메뉴 건너뛰기




Volumn 418, Issue 3, 2009, Pages 491-506

Signal co-operation between integrins and other receptor systems

Author keywords

Adhesion complex; Adhesome; Cytokine receptor; Growth factor receptor; Integrin; Integrin signalling; Syndecan

Indexed keywords

ADHESOME; CYTOKINE RECEPTOR; GROWTH FACTOR RECEPTOR; INTEGRIN; INTEGRIN SIGNALLING; SYNDECAN;

EID: 62149091091     PISSN: 02646021     EISSN: 14708728     Source Type: Journal    
DOI: 10.1042/BJ20081948     Document Type: Review
Times cited : (252)

References (176)
  • 3
    • 33746800269 scopus 로고    scopus 로고
    • Focal adhesions: What's new inside
    • Lo, S. H. (2006) Focal adhesions: what's new inside. Dev. Biol. 294, 280-291
    • (2006) Dev. Biol , vol.294 , pp. 280-291
    • Lo, S.H.1
  • 4
    • 33846309701 scopus 로고    scopus 로고
    • Integrins and the actin cytoskeleton
    • Delon, I. and Brown, N. H. (2007) Integrins and the actin cytoskeleton. Curr. Opin. Cell Biol. 19, 43-50
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 43-50
    • Delon, I.1    Brown, N.H.2
  • 5
    • 33748328139 scopus 로고    scopus 로고
    • The matrix reorganized: Extracellular matrix remodeling and integrin signaling
    • Larsen, M., Artym, V. V., Green, J. A. and Yamada, K. M. (2006) The matrix reorganized: extracellular matrix remodeling and integrin signaling. Curr. Opin. Cell Biol. 18, 463-471
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 463-471
    • Larsen, M.1    Artym, V.V.2    Green, J.A.3    Yamada, K.M.4
  • 6
    • 27944497333 scopus 로고    scopus 로고
    • Tissue cells feel and respond to the stiffness of their substrate
    • Discher, D. E., Janmey, P. and Wang, Y. L. (2005) Tissue cells feel and respond to the stiffness of their substrate. Science 310, 1139-1143
    • (2005) Science , vol.310 , pp. 1139-1143
    • Discher, D.E.1    Janmey, P.2    Wang, Y.L.3
  • 7
  • 9
    • 61949262034 scopus 로고    scopus 로고
    • Integrins and cell-fate determination
    • Streuli, C. H. (2009) Integrins and cell-fate determination. J. Cell Sci. 122, 171-177
    • (2009) J. Cell Sci , vol.122 , pp. 171-177
    • Streuli, C.H.1
  • 10
    • 28444441957 scopus 로고    scopus 로고
    • Tetraspanin functions and associated microdomains
    • Hemler, M. E. (2005) Tetraspanin functions and associated microdomains. Nat. Rev. Mol. Cell Biol. 6, 801-811
    • (2005) Nat. Rev. Mol. Cell Biol , vol.6 , pp. 801-811
    • Hemler, M.E.1
  • 11
    • 35648987939 scopus 로고    scopus 로고
    • Intracellular trafficking of raft/caveolae domains: Insights from integrin signaling
    • Echarri, A., Muriel, O. and Del Pozo, M. A. (2007) Intracellular trafficking of raft/caveolae domains: insights from integrin signaling. Semin. Cell Dev. Biol. 18, 627-637
    • (2007) Semin. Cell Dev. Biol , vol.18 , pp. 627-637
    • Echarri, A.1    Muriel, O.2    Del Pozo, M.A.3
  • 13
    • 42449160630 scopus 로고    scopus 로고
    • Integrin connections to the cytoskeleton through talin and vinculin
    • Ziegler, W. H., Gingras, A. R., Critchley, D. R. and Emsley, J. (2008) Integrin connections to the cytoskeleton through talin and vinculin. Biochem. Soc. Trans. 36, 235-239
    • (2008) Biochem. Soc. Trans , vol.36 , pp. 235-239
    • Ziegler, W.H.1    Gingras, A.R.2    Critchley, D.R.3    Emsley, J.4
  • 15
    • 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. and Weaver, V. M. (2007) Mammary epithelial cell: influence of extracellular matrix composition and organization during development and tumorigenesis. Int. J. Biochem. Cell Biol. 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
  • 18
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K. and Wennerberg, K. (2004) Rho and Rac take center stage. Cell 116, 167-179
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 19
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra, S. K. and Schlaepfer, D. D. (2006) Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr. Opin. Cell Biol. 18, 516-523
    • (2006) Curr. Opin. Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 21
    • 0345687500 scopus 로고    scopus 로고
    • Positional control of cell fate through joint integrin/receptor protein kinase signaling
    • Giancotti, F. G. and Tarone, G. (2003) Positional control of cell fate through joint integrin/receptor protein kinase signaling. Annu. Rev. Cell Dev. Biol. 19, 173-206
    • (2003) Annu. Rev. Cell Dev. Biol , vol.19 , pp. 173-206
    • Giancotti, F.G.1    Tarone, G.2
  • 22
    • 33847673133 scopus 로고    scopus 로고
    • The extracellular matrix as an adhesion checkpoint for mammary epithelial function
    • Katz, E. and Streuli, C. H. (2007) The extracellular matrix as an adhesion checkpoint for mammary epithelial function. Int. J. Biochem. Cell Biol. 39, 715-726
    • (2007) Int. J. Biochem. Cell Biol , vol.39 , pp. 715-726
    • Katz, E.1    Streuli, C.H.2
  • 23
    • 36048945388 scopus 로고    scopus 로고
    • Three-dimensional microenvironments modulate fibroblast signaling responses
    • Green, J. A. and Yamada, K. M. (2007) Three-dimensional microenvironments modulate fibroblast signaling responses. Adv. Drug Delivery Rev. 59, 1293-1298
    • (2007) Adv. Drug Delivery Rev , vol.59 , pp. 1293-1298
    • Green, J.A.1    Yamada, K.M.2
  • 24
    • 25444443688 scopus 로고    scopus 로고
    • Modelling glandular epithelial cancers in three-dimensional cultures
    • Debnath, J. and Brugge, J. S. (2005) Modelling glandular epithelial cancers in three-dimensional cultures. Nat. Rev. Cancer 5, 675-688
    • (2005) Nat. Rev. Cancer , vol.5 , pp. 675-688
    • Debnath, J.1    Brugge, J.S.2
  • 25
    • 33748967069 scopus 로고    scopus 로고
    • Of extracellular matrix, scaffolds, and signaling: Tissue architecture regulates development, homeostasis, and cancer
    • Nelson, C. M. and Bissell, M. J. (2006) Of extracellular matrix, scaffolds, and signaling: tissue architecture regulates development, homeostasis, and cancer. Annu. Rev. Cell Dev. Biol. 22, 287-309
    • (2006) Annu. Rev. Cell Dev. Biol , vol.22 , pp. 287-309
    • Nelson, C.M.1    Bissell, M.J.2
  • 26
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan, D. and Weinberg, R. A. (2000) The hallmarks of cancer. Cell 100, 57-70
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 27
    • 67650730684 scopus 로고    scopus 로고
    • Cell adhesion and cancer
    • In The, Pelengaris, S. and Kahn, M, eds, pp, Blackwell Publishing, Malden, MA, U.S.A
    • Streuli, C. H. (2006) Cell adhesion and cancer. In The Molecular Biology of Cancer (Pelengaris, S. and Kahn, M., eds), pp. 356-387, Blackwell Publishing, Malden, MA, U.S.A.
    • (2006) Molecular Biology of Cancer , pp. 356-387
    • Streuli, C.H.1
  • 28
    • 44849121993 scopus 로고    scopus 로고
    • αvβ6 Integrin promotes the invasion of morphoeic basal cell carcinoma through stromal modulation
    • Marsh, D., Dickinson, S., Neill, G. W., Marshall, J. F., Hart, I. R. and Thomas, G. J. (2008) αvβ6 Integrin promotes the invasion of morphoeic basal cell carcinoma through stromal modulation. Cancer Res. 68, 3295-3303
    • (2008) Cancer Res , vol.68 , pp. 3295-3303
    • Marsh, D.1    Dickinson, S.2    Neill, G.W.3    Marshall, J.F.4    Hart, I.R.5    Thomas, G.J.6
  • 29
    • 39749084606 scopus 로고    scopus 로고
    • Analysis of integrin β4 expression in human breast cancer: Association with basal-like tumors and prognostic significance
    • Lu, S., Simin, K., Khan, A. and Mercurio, A. M. (2008) Analysis of integrin β4 expression in human breast cancer: association with basal-like tumors and prognostic significance. Clin. Cancer Res. 14, 1050-1058
    • (2008) Clin. Cancer Res , vol.14 , pp. 1050-1058
    • Lu, S.1    Simin, K.2    Khan, A.3    Mercurio, A.M.4
  • 30
    • 59449086789 scopus 로고    scopus 로고
    • Integrin α6β4 controls the expression of genes assocated with cell motility, invasion and metastasis including S100A4/ metastasin
    • Chen, M., Sinha, M., Luxon, B. A., Bresnick, A. R. and O'Connor, K. L. (2009) Integrin α6β4 controls the expression of genes assocated with cell motility, invasion and metastasis including S100A4/ metastasin. J. Biol. Chem. 284, 1484-1494
    • (2009) J. Biol. Chem , vol.284 , pp. 1484-1494
    • Chen, M.1    Sinha, M.2    Luxon, B.A.3    Bresnick, A.R.4    O'Connor, K.L.5
  • 31
    • 0032969073 scopus 로고    scopus 로고
    • Endothelial cell integrin α5β1 expression is modulated by cytokines and during migration in vitro
    • Collo, G. and Pepper, M. S. (1999) Endothelial cell integrin α5β1 expression is modulated by cytokines and during migration in vitro. J. Cell Sci. 112, 569-578
    • (1999) J. Cell Sci , vol.112 , pp. 569-578
    • Collo, G.1    Pepper, M.S.2
  • 32
    • 0028987192 scopus 로고
    • Transforming growth factor-β1 modulates β1 and β5 integrin receptors and induces the de novo expression of the αvβ6 heterodimer in normal human keratinocytes: Implications for wound healing
    • Zambruno, G., Marchisio, P. C., Marconi, A., Vaschieri, C., Melchiori, A., Giannetti, A. and De Luca, M. (1995) Transforming growth factor-β1 modulates β1 and β5 integrin receptors and induces the de novo expression of the αvβ6 heterodimer in normal human keratinocytes: implications for wound healing. J. Cell Biol. 129, 853-865
    • (1995) J. Cell Biol , vol.129 , pp. 853-865
    • Zambruno, G.1    Marchisio, P.C.2    Marconi, A.3    Vaschieri, C.4    Melchiori, A.5    Giannetti, A.6    De Luca, M.7
  • 33
    • 50849142875 scopus 로고    scopus 로고
    • Temporal and spatial regulation of integrins during development
    • Meighan, C. M. and Schwarzbauer, J. E. (2008) Temporal and spatial regulation of integrins during development. Curr. Opin. Cell Biol. 20, 520-524
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 520-524
    • Meighan, C.M.1    Schwarzbauer, J.E.2
  • 34
    • 44649198353 scopus 로고    scopus 로고
    • Endocytic transport of integrins during cell migration and invasion
    • Caswell, P. and Norman, J. (2008) Endocytic transport of integrins during cell migration and invasion. Trends Cell Biol. 18, 257-263
    • (2008) Trends Cell Biol , vol.18 , pp. 257-263
    • Caswell, P.1    Norman, J.2
  • 35
    • 56149110341 scopus 로고    scopus 로고
    • Integrin β3 expression is regulated by let-7a miRNA in malignant melanoma
    • Muller, D. W. and Bosserhoff, A. K. (2008) Integrin β3 expression is regulated by let-7a miRNA in malignant melanoma. Oncogene 27, 6698-6706
    • (2008) Oncogene , vol.27 , pp. 6698-6706
    • Muller, D.W.1    Bosserhoff, A.K.2
  • 37
    • 35748975965 scopus 로고    scopus 로고
    • Tetraspanin CD151 promotes cell migration by regulating integrin trafficking
    • Liu, L., He, B., Liu, W. M., Zhou, D., Cox, J. V. and Zhang, X. A. (2007) Tetraspanin CD151 promotes cell migration by regulating integrin trafficking. J. Biol. Chem. 282, 31631-31642
    • (2007) J. Biol. Chem , vol.282 , pp. 31631-31642
    • Liu, L.1    He, B.2    Liu, W.M.3    Zhou, D.4    Cox, J.V.5    Zhang, X.A.6
  • 39
    • 35648978998 scopus 로고    scopus 로고
    • Structure and mechanics of integrin-based cell adhesion
    • Arnaout, M. A., Goodman, S. L. and Xiong, J. P. (2007) Structure and mechanics of integrin-based cell adhesion. Curr. Opin. Cell Biol. 19, 495-507
    • (2007) Curr. Opin. Cell Biol , vol.19 , pp. 495-507
    • Arnaout, M.A.1    Goodman, S.L.2    Xiong, J.P.3
  • 40
    • 34247891506 scopus 로고    scopus 로고
    • Structural basis of integrin regulation and signaling
    • Luo, B. H., Carman, C. V. and Springer, T. A. (2007) Structural basis of integrin regulation and signaling. Annu. Rev. Immunol. 25, 619-647
    • (2007) Annu. Rev. Immunol , vol.25 , pp. 619-647
    • Luo, B.H.1    Carman, C.V.2    Springer, T.A.3
  • 41
    • 21844450244 scopus 로고    scopus 로고
    • Intracellular signalling controlling integrin activation in lymphocytes
    • Kinashi, T. (2005) Intracellular signalling controlling integrin activation in lymphocytes. Nat. Rev. Immunol. 5, 546-559
    • (2005) Nat. Rev. Immunol , vol.5 , pp. 546-559
    • Kinashi, T.1
  • 42
    • 34250768894 scopus 로고    scopus 로고
    • Platelet integrin αIIbβ3: Activation mechanisms
    • Ma, Y. Q., Qin, J. and Plow, E. F. (2007) Platelet integrin αIIbβ3: activation mechanisms. J. Thromb. Haemostasis 5, 1345-1352
    • (2007) J. Thromb. Haemostasis , vol.5 , pp. 1345-1352
    • Ma, Y.Q.1    Qin, J.2    Plow, E.F.3
  • 43
    • 33645837225 scopus 로고    scopus 로고
    • Multiple functions of the integrin α6β4 in epidermal homeostasis and tumorigenesis
    • Wilhelmsen, K., Litjens, S. H. and Sonnenberg, A. (2006) Multiple functions of the integrin α6β4 in epidermal homeostasis and tumorigenesis. Mol. Cell. Biol. 26, 2877-2886
    • (2006) Mol. Cell. Biol , vol.26 , pp. 2877-2886
    • Wilhelmsen, K.1    Litjens, S.H.2    Sonnenberg, A.3
  • 45
    • 42049097655 scopus 로고    scopus 로고
    • Induction of an epithelial integrin αvβ6 in human cytomegalovirus-infected endothelial cells leads to activation of transforming growth factor-β1 and increased collagen production
    • Tabata, T., Kawakatsu, H., Maidji, E., Sakai, T., Sakai, K., Fang-Hoover, J., Aiba, M., Sheppard, D. and Pereira, L. (2008) Induction of an epithelial integrin αvβ6 in human cytomegalovirus-infected endothelial cells leads to activation of transforming growth factor-β1 and increased collagen production. Am. J. Pathol. 172, 1127-1140
    • (2008) Am. J. Pathol , vol.172 , pp. 1127-1140
    • Tabata, T.1    Kawakatsu, H.2    Maidji, E.3    Sakai, T.4    Sakai, K.5    Fang-Hoover, J.6    Aiba, M.7    Sheppard, D.8    Pereira, L.9
  • 47
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto, S., Teramoto, H., Gutkind, J. S. and Yamada, K. M. (1996) Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J. Cell Biol. 135, 1633-1642
    • (1996) J. Cell Biol , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 48
    • 0032538798 scopus 로고    scopus 로고
    • Integrins induce activation of EGF receptor: Role in MAP kinase induction and adhesion-dependent cell survival
    • Moro, L., Venturino, M., Bozzo, C., Silengo, L., Altruda, F., Beguinot, L., Tarone, G. and Defilippi, P. (1998) Integrins induce activation of EGF receptor: role in MAP kinase induction and adhesion-dependent cell survival. EMBO J. 17, 6622-6632
    • (1998) EMBO J , vol.17 , pp. 6622-6632
    • Moro, L.1    Venturino, M.2    Bozzo, C.3    Silengo, L.4    Altruda, F.5    Beguinot, L.6    Tarone, G.7    Defilippi, P.8
  • 49
    • 35148888159 scopus 로고    scopus 로고
    • Analysis of integrin signaling by fluorescence resonance energy transfer
    • Wang, Y. and Chien, S. (2007) Analysis of integrin signaling by fluorescence resonance energy transfer. Methods Enzymol. 426, 177-201
    • (2007) Methods Enzymol , vol.426 , pp. 177-201
    • Wang, Y.1    Chien, S.2
  • 50
    • 9644289575 scopus 로고    scopus 로고
    • Integrins: Versatile integrators of extracellular signals
    • Ffrench-Constant, C. and Colognato, H. (2004) Integrins: versatile integrators of extracellular signals. Trends Cell Biol. 14, 678-686
    • (2004) Trends Cell Biol , vol.14 , pp. 678-686
    • Ffrench-Constant, C.1    Colognato, H.2
  • 52
    • 0037458140 scopus 로고    scopus 로고
    • Regulation of integrin growth factor interactions in oligodendrocytes by lipid raft microdomains
    • Baron, W., Decker, L., Colognato, H. and Ffrench-Constant, C. (2003) Regulation of integrin growth factor interactions in oligodendrocytes by lipid raft microdomains. Curr. Biol. 13, 151-155
    • (2003) Curr. Biol , vol.13 , pp. 151-155
    • Baron, W.1    Decker, L.2    Colognato, H.3    Ffrench-Constant, C.4
  • 53
    • 0033594105 scopus 로고    scopus 로고
    • Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling
    • Farrelly, N., Lee, Y. J., Oliver, J., Dive, C. and Streuli, C. H. (1999) Extracellular matrix regulates apoptosis in mammary epithelium through a control on insulin signaling. J. Cell Biol. 144, 1337-1348
    • (1999) J. Cell Biol , vol.144 , pp. 1337-1348
    • Farrelly, N.1    Lee, Y.J.2    Oliver, J.3    Dive, C.4    Streuli, C.H.5
  • 54
    • 0033529711 scopus 로고    scopus 로고
    • Extracellular matrix selectively modulates the response of mammary epithelial cells to different soluble signaling ligands
    • Lee, Y. J. and Streuli, C. H. (1999) Extracellular matrix selectively modulates the response of mammary epithelial cells to different soluble signaling ligands. J. Biol. Chem. 274, 22401-22408
    • (1999) J. Biol. Chem , vol.274 , pp. 22401-22408
    • Lee, Y.J.1    Streuli, C.H.2
  • 55
    • 0001811693 scopus 로고    scopus 로고
    • The mammary gland epithelial cell
    • Harris, A, ed, pp, Cambridge University Press, Cambridge, U.K
    • Pullan, S. and Streuli, C. H. (1996) The mammary gland epithelial cell. In Epithelial Cell Culture (Harris, A., ed.), pp. 97-121, Cambridge University Press, Cambridge, U.K.
    • (1996) Epithelial Cell Culture , pp. 97-121
    • Pullan, S.1    Streuli, C.H.2
  • 58
    • 0034665166 scopus 로고    scopus 로고
    • Selective inhibition of vascular endothelial growth factor (VEGF) receptor 2 (KDR/Flk-1) activity by a monoclonal anti-VEGF antibody blocks tumor growth in mice
    • Brekken, R. A., Overholser, J. P., Stastny, V. A., Waltenberger, J., Minna, J. D. and Thorpe, P. E. (2000) Selective inhibition of vascular endothelial growth factor (VEGF) receptor 2 (KDR/Flk-1) activity by a monoclonal anti-VEGF antibody blocks tumor growth in mice. Cancer Res. 60, 5117-5124
    • (2000) Cancer Res , vol.60 , pp. 5117-5124
    • Brekken, R.A.1    Overholser, J.P.2    Stastny, V.A.3    Waltenberger, J.4    Minna, J.D.5    Thorpe, P.E.6
  • 61
    • 0033558087 scopus 로고    scopus 로고
    • Role of αvβ3 integrin in the activation of vascular endothelial growth factor receptor-2
    • Soldi, R., Mitola, S., Strasly, M., Defilippi, P., Tarone, G. and Bussolino, F. (1999) Role of αvβ3 integrin in the activation of vascular endothelial growth factor receptor-2. EMBO J. 18, 882-892
    • (1999) EMBO J , vol.18 , pp. 882-892
    • Soldi, R.1    Mitola, S.2    Strasly, M.3    Defilippi, P.4    Tarone, G.5    Bussolino, F.6
  • 62
    • 33750499985 scopus 로고    scopus 로고
    • Integrin signaling is critical for pathological angiogenesis
    • Mahabeleshwar, G. H., Feng, W., Phillips, D. R. and Byzova, T. V. (2006) Integrin signaling is critical for pathological angiogenesis. J. Exp. Med. 203, 2495-2507
    • (2006) J. Exp. Med , vol.203 , pp. 2495-2507
    • Mahabeleshwar, G.H.1    Feng, W.2    Phillips, D.R.3    Byzova, T.V.4
  • 63
    • 34748863572 scopus 로고    scopus 로고
    • Mechanisms of integrin-vascular endothelial growth factor receptor cross-activation in angiogenesis
    • Mahabeleshwar, G. H., Feng, W., Reddy, K., Plow, E. F. and Byzova, T. V. (2007) Mechanisms of integrin-vascular endothelial growth factor receptor cross-activation in angiogenesis. Circ. Res. 101, 570-580
    • (2007) Circ. Res , vol.101 , pp. 570-580
    • Mahabeleshwar, G.H.1    Feng, W.2    Reddy, K.3    Plow, E.F.4    Byzova, T.V.5
  • 64
    • 13544252467 scopus 로고    scopus 로고
    • Tumor metastasis but not tumor growth is dependent on Src-mediated vascular permeability
    • Criscuoli, M. L., Nguyen, M. and Eliceiri, B. P. (2005) Tumor metastasis but not tumor growth is dependent on Src-mediated vascular permeability. Blood 105, 1508-1514
    • (2005) Blood , vol.105 , pp. 1508-1514
    • Criscuoli, M.L.1    Nguyen, M.2    Eliceiri, B.P.3
  • 65
    • 4544235743 scopus 로고    scopus 로고
    • c-Src and cooperating partners in human cancer
    • Ishizawar, R. and Parsons, S. J. (2004) c-Src and cooperating partners in human cancer. Cancer Cell. 6, 209-214
    • (2004) Cancer Cell , vol.6 , pp. 209-214
    • Ishizawar, R.1    Parsons, S.J.2
  • 66
    • 0842280613 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates vascular morphogenesis induced by vascular endothelial growth factor
    • Kaneko, Y., Kitazato, K. and Basaki, Y. (2004) Integrin-linked kinase regulates vascular morphogenesis induced by vascular endothelial growth factor. J. Cell Sci. 117, 407-415
    • (2004) J. Cell Sci , vol.117 , pp. 407-415
    • Kaneko, Y.1    Kitazato, K.2    Basaki, Y.3
  • 68
    • 51049108993 scopus 로고    scopus 로고
    • αvβ3 integrin and angiogenesis: A moody integrin in a changing environment
    • Hodivala-Dilke, K. (2008) αvβ3 integrin and angiogenesis: a moody integrin in a changing environment. Curr. Opin. Cell Biol. 20, 514-519
    • (2008) Curr. Opin. Cell Biol , vol.20 , pp. 514-519
    • Hodivala-Dilke, K.1
  • 70
    • 9244231286 scopus 로고    scopus 로고
    • Elevated Flk1 (vascular endothelial growth factor receptor 2) signaling mediates enhanced angiogenesis in β3-integrin-deficient mice
    • Reynolds, A. R., Reynolds, L. E., Nagel, T. E., Lively, J. C., Robinson, S. D., Hicklin, D. J., Bodary, S. C. and Hodivala-Dilke, K. M. (2004) Elevated Flk1 (vascular endothelial growth factor receptor 2) signaling mediates enhanced angiogenesis in β3-integrin-deficient mice. Cancer Res. 64, 8643-8650
    • (2004) Cancer Res , vol.64 , pp. 8643-8650
    • Reynolds, A.R.1    Reynolds, L.E.2    Nagel, T.E.3    Lively, J.C.4    Robinson, S.D.5    Hicklin, D.J.6    Bodary, S.C.7    Hodivala-Dilke, K.M.8
  • 71
    • 0032514841 scopus 로고    scopus 로고
    • Extensive vasculogenesis, angiogenesis, and organogenesis precede lethality in mice lacking all αv integrins
    • Bader, B. L., Rayburn, H., Crowley, D. and Hynes, R. O. (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
  • 74
    • 24944468632 scopus 로고    scopus 로고
    • Stable interaction between α5β1 integrin and Tie2 tyrosine kinase receptor regulates endothelial cell response to Ang-1
    • Cascone, I., Napione, L., Maniero, F., Serini, G. and Bussolino, F. (2005) Stable interaction between α5β1 integrin and Tie2 tyrosine kinase receptor regulates endothelial cell response to Ang-1. J. Cell Biol. 170, 993-1004
    • (2005) J. Cell Biol , vol.170 , pp. 993-1004
    • Cascone, I.1    Napione, L.2    Maniero, F.3    Serini, G.4    Bussolino, F.5
  • 77
    • 0032483575 scopus 로고    scopus 로고
    • A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth
    • Wary, K. K., Mariotti, A., Zurzolo, C. and Giancotti, F. G. (1998) A requirement for caveolin-1 and associated kinase Fyn in integrin signaling and anchorage-dependent cell growth. Cell 94, 625-634
    • (1998) Cell , vol.94 , pp. 625-634
    • Wary, K.K.1    Mariotti, A.2    Zurzolo, C.3    Giancotti, F.G.4
  • 78
    • 42349100236 scopus 로고    scopus 로고
    • Besides adhesion: New perspectives of integrin functions in angiogenesis
    • Serini, G., Napione, L., Arese, M. and Bussolino, F. (2008) Besides adhesion: new perspectives of integrin functions in angiogenesis. Cardiovasc. Res. 78, 213-222
    • (2008) Cardiovasc. Res , vol.78 , pp. 213-222
    • Serini, G.1    Napione, L.2    Arese, M.3    Bussolino, F.4
  • 81
    • 33745947286 scopus 로고    scopus 로고
    • Current insights into the formation and breakdown of hemidesmosomes
    • Litjens, S. H., de Pereda, J. M. and 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
  • 82
    • 0032528060 scopus 로고    scopus 로고
    • Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain
    • Murgia, C., Blaikie, P., Kim, N., Dans, M., Petrie, H. T. and Giancotti, F. G. (1998) Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 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
  • 83
    • 0032962217 scopus 로고    scopus 로고
    • Mutation analysis and molecular genetics of epidermolysis bullosa
    • Pulkkinen, L. and Uitto, J. (1999) Mutation analysis and molecular genetics of epidermolysis bullosa. Matrix Biol. 18, 29-42
    • (1999) Matrix Biol , vol.18 , pp. 29-42
    • Pulkkinen, L.1    Uitto, J.2
  • 84
    • 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-κB, causing defects in epidermal growth and migration
    • Nikolopoulos, S. N., Blaikie, P., Yoshioka, T., Guo, W., Puri, C., Tacchetti, C. and Giancotti, F. G. (2005) Targeted deletion of the integrin β4 signaling domain suppresses laminin-5-dependent nuclear entry of mitogen-activated protein kinases and NF-κB, 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
  • 86
    • 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, S. H., Kuikman, I., Margadant, C., van Rheenen, J. and 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
  • 88
    • 33750514792 scopus 로고    scopus 로고
    • β4 integrin and epidermal growth factor coordinately regulate electric field-mediated directional migration via Rac1
    • Pullar, C. E., Baier, B. S., Kariya, Y., Russell, A. J., Horst, B. A., Marinkovich, M. P. and Isseroff, R. R. (2006) β4 integrin and epidermal growth factor coordinately regulate electric field-mediated directional migration via Rac1. Mol. Biol. Cell 17, 4925-4935
    • (2006) Mol. Biol. Cell , vol.17 , pp. 4925-4935
    • Pullar, C.E.1    Baier, B.S.2    Kariya, Y.3    Russell, A.J.4    Horst, B.A.5    Marinkovich, M.P.6    Isseroff, R.R.7
  • 89
    • 0042679580 scopus 로고    scopus 로고
    • The MSP receptor regulates α6β4 and α3β1 integrins via 14-3-3 proteins in keratinocyte migration
    • Santoro, M. M., Gaudino, G. and Marchisio, P. C. (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
  • 90
    • 0034686013 scopus 로고    scopus 로고
    • Integrin-mediated RON growth factor receptor phosphorylation requires tyrosine kinase activity of both the receptor and c-Src
    • Danilkovitch-Miagkova, A., Angeloni, D., Skeel, A., Donley, S., Lerman, M. and Leonard, E. J. (2000) Integrin-mediated RON growth factor receptor phosphorylation requires tyrosine kinase activity of both the receptor and c-Src. J. Biol. Chem. 275, 14783-14786
    • (2000) J. Biol. Chem , vol.275 , pp. 14783-14786
    • Danilkovitch-Miagkova, A.1    Angeloni, D.2    Skeel, A.3    Donley, S.4    Lerman, M.5    Leonard, E.J.6
  • 91
    • 34748863597 scopus 로고    scopus 로고
    • Targeting integrin β4 for cancer and anti-angiogenic therapy
    • Giancotti, F. G. (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
  • 92
    • 27644496163 scopus 로고    scopus 로고
    • Mobilization and activation of a signaling competent α6β4 integrin underlies its contribution to carcinoma progression
    • Lipscomb, E. A. and Mercurio, A. M. (2005) Mobilization and activation of a signaling competent α6β4 integrin underlies its contribution to carcinoma progression. Cancer Metastasis Rev. 24, 413-423
    • (2005) Cancer Metastasis Rev , vol.24 , pp. 413-423
    • Lipscomb, E.A.1    Mercurio, A.M.2
  • 93
    • 34248215265 scopus 로고    scopus 로고
    • Involvement of α6β4 integrin in the mechanisms that regulate breast cancer progression
    • Bon, G., Folgiero, V., Di Carlo, S., Sacchi, A. and Falcioni, R. (2007) Involvement of α6β4 integrin in the mechanisms that regulate breast cancer progression. Breast Cancer Res. 9, 203
    • (2007) Breast Cancer Res , vol.9 , pp. 203
    • Bon, G.1    Folgiero, V.2    Di Carlo, S.3    Sacchi, A.4    Falcioni, R.5
  • 95
    • 33847750616 scopus 로고    scopus 로고
    • The α6β4 integrin can regulate ErbB-3 expression: Implications for α6β4 signaling and function
    • Folgiero, V., Bachelder, R. E., Bon, G., Sacchi, A., Falcioni, R. and Mercurio, A. M. (2007) The α6β4 integrin can regulate ErbB-3 expression: implications for α6β4 signaling and function. Cancer Res. 67, 1645-1652
    • (2007) Cancer Res , vol.67 , pp. 1645-1652
    • Folgiero, V.1    Bachelder, R.E.2    Bon, G.3    Sacchi, A.4    Falcioni, R.5    Mercurio, A.M.6
  • 96
    • 33645050918 scopus 로고    scopus 로고
    • A novel mechanism for integrin-mediated ras activation in breast carcinoma cells: The α6β4 integrin regulates ErbB2 translation and transactivates epidermal growth factor receptor/ErbB2 signaling
    • Yoon, S. O., Shin, S. and Lipscomb, E. A. (2006) A novel mechanism for integrin-mediated ras activation in breast carcinoma cells: the α6β4 integrin regulates ErbB2 translation and transactivates epidermal growth factor receptor/ErbB2 signaling. Cancer Res. 66, 2732-2739
    • (2006) Cancer Res , vol.66 , pp. 2732-2739
    • Yoon, S.O.1    Shin, S.2    Lipscomb, E.A.3
  • 97
    • 0034951677 scopus 로고    scopus 로고
    • Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion
    • Shaw, L. M. (2001) Identification of insulin receptor substrate 1 (IRS-1) and IRS-2 as signaling intermediates in the α6β4 integrin-dependent activation of phosphoinositide 3-OH kinase and promotion of invasion. Mol. Cell. Biol. 21, 5082-5093
    • (2001) Mol. Cell. Biol , vol.21 , pp. 5082-5093
    • Shaw, L.M.1
  • 98
    • 28244478626 scopus 로고    scopus 로고
    • β4 integrin is a transforming molecule that unleashes Met tyrosine kinase tumorigenesis
    • Bertotti, A., Comoglio, P. M. and Trusolino, L. (2005) β4 integrin is a transforming molecule that unleashes Met tyrosine kinase tumorigenesis. Cancer Res. 65, 10674-10679
    • (2005) Cancer Res , vol.65 , pp. 10674-10679
    • Bertotti, A.1    Comoglio, P.M.2    Trusolino, L.3
  • 99
    • 3543011958 scopus 로고    scopus 로고
    • The Met receptor and α6β4 integrin can function independently to promote carcinoma invasion
    • Chung, J., Yoon, S. O., Lipscomb, E. A. and Mercurio, A. M. (2004) The Met receptor and α6β4 integrin can function independently to promote carcinoma invasion. J. Biol. Chem. 279, 32287-32293
    • (2004) J. Biol. Chem , vol.279 , pp. 32287-32293
    • Chung, J.1    Yoon, S.O.2    Lipscomb, E.A.3    Mercurio, A.M.4
  • 100
    • 35648976145 scopus 로고    scopus 로고
    • Intrinsic signaling functions of the β4 integrin intracellular domain
    • Merdek, K. D., Yang, X., Taglienti, C. A., Shaw, L. M. and Mercurio, A. M. (2007) Intrinsic signaling functions of the β4 integrin intracellular domain. J. Biol. Chem. 282, 30322-30330
    • (2007) J. Biol. Chem , vol.282 , pp. 30322-30330
    • Merdek, K.D.1    Yang, X.2    Taglienti, C.A.3    Shaw, L.M.4    Mercurio, A.M.5
  • 101
    • 0347363470 scopus 로고    scopus 로고
    • Autocrine laminin-5 ligates α6β4 integrin and activates RAC and NF-κB to mediate anchorage-independent survival of mammary tumors
    • Zahir, N., Lakins, J. N., Russell, A., Ming, W., Chatterjee, C., Rozenberg, G. I., Marinkovich, M. P. and Weaver, V. M. (2003) Autocrine laminin-5 ligates α6β4 integrin and activates RAC and NF-κB to mediate anchorage-independent survival of mammary tumors. J. Cell Biol. 163, 1397-1407
    • (2003) J. Cell Biol , vol.163 , pp. 1397-1407
    • Zahir, N.1    Lakins, J.N.2    Russell, A.3    Ming, W.4    Chatterjee, C.5    Rozenberg, G.I.6    Marinkovich, M.P.7    Weaver, V.M.8
  • 102
    • 36248998112 scopus 로고    scopus 로고
    • α6β4 integrin activates Rac-dependent p21-activated kinase 1 to drive NF-κB-dependent resistance to apoptosis in 3D mammary acini
    • Friedland, J. C., Lakins, J. N., Kazanietz, M. G., Chernoff, J., Boettiger, D. and Weaver, V. M. (2007) α6β4 integrin activates Rac-dependent p21-activated kinase 1 to drive NF-κB-dependent resistance to apoptosis in 3D mammary acini. J. Cell Sci. 120, 3700-3712
    • (2007) J. Cell Sci , vol.120 , pp. 3700-3712
    • Friedland, J.C.1    Lakins, J.N.2    Kazanietz, M.G.3    Chernoff, J.4    Boettiger, D.5    Weaver, V.M.6
  • 103
    • 33745186855 scopus 로고    scopus 로고
    • Loss of β4 integrin subunit reduces the tumorigenicity of MCF7 mammary cells and causes apoptosis upon hormone deprivation
    • Bon, G., Folgiero, V., Bossi, G., Felicioni, L., Marchetti, A., Sacchi, A. and Falcioni, R. (2006) Loss of β4 integrin subunit reduces the tumorigenicity of MCF7 mammary cells and causes apoptosis upon hormone deprivation. Clin. Cancer Res. 12, 3280-3287
    • (2006) Clin. Cancer Res , vol.12 , pp. 3280-3287
    • Bon, G.1    Folgiero, V.2    Bossi, G.3    Felicioni, L.4    Marchetti, A.5    Sacchi, A.6    Falcioni, R.7
  • 106
    • 0036364538 scopus 로고    scopus 로고
    • Integrin control of cell cycle: A new role for ubiquitin ligase
    • Pu, Q. Q. and Streuli, C. H. (2002) Integrin control of cell cycle: a new role for ubiquitin ligase. Bioessays 24, 17-21
    • (2002) Bioessays , vol.24 , pp. 17-21
    • Pu, Q.Q.1    Streuli, C.H.2
  • 107
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin, A. E., Stewart, S. A., Assoian, R. K. and Juliano, R. L. (2001) Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J. Cell Biol. 153, 273-282
    • (2001) J. Cell Biol , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 109
    • 0035954432 scopus 로고    scopus 로고
    • Role of the F-box protein Skp2 in adhesion-dependent cell cycle progression
    • Carrano, A. C. and Pagano, M. (2001) Role of the F-box protein Skp2 in adhesion-dependent cell cycle progression. J. Cell Biol. 153, 1381-1390
    • (2001) J. Cell Biol , vol.153 , pp. 1381-1390
    • Carrano, A.C.1    Pagano, M.2
  • 110
    • 0030766846 scopus 로고    scopus 로고
    • Growth factor activation of MAP kinase requires cell adhesion
    • Renshaw, M. W., Ren, X. D. and Schwartz, M. A. (1997) Growth factor activation of MAP kinase requires cell adhesion. EMBO J. 16, 5592-5599
    • (1997) EMBO J , vol.16 , pp. 5592-5599
    • Renshaw, M.W.1    Ren, X.D.2    Schwartz, M.A.3
  • 111
    • 0029876639 scopus 로고    scopus 로고
    • Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein
    • Zhu, X., Ohtsubo, M., Bohmer, R. M., Roberts, J. M. and Assoian, R. K. (1996) Adhesion-dependent cell cycle progression linked to the expression of cyclin D1, activation of cyclin E-cdk2, and phosphorylation of the retinoblastoma protein. J. Cell Biol. 133, 391-403
    • (1996) J. Cell Biol , vol.133 , pp. 391-403
    • Zhu, X.1    Ohtsubo, M.2    Bohmer, R.M.3    Roberts, J.M.4    Assoian, R.K.5
  • 112
    • 0035150990 scopus 로고    scopus 로고
    • Growth-factor-dependent mitogenesis requires two distinct phases of signalling
    • Jones, S. M. and Kazlauskas, A. (2001) Growth-factor-dependent mitogenesis requires two distinct phases of signalling. Nat. Cell Biol. 3, 165-172
    • (2001) Nat. Cell Biol , vol.3 , pp. 165-172
    • Jones, S.M.1    Kazlauskas, A.2
  • 113
    • 0037088647 scopus 로고    scopus 로고
    • Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines
    • Moro, L., Dolce, L., Cabodi, S., Bergatto, E., Boeri Erba, E., Smeriglio, M., Turco, E., Retta, S. F., Giuffrida, M. G., Venturino, M. et al. (2002) Integrin-induced epidermal growth factor (EGF) receptor activation requires c-Src and p130Cas and leads to phosphorylation of specific EGF receptor tyrosines. J. Biol. Chem. 277, 9405-9414
    • (2002) J. Biol. Chem , vol.277 , pp. 9405-9414
    • Moro, L.1    Dolce, L.2    Cabodi, S.3    Bergatto, E.4    Boeri Erba, E.5    Smeriglio, M.6    Turco, E.7    Retta, S.F.8    Giuffrida, M.G.9    Venturino, M.10
  • 114
    • 4544302236 scopus 로고    scopus 로고
    • Epidermal growth factor receptor-dependent regulation of integrin-mediated signaling and cell cycle entry in epithelial cells
    • Bill, H. M., Knudsen, B., Moores, S. L., Muthuswamy, S. K., Rao, V. R., Brugge, J. S. and Miranti, C. K. (2004) Epidermal growth factor receptor-dependent regulation of integrin-mediated signaling and cell cycle entry in epithelial cells. Mol. Cell. Biol. 24, 8586-8599
    • (2004) Mol. Cell. Biol , vol.24 , pp. 8586-8599
    • Bill, H.M.1    Knudsen, B.2    Moores, S.L.3    Muthuswamy, S.K.4    Rao, V.R.5    Brugge, J.S.6    Miranti, C.K.7
  • 115
    • 0033538527 scopus 로고    scopus 로고
    • Integrins enhance platelet-derived growth factor (PDGF)-dependent responses by altering the signal relay enzymes that are recruited to the PDGFβ receptor
    • DeMali, K. A., Balciunaite, E. and Kazlauskas, A. (1999) Integrins enhance platelet-derived growth factor (PDGF)-dependent responses by altering the signal relay enzymes that are recruited to the PDGFβ receptor. J. Biol. Chem. 274, 19551-19558
    • (1999) J. Biol. Chem , vol.274 , pp. 19551-19558
    • DeMali, K.A.1    Balciunaite, E.2    Kazlauskas, A.3
  • 116
    • 47249118481 scopus 로고    scopus 로고
    • Noonan syndrome-associated SHP-2/ Ptpn11 mutants enhance SIRPα and PZR tyrosyl phosphorylation and promote adhesion-mediated ERK activation
    • Eminaga, S. and Bennett, A. M. (2008) Noonan syndrome-associated SHP-2/ Ptpn11 mutants enhance SIRPα and PZR tyrosyl phosphorylation and promote adhesion-mediated ERK activation. J. Biol. Chem. 283, 15328-15338
    • (2008) J. Biol. Chem , vol.283 , pp. 15328-15338
    • Eminaga, S.1    Bennett, A.M.2
  • 118
    • 0034595381 scopus 로고    scopus 로고
    • Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK
    • del Pozo, M. A., Price, L. S., Alderson, N. B., Ren, X. D. and Schwartz, M. A. (2000) Adhesion to the extracellular matrix regulates the coupling of the small GTPase Rac to its effector PAK. EMBO J. 19, 2008-2014
    • (2000) EMBO J , vol.19 , pp. 2008-2014
    • del Pozo, M.A.1    Price, L.S.2    Alderson, N.B.3    Ren, X.D.4    Schwartz, M.A.5
  • 119
    • 34247562835 scopus 로고    scopus 로고
    • Rac, membrane heterogeneity, caveolin and regulation of growth by integrins
    • Del Pozo, M. A. and Schwartz, M. A. (2007) Rac, membrane heterogeneity, caveolin and regulation of growth by integrins. Trends Cell Biol. 17, 246-250
    • (2007) Trends Cell Biol , vol.17 , pp. 246-250
    • Del Pozo, M.A.1    Schwartz, M.A.2
  • 120
    • 2542481699 scopus 로고    scopus 로고
    • The integrin β1 subunit transmembrane domain regulates phosphatidylinositol 3-kinase-dependent tyrosine phosphorylation of Crk-associated substrate
    • Armulik, A., Velling, T. and Johansson, S. (2004) The integrin β1 subunit transmembrane domain regulates phosphatidylinositol 3-kinase-dependent tyrosine phosphorylation of Crk-associated substrate. Mol. Biol. Cell 15, 2558-2567
    • (2004) Mol. Biol. Cell , vol.15 , pp. 2558-2567
    • Armulik, A.1    Velling, T.2    Johansson, S.3
  • 121
    • 11344254134 scopus 로고    scopus 로고
    • Velling, T., Nilsson, S., Stefansson, A. and Johansson, S. (2004) β1-Integrins induce phosphorylation of Akt on serine 473 independently of focal adhesion kinase and Src family kinases. EMBO Rep. 5, 901-905
    • Velling, T., Nilsson, S., Stefansson, A. and Johansson, S. (2004) β1-Integrins induce phosphorylation of Akt on serine 473 independently of focal adhesion kinase and Src family kinases. EMBO Rep. 5, 901-905
  • 122
    • 36749044792 scopus 로고    scopus 로고
    • EGFR and β1 integrins utilize different signaling pathways to activate Akt
    • Velling, T., Stefansson, A. and Johansson, S. (2008) EGFR and β1 integrins utilize different signaling pathways to activate Akt. Exp. Cell Res. 314, 309-316
    • (2008) Exp. Cell Res , vol.314 , pp. 309-316
    • Velling, T.1    Stefansson, A.2    Johansson, S.3
  • 123
    • 12344285901 scopus 로고    scopus 로고
    • Negative regulation of EGFR signalling through integrin-α1β1-mediated activation of protein tyrosine phosphatase TCPTP
    • Mattila, E., Pellinen, T., Nevo, J., Vuoriluoto, K., Arjonen, A. and Ivaska, J. (2005) Negative regulation of EGFR signalling through integrin-α1β1-mediated activation of protein tyrosine phosphatase TCPTP. Nat. Cell Biol. 7, 78-85
    • (2005) Nat. Cell Biol , vol.7 , pp. 78-85
    • Mattila, E.1    Pellinen, T.2    Nevo, J.3    Vuoriluoto, K.4    Arjonen, A.5    Ivaska, J.6
  • 124
    • 0031935043 scopus 로고    scopus 로고
    • Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase
    • Tiganis, T., Bennett, A. M., Ravichandran, K. S. and Tonks, N. K. (1998) Epidermal growth factor receptor and the adaptor protein p52Shc are specific substrates of T-cell protein tyrosine phosphatase. Mol. Cell. Biol. 18, 1622-1634
    • (1998) Mol. Cell. Biol , vol.18 , pp. 1622-1634
    • Tiganis, T.1    Bennett, A.M.2    Ravichandran, K.S.3    Tonks, N.K.4
  • 126
    • 0029872839 scopus 로고    scopus 로고
    • Trisomy 7p and malignant transformation of human breast epithelial cells following epidermal growth factor withdrawal
    • Briand, P., Nielsen, K. V., Madsen, M. W. and Petersen, O. W. (1996) Trisomy 7p and malignant transformation of human breast epithelial cells following epidermal growth factor withdrawal. Cancer Res. 56, 2039-2044
    • (1996) Cancer Res , vol.56 , pp. 2039-2044
    • Briand, P.1    Nielsen, K.V.2    Madsen, M.W.3    Petersen, O.W.4
  • 127
    • 0030936450 scopus 로고    scopus 로고
    • Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies
    • Weaver, V. M., Petersen, O. W., Wang, F., Larabell, C. A., Briand, P., Damsky, C. and Bissell, M. J. (1997) Reversion of the malignant phenotype of human breast cells in three-dimensional culture and in vivo by integrin blocking antibodies. J. Cell Biol. 137, 231-245
    • (1997) J. Cell Biol , vol.137 , pp. 231-245
    • Weaver, V.M.1    Petersen, O.W.2    Wang, F.3    Larabell, C.A.4    Briand, P.5    Damsky, C.6    Bissell, M.J.7
  • 129
    • 32944469169 scopus 로고    scopus 로고
    • β1 integrin inhibitory antibody induces apoptosis of breast cancer cells, inhibits growth, and distinguishes malignant from normal phenotype in three dimensional cultures and in vivo
    • Park, C. C., Zhang, H., Pallavicini, M., Gray, J. W., Baehner, F., Park, C. J. and Bissell, M. J. (2006) β1 integrin inhibitory antibody induces apoptosis of breast cancer cells, inhibits growth, and distinguishes malignant from normal phenotype in three dimensional cultures and in vivo. Cancer Res. 66, 1526-1535
    • (2006) Cancer Res , vol.66 , pp. 1526-1535
    • Park, C.C.1    Zhang, H.2    Pallavicini, M.3    Gray, J.W.4    Baehner, F.5    Park, C.J.6    Bissell, M.J.7
  • 130
    • 0037008761 scopus 로고    scopus 로고
    • Activation of BAD by therapeutic inhibition of epidermal growth factor receptor and transactivation by insulin-like growth factor receptor
    • Gilmore, A. P., Valentijn, A. J., Wang, P., Ranger, A. M., Bundred, N., O'Hare, M. J., Wakeling, A., Korsmeyer, S. J. and Streuli, C. H. (2002) Activation of BAD by therapeutic inhibition of epidermal growth factor receptor and transactivation by insulin-like growth factor receptor. J. Biol. Chem. 277, 27643-27650
    • (2002) J. Biol. Chem , vol.277 , pp. 27643-27650
    • Gilmore, A.P.1    Valentijn, A.J.2    Wang, P.3    Ranger, A.M.4    Bundred, N.5    O'Hare, M.J.6    Wakeling, A.7    Korsmeyer, S.J.8    Streuli, C.H.9
  • 131
    • 0034854417 scopus 로고    scopus 로고
    • ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial acini
    • Muthuswamy, S. K., Li, D., Lelievre, S., Bissell, M. J. and Brugge, J. S. (2001) ErbB2, but not ErbB1, reinitiates proliferation and induces luminal repopulation in epithelial acini. Nat. Cell Biol. 3, 785-792
    • (2001) Nat. Cell Biol , vol.3 , pp. 785-792
    • Muthuswamy, S.K.1    Li, D.2    Lelievre, S.3    Bissell, M.J.4    Brugge, J.S.5
  • 133
    • 5144235557 scopus 로고    scopus 로고
    • Targeted disruption of β1-integrin in a transgenic mouse model of human breast cancer reveals an essential role in mammary tumor induction
    • White, D. E., Kurpios, N. A., Zuo, D., Hassell, J. A., Blaess, S., Mueller, U. and Muller, W. J. (2004) Targeted disruption of β1-integrin in a transgenic mouse model of human breast cancer reveals an essential role in mammary tumor induction. Cancer Cell 6, 159-170
    • (2004) Cancer Cell , vol.6 , pp. 159-170
    • White, D.E.1    Kurpios, N.A.2    Zuo, D.3    Hassell, J.A.4    Blaess, S.5    Mueller, U.6    Muller, W.J.7
  • 134
    • 0141618355 scopus 로고    scopus 로고
    • EGF receptor mediates adhesion-dependent activation of the Rac GTPase: A role for phosphatidylinositol 3-kinase and Vav2
    • Marcoux, N. and Vuori, K. (2003) EGF receptor mediates adhesion-dependent activation of the Rac GTPase: a role for phosphatidylinositol 3-kinase and Vav2. Oncogene 22, 6100-6106
    • (2003) Oncogene , vol.22 , pp. 6100-6106
    • Marcoux, N.1    Vuori, K.2
  • 135
    • 33750353471 scopus 로고    scopus 로고
    • Rab11a differentially modulates epidermal growth factor-induced proliferation and motility in immortal breast cells
    • Palmieri, D., Bouadis, A., Ronchetti, R., Merino, M. J. and Steeg, P. S. (2006) Rab11a differentially modulates epidermal growth factor-induced proliferation and motility in immortal breast cells. Breast Cancer Res. Treat. 100, 127-137
    • (2006) Breast Cancer Res. Treat , vol.100 , pp. 127-137
    • Palmieri, D.1    Bouadis, A.2    Ronchetti, R.3    Merino, M.J.4    Steeg, P.S.5
  • 136
  • 137
    • 40849088170 scopus 로고    scopus 로고
    • Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization
    • Fielding, A. B., Dobreva, I., McDonald, P. C., Foster, L. J. and Dedhar, S. (2008) Integrin-linked kinase localizes to the centrosome and regulates mitotic spindle organization. J. Cell Biol. 180, 681-689
    • (2008) J. Cell Biol , vol.180 , pp. 681-689
    • Fielding, A.B.1    Dobreva, I.2    McDonald, P.C.3    Foster, L.J.4    Dedhar, S.5
  • 138
    • 27144495462 scopus 로고    scopus 로고
    • The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome
    • Pugacheva, E. N. and Golemis, E. A. (2005) The focal adhesion scaffolding protein HEF1 regulates activation of the Aurora-A and Nek2 kinases at the centrosome. Nat. Cell Biol. 7, 937-946
    • (2005) Nat. Cell Biol , vol.7 , pp. 937-946
    • Pugacheva, E.N.1    Golemis, E.A.2
  • 139
    • 33744488545 scopus 로고    scopus 로고
    • Cellular mechanotransduction: Putting all the pieces together again
    • Ingber, D. E. (2006) Cellular mechanotransduction: putting all the pieces together again. FASEB J. 20, 811-827
    • (2006) FASEB J , vol.20 , pp. 811-827
    • Ingber, D.E.1
  • 140
    • 33846140462 scopus 로고    scopus 로고
    • KASH-domain proteins in nuclear migration, anchorage and other processes
    • Wilhelmsen, K., Ketema, M., Truong, H. and Sonnenberg, A. (2006) KASH-domain proteins in nuclear migration, anchorage and other processes. J. Cell Sci. 119, 5021-5029
    • (2006) J. Cell Sci , vol.119 , pp. 5021-5029
    • Wilhelmsen, K.1    Ketema, M.2    Truong, H.3    Sonnenberg, A.4
  • 141
    • 34547108380 scopus 로고    scopus 로고
    • JAK-STAT signaling: From interferons to cytokines
    • Schindler, C., Levy, D. E. and Decker, T. (2007) JAK-STAT signaling: from interferons to cytokines. J. Biol. Chem. 282, 20059-20063
    • (2007) J. Biol. Chem , vol.282 , pp. 20059-20063
    • Schindler, C.1    Levy, D.E.2    Decker, T.3
  • 142
    • 33847351136 scopus 로고    scopus 로고
    • The JAK-STAT signaling pathway: Input and output integration
    • Murray, P. J. (2007) The JAK-STAT signaling pathway: input and output integration. J. Immunol. 178, 2623-2629
    • (2007) J. Immunol , vol.178 , pp. 2623-2629
    • Murray, P.J.1
  • 143
    • 0034757830 scopus 로고    scopus 로고
    • Prolactin receptor signal transduction
    • Clevenger, C. V. and Kline, J. B. (2001) Prolactin receptor signal transduction. Lupus 10, 706-718
    • (2001) Lupus , vol.10 , pp. 706-718
    • Clevenger, C.V.1    Kline, J.B.2
  • 144
    • 33845663497 scopus 로고    scopus 로고
    • SH2B1 (SH2-B) and JAK2: A multifunctional adaptor protein and kinase made for each other
    • Maures, T. J., Kurzer, J. H. and Carter-Su, C. (2007) SH2B1 (SH2-B) and JAK2: a multifunctional adaptor protein and kinase made for each other. Trends Endocrinol. Metab. 18, 38-45
    • (2007) Trends Endocrinol. Metab , vol.18 , pp. 38-45
    • Maures, T.J.1    Kurzer, J.H.2    Carter-Su, C.3
  • 145
    • 37549002500 scopus 로고    scopus 로고
    • IRAK1: A critical signaling mediator of innate immunity
    • Gottipati, S., Rao, N. L. and Fung-Leung, W. P. (2008) IRAK1: a critical signaling mediator of innate immunity. Cell. Signalling 20, 269-276
    • (2008) Cell. Signalling , vol.20 , pp. 269-276
    • Gottipati, S.1    Rao, N.L.2    Fung-Leung, W.P.3
  • 146
    • 34247855063 scopus 로고    scopus 로고
    • Effect of the α3β1 integrin on the IL-1 stimulated activation of c-Jun N-terminal kinase (JNK) in CACO-2 cells
    • Stulic, M., Lubin, F. D., O'Donnell, P. M., Tammariello, S. P. and McGee, D. W. (2007) Effect of the α3β1 integrin on the IL-1 stimulated activation of c-Jun N-terminