , vol.151 , pp. 1435-1448
    • Nikolopoulos, S.N.1    Turner, C.E.2
  • 97
    • 21744455891 scopus 로고    scopus 로고
    • Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-kB, causing defects in epidermal growth and migration
    • Nikolopoulos SN, Blaikie P, Yoshioka T, Guo W, Puri C, Tacchetti C, Giancotti FG. 2005. Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-kB, causing defects in epidermal growth and migration. Mol Cell Biol 25: 6090-6102.
    • (2005) Mol Cell Biol , vol.25 , pp. 6090-6102
    • Nikolopoulos, S.N.1    Blaikie, P.2    Yoshioka, T.3    Guo, W.4    Puri, C.5    Tacchetti, C.6    Giancotti, F.G.7
  • 99
    • 34548118392 scopus 로고    scopus 로고
    • UNC-97/PINCH is involved in the assembly of integrin cell adhesion complexes in Caenorhabditis elegans body wall muscle
    • Norman KR, Cordes S, Qadota H, Rahmani P, Moerman DG. 2007. UNC-97/PINCH is involved in the assembly of integrin cell adhesion complexes in Caenorhabditis elegans body wall muscle. Dev Biol 309: 45-55.
    • (2007) Dev Biol , vol.309 , pp. 45-55
    • Norman, K.R.1    Cordes, S.2    Qadota, H.3    Rahmani, P.4    Moerman, D.G.5
  • 100
    • 0035126590 scopus 로고    scopus 로고
    • Parvin, a 42 kDa focal adhesion protein, related to the α-actinin superfamily
    • Olski TM, Noegel AA, Korenbaum E. 2001. Parvin, a 42 kDa focal adhesion protein, related to the α-actinin superfamily. J Cell Sci 114: 525-538.
    • (2001) J Cell Sci , vol.114 , pp. 525-538
    • Olski, T.M.1    Noegel, A.A.2    Korenbaum, E.3
  • 101
    • 0037107551 scopus 로고    scopus 로고
    • Fibronectin at a glance
    • Pankov R, Yamada KM. 2002. Fibronectin at a glance. J Cell Sci 115: 3861-3863.
    • (2002) J Cell Sci , vol.115 , pp. 3861-3863
    • Pankov, R.1    Yamada, K.M.2
  • 102
    • 0035158066 scopus 로고    scopus 로고
    • Complete cytolysis and neonatal lethality in keratin 5 knockout mice reveal its fundamental role in skin integrity and in epidermolysis bullosa simplex
    • Peters B, Kirfel J, Bussow H, Vidal M, Magin TM. 2001. Complete cytolysis and neonatal lethality in keratin 5 knockout mice reveal its fundamental role in skin integrity and in epidermolysis bullosa simplex. Mol Biol Cell 12: 1775-1789.
    • (2001) Mol Biol Cell , vol.12 , pp. 1775-1789
    • Peters, B.1    Kirfel, J.2    Bussow, H.3    Vidal, M.4    Magin, T.M.5
  • 104
    • 0032563558 scopus 로고    scopus 로고
    • Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells
    • Priddle H, Hemmings L, Monkley S, Woods A, Patel B, Sutton D, Dunn GA, Zicha D, Critchley DR. 1998. Disruption of the talin gene compromises focal adhesion assembly in undifferentiated but not differentiated embryonic stem cells. J Cell Biol 142: 1121-1133.
    • (1998) J Cell Biol , vol.142 , pp. 1121-1133
    • Priddle, H.1    Hemmings, L.2    Monkley, S.3    Woods, A.4    Patel, B.5    Sutton, D.6    Dunn, G.A.7    Zicha, D.8    Critchley, D.R.9
  • 105
    • 0032845770 scopus 로고    scopus 로고
    • Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells
    • Rabinovitz I, Toker A, Mercurio AM. 1999. Protein kinase C-dependent mobilization of the α6β4 integrin from hemidesmosomes and its association with actin-rich cell protrusions drive the chemotactic migration of carcinoma cells. J Cell Biol 146: 1147-1160.
    • (1999) J Cell Biol , vol.146 , pp. 1147-1160
    • Rabinovitz, I.1    Toker, A.2    Mercurio, A.M.3
  • 106
    • 2942628076 scopus 로고    scopus 로고
    • Protein kinase C-α phosphorylation of specific serines in the connecting segment of the β4 integrin regulates the dynamics of type II hemidesmosomes
    • Rabinovitz I, Tsomo L, Mercurio AM. 2004. Protein kinase C-α phosphorylation of specific serines in the connecting segment of the β4 integrin regulates the dynamics of type II hemidesmosomes. Mol Cell Biol 24: 4351-4360.
    • (2004) Mol Cell Biol , vol.24 , pp. 4351-4360
    • Rabinovitz, I.1    Tsomo, L.2    Mercurio, A.M.3
  • 107
    • 16844373398 scopus 로고    scopus 로고
    • Keratinocytes display normal proliferation, survival and differentiation in conditional β4-integrin knockout mice
    • Raymond K, Kreft M, Janssen H, Calafat J, Sonnenberg A. 2005. Keratinocytes display normal proliferation, survival and differentiation in conditional β4-integrin knockout mice. J Cell Sci 118: 1045-1060.
    • (2005) J Cell Sci , vol.118 , pp. 1045-1060
    • Raymond, K.1    Kreft, M.2    Janssen, H.3    Calafat, J.4    Sonnenberg, A.5
  • 108
    • 0032489678 scopus 로고    scopus 로고
    • Linking integrin α6β4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the β4 subunit and plectin at multiple molecular sites
    • Rezniczek GA, de Pereda JM, Reipert S, Wiche G. 1998. Linking integrin α6β4-based cell adhesion to the intermediate filament cytoskeleton: Direct interaction between the β4 subunit and plectin at multiple molecular sites. J Cell Biol 141: 209-225.
    • (1998) J Cell Biol , vol.141 , pp. 209-225
    • Rezniczek, G.A.1    de Pereda, J.M.2    Reipert, S.3    Wiche, G.4
  • 109
    • 0033553883 scopus 로고    scopus 로고
    • Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells
    • Ryan MC, Lee K, Miyashita Y, Carter WG. 1999. Targeted disruption of the LAMA3 gene in mice reveals abnormalities in survival and late stage differentiation of epithelial cells. J Cell Biol 145: 1309-1323.
    • (1999) J Cell Biol , vol.145 , pp. 1309-1323
    • Ryan, M.C.1    Lee, K.2    Miyashita, Y.3    Carter, W.G.4
  • 111
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates α6β4 and α3β1 integrins via 14-3-3 proteins in keratinocyte migration
    • Santoro MM, Gaudino G, Marchisio PC. 2003. The MSP receptor regulates α6β4 and α3β1 integrins via 14-3-3 proteins in keratinocyte migration. Dev Cell 5: 257-271.
    • (2003) Dev Cell , vol.5 , pp. 257-271
    • Santoro, M.M.1    Gaudino, G.2    Marchisio, P.C.3
  • 113
    • 84863875404 scopus 로고    scopus 로고
    • Deciphering the mechanisms of fibronectin matrix assembly
    • doi: 10.1101/cshperspect.a005041
    • Schwarzbauer JE, DeSimone DW. 2011. Deciphering the mechanisms of fibronectin matrix assembly. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a005041.
    • (2011) Cold Spring Harb Perspect Biol
    • Schwarzbauer, J.E.1    DeSimone, D.W.2
  • 114
    • 77949862490 scopus 로고    scopus 로고
    • The final steps of integrin activation: The end game
    • Shattil SJ, Kim C, Ginsberg MH. 2010. The final steps of integrin activation: the end game. Nat Rev Mol Cell Biol 11: 288-300.
    • (2010) Nat Rev Mol Cell Biol , vol.11 , pp. 288-300
    • Shattil, S.J.1    Kim, C.2    Ginsberg, M.H.3
  • 115
    • 33751578411 scopus 로고    scopus 로고
    • Talin1 regulates TCR-mediated LFA-1 function
    • Simonson WT, Franco SJ, Huttenlocher A. 2006. Talin1 regulates TCR-mediated LFA-1 function. J Immunol 177: 7707-7714.
    • (2006) J Immunol , vol.177 , pp. 7707-7714
    • Simonson, W.T.1    Franco, S.J.2    Huttenlocher, A.3
  • 116
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • Smyth N, Vatansever HS, Murray P, Meyer M, Frie C, Paulsson M, Edgar D. 1999. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J Cell Biol 144: 151-160.
    • (1999) J Cell Biol , vol.144 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3    Meyer, M.4    Frie, C.5    Paulsson, M.6    Edgar, D.7
  • 117
    • 23844484860 scopus 로고    scopus 로고
    • Zebrafish penner/lethal giant larvae 2 functions in hemidesmosome formation, maintenance of cellular morphology and growth regulation in the developing basal epidermis
    • Sonawane M, Carpio Y, Geisler R, Schwarz H, Maischein HM, Nuesslein-Volhard C. 2005. Zebrafish penner/lethal giant larvae 2 functions in hemidesmosome formation, maintenance of cellular morphology and growth regulation in the developing basal epidermis. Development 132: 3255-3265.
    • (2005) Development , vol.132 , pp. 3255-3265
    • Sonawane, M.1    Carpio, Y.2    Geisler, R.3    Schwarz, H.4    Maischein, H.M.5    Nuesslein-Volhard, C.6
  • 118
    • 67650757498 scopus 로고    scopus 로고
    • Lgl2 and E-cadherin act antagonistically to regulate hemidesmosome formation during epidermal development in zebrafish
    • Sonawane M, Martin-Maischein H, Schwarz H, Nusslein-Volhard C. 2009. Lgl2 and E-cadherin act antagonistically to regulate hemidesmosome formation during epidermal development in zebrafish. Development 136: 1231-1240.
    • (2009) Development , vol.136 , pp. 1231-1240
    • Sonawane, M.1    Martin-Maischein, H.2    Schwarz, H.3    Nusslein-Volhard, C.4
  • 119
    • 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 CF, Grall D, Fässler R, Van Obberghen-Schilling E. 2009. 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 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    Fässler, R.5    van Obberghen-Schilling, E.6
  • 120
    • 67349213676 scopus 로고    scopus 로고
    • A molecular trio in relapse and remission in multiple sclerosis
    • Steinman L. 2009. A molecular trio in relapse and remission in multiple sclerosis. Nat Rev Immunol 9: 440-447.
    • (2009) Nat Rev Immunol , vol.9 , pp. 440-447
    • Steinman, L.1
  • 121
    • 0034658462 scopus 로고    scopus 로고
    • The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin α6β4 and may regulate the spatial organization of hemidesmosomes
    • Sterk LM, Geuijen CA, Oomen LC, Calafat J, Janssen H, Sonnenberg A. 2000. The tetraspan molecule CD151, a novel constituent of hemidesmosomes, associates with the integrin α6β4 and may regulate the spatial organization of hemidesmosomes. J Cell Biol 149: 969-982.
    • (2000) J Cell Biol , vol.149 , pp. 969-982
    • Sterk, L.M.1    Geuijen, C.A.2    Oomen, L.C.3    Calafat, J.4    Janssen, H.5    Sonnenberg, A.6
  • 122
    • 0028318185 scopus 로고
    • Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus
    • Sunada Y, Bernier SM, Kozak CA, Yamada Y, Campbell KP. 1994. Deficiency of merosin in dystrophic dy mice and genetic linkage of laminin M chain gene to dy locus. J Biol Chem 269: 13729-13732.
    • (1994) J Biol Chem , vol.269 , pp. 13729-13732
    • Sunada, Y.1    Bernier, S.M.2    Kozak, C.A.3    Yamada, Y.4    Campbell, K.P.5
  • 126
    • 3042708208 scopus 로고    scopus 로고
    • Deletion of the alternatively spliced fibronectin EIIIA domain in mice reduces atherosclerosis
    • Tan MH, Sun Z, Opitz SL, Schmidt TE, Peters JH, George EL. 2004. Deletion of the alternatively spliced fibronectin EIIIA domain in mice reduces atherosclerosis. Blood 104: 11-18.
    • (2004) Blood , vol.104 , pp. 11-18
    • Tan, M.H.1    Sun, Z.2    Opitz, S.L.3    Schmidt, T.E.4    Peters, J.H.5    George, E.L.6
  • 127
    • 33744829519 scopus 로고    scopus 로고
    • An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton
    • Tanentzapf G, Brown NH. 2006. An interaction between integrin and the talin FERM domain mediates integrin activation but not linkage to the cytoskeleton. Nat Cell Biol 8: 601-606.
    • (2006) Nat Cell Biol , vol.8 , pp. 601-606
    • Tanentzapf, G.1    Brown, N.H.2
  • 128
    • 33646683097 scopus 로고    scopus 로고
    • Multiple factors contribute to integrin-talin interactions in vivo
    • Tanentzapf G, Martin-Bermudo MD, Hicks MS, Brown NH. 2006. Multiple factors contribute to integrin-talin interactions in vivo. J Cell Sci 119: 1632-1644.
    • (2006) J Cell Sci , vol.119 , pp. 1632-1644
    • Tanentzapf, G.1    Martin-Bermudo, M.D.2    Hicks, M.S.3    Brown, N.H.4
  • 129
    • 2442701762 scopus 로고    scopus 로고
    • Keratinocytes from patients lacking collagen XVII display a migratory phenotype
    • Tasanen K, Tunggal L, Chometon G, Bruckner-Tuderman L, Aumailley M. 2004. Keratinocytes from patients lacking collagen XVII display a migratory phenotype. Am J Path 164: 2027-2038.
    • (2004) Am J Path , vol.164 , pp. 2027-2038
    • Tasanen, K.1    Tunggal, L.2    Chometon, G.3    Bruckner-Tuderman, L.4    Aumailley, M.5
  • 130
    • 0035977147 scopus 로고    scopus 로고
    • A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth
    • Trusolino L, Bertotti A, Comoglio PM. 2001. A signaling adapter function for α6β4 integrin in the control of HGF-dependent invasive growth. Cell 107: 643-654.
    • (2001) Cell , vol.107 , pp. 643-654
    • Trusolino, L.1    Bertotti, A.2    Comoglio, P.M.3
  • 133
    • 0035972170 scopus 로고    scopus 로고
    • A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading
    • Tu Y, Huang Y, Zhang Y, Hua Y, Wu C. 2001. A new focal adhesion protein that interacts with integrin-linked kinase and regulates cell adhesion and spreading. J Cell Biol 153: 585-598.
    • (2001) J Cell Biol , vol.153 , pp. 585-598
    • Tu, Y.1    Huang, Y.2    Zhang, Y.3    Hua, Y.4    Wu, C.5
  • 134
    • 0033020670 scopus 로고    scopus 로고
    • The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells
    • Tu Y, Li F, Goicoechea S, Wu C. 1999. The LIM-only protein PINCH directly interacts with integrin-linked kinase and is recruited to integrin-rich sites in spreading cells. Mol Cell Biol 19: 2425-2434.
    • (1999) Mol Cell Biol , vol.19 , pp. 2425-2434
    • Tu, Y.1    Li, F.2    Goicoechea, S.3    Wu, C.4
  • 135
    • 0028197645 scopus 로고
    • Demonstration of type II hemidesmosomes in a mammary gland epithelial cell line, BMGE-H
    • Uematsu J, Nishizawa Y, Sonnenberg A, Owaribe K. 1994. Demonstration of type II hemidesmosomes in a mammary gland epithelial cell line, BMGE-H. J Biochem 115: 469-476.
    • (1994) J Biochem , vol.115 , pp. 469-476
    • Uematsu, J.1    Nishizawa, Y.2    Sonnenberg, A.3    Owaribe, K.4
  • 136
    • 66749179401 scopus 로고    scopus 로고
    • Progress in heritable skin diseases: Translational implications of mutation analysis and prospects of molecular therapies
    • Uitto J. 2009. Progress in heritable skin diseases: Translational implications of mutation analysis and prospects of molecular therapies. Acta Derm Venereol 89: 228-235.
    • (2009) Acta Derm Venereol , vol.89 , pp. 228-235
    • Uitto, J.1
  • 137
    • 60849126413 scopus 로고    scopus 로고
    • Ultrastructural localization of integrin subunits β4 and α3 within the migrating epithelial tongue of in vivo human wounds
    • Underwood RA, Carter WG, Usui ML, Olerud JE. 2009. Ultrastructural localization of integrin subunits β4 and α3 within the migrating epithelial tongue of in vivo human wounds. J Histochem Cytochem 57: 123-142.
    • (2009) J Histochem Cytochem , vol.57 , pp. 123-142
    • Underwood, R.A.1    Carter, W.G.2    Usui, M.L.3    Olerud, J.E.4
  • 139
    • 33747877557 scopus 로고    scopus 로고
    • The kindlins: Subcellular localization and expression during murine development
    • Ussar S, Wang HV, Linder S, Fässler R, Moser M. 2006. The kindlins: Subcellular localization and expression during murine development. Exp Cell Res 312: 3142-3151.
    • (2006) Exp Cell Res , vol.312 , pp. 3142-3151
    • Ussar, S.1    Wang, H.V.2    Linder, S.3    Fässler, R.4    Moser, M.5
  • 140
    • 85047682713 scopus 로고    scopus 로고
    • Alpha4-integrin-VCAM-1 binding mediates G protein-independent capture of encephalitogenic T cell blasts to CNS white matter microvessels
    • Vajkoczy P, Laschinger M, Engelhardt B. 2001. Alpha4-integrin-VCAM-1 binding mediates G protein-independent capture of encephalitogenic T cell blasts to CNS white matter microvessels. J Clin Invest 108: 557-565.
    • (2001) J Clin Invest , vol.108 , pp. 557-565
    • Vajkoczy, P.1    Laschinger, M.2    Engelhardt, B.3
  • 141
  • 142
    • 0025976155 scopus 로고
    • Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease
    • Vassar R, Coulombe PA, Degenstein L, Albers K, Fuchs E. 1991. Mutant keratin expression in transgenic mice causes marked abnormalities resembling a human genetic skin disease. Cell 64: 365-380.
    • (1991) Cell , vol.64 , pp. 365-380
    • Vassar, R.1    Coulombe, P.A.2    Degenstein, L.3    Albers, K.4    Fuchs, E.5
  • 143
    • 0024418764 scopus 로고
    • Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin
    • Wayner EA, Garcia-Pardo A, Humphries MJ, McDonald JA, Carter WG. 1989. Identification and characterization of the T lymphocyte adhesion receptor for an alternative cell attachment domain (CS-1) in plasma fibronectin. J Cell Biol 109: 1321-1330.
    • (1989) J Cell Biol , vol.109 , pp. 1321-1330
    • Wayner, E.A.1    Garcia-Pardo, A.2    Humphries, M.J.3    McDonald, J.A.4    Carter, W.G.5
  • 144
    • 0006827927 scopus 로고
    • Electron-microscopic study of the texture of the basement membrane of larval amphibian skin
    • Weiss P, Ferris W. 1954. Electron-microscopic study of the texture of the basement membrane of larval amphibian skin. Proc Natl Acad Sci 40: 528-540.
    • (1954) Proc Natl Acad Sci , vol.40 , pp. 528-540
    • Weiss, P.1    Ferris, W.2
  • 145
    • 75049085759 scopus 로고    scopus 로고
    • The ILK/PINCH/parvin complex: The kinase is dead, long live the pseudokinase!
    • Wickström SA, Lange A, Montanez E, Fässler R. 2010. The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase! EMBO J 29: 281-291.
    • (2010) EMBO J , vol.29 , pp. 281-291
    • Wickström, S.A.1    Lange, A.2    Montanez, E.3    Fässler, R.4
  • 146
    • 34548477663 scopus 로고    scopus 로고
    • Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption
    • Wilhelmsen K, Litjens SH, Kuikman I, Margadant C, van Rheenen J, Sonnenberg A. 2007. Serine phosphorylation of the integrin β4 subunit is necessary for epidermal growth factor receptor induced hemidesmosome disruption. Mol Biol Cell 18: 3512-3522.
    • (2007) Mol Biol Cell , vol.18 , pp. 3512-3522
    • Wilhelmsen, K.1    Litjens, S.H.2    Kuikman, I.3    Margadant, C.4    van Rheenen, J.5    Sonnenberg, A.6
  • 148
    • 0028135436 scopus 로고
    • Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene
    • Xu H, Wu XR, Wewer UM, Engvall E. 1994. Murine muscular dystrophy caused by a mutation in the laminin α2 (Lama2) gene. Nat Genet 8: 297-302.
    • (1994) Nat Genet , vol.8 , pp. 297-302
    • Xu, H.1    Wu, X.R.2    Wewer, U.M.3    Engvall, E.4
  • 150
    • 0027371908 scopus 로고
    • Embryonic mesodermal defects in α5 integrin-deficient mice
    • Yang JT, Rayburn H, Hynes RO. 1993. Embryonic mesodermal defects in α5 integrin-deficient mice. Development 119: 1093-1105.
    • (1993) Development , vol.119 , pp. 1093-1105
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 151
    • 0028955748 scopus 로고
    • Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development
    • Yang JT, Rayburn H, Hynes RO. 1995. Cell adhesion events mediated by α4 integrins are essential in placental and cardiac development. Development 121: 549-560.
    • (1995) Development , vol.121 , pp. 549-560
    • Yang, J.T.1    Rayburn, H.2    Hynes, R.O.3
  • 152
    • 0033571018 scopus 로고    scopus 로고
    • Overlapping and independent functions of fibronectin receptor integrins in early mesodermal development
    • Yang JT, Bader BL, Kreidberg JA, Ullman-Cullere M, Trevithick JE, Hynes RO. 1999. Overlapping and independent functions of fibronectin receptor integrins in early mesodermal development. Dev Biol 215: 264-277.
    • (1999) Dev Biol , vol.215 , pp. 264-277
    • Yang, J.T.1    Bader, B.L.2    Kreidberg, J.A.3    Ullman-Cullere, M.4    Trevithick, J.E.5    Hynes, R.O.6
  • 153
    • 0026506799 scopus 로고
    • Prevention of experimental autoimmune encephalomyelitis by antibodies against α4 β1 integrin
    • Yednock TA, Cannon C, Fritz LC, Sanchez-Madrid F, Steinman L, Karin N. 1992. Prevention of experimental autoimmune encephalomyelitis by antibodies against α4 β1 integrin. Nature 356: 63-66.
    • (1992) Nature , vol.356 , pp. 63-66
    • Yednock, T.A.1    Cannon, C.2    Fritz, L.C.3    Sanchez-Madrid, F.4    Steinman, L.5    Karin, N.6
  • 154
    • 84861222127 scopus 로고    scopus 로고
    • Basement membranes: Cell scaffoldings and signaling platforms
    • doi: 10.1101/cshperspect.a004911
    • Yurchenco PD. 2010. Basement membranes: cell scaffoldings and signaling platforms. Cold Spring Harb Perspect Biol doi: 10.1101/cshperspect.a004911.
    • (2010) Cold Spring Harb Perspect Biol
    • Yurchenco, P.D.1
  • 156
    • 0037115611 scopus 로고    scopus 로고
    • Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites
    • Zhang Y, Chen K, Tu Y, Velyvis A, Yang Y, Qin J, Wu C. 2002. Assembly of the PINCH-ILK-CH-ILKBP complex precedes and is essential for localization of each component to cell-matrix adhesion sites. J Cell Sci 115: 4777-4786.
    • (2002) J Cell Sci , vol.115 , pp. 4777-4786
    • Zhang, Y.1    Chen, K.2    Tu, Y.3    Velyvis, A.4    Yang, Y.5    Qin, J.6    Wu, C.7


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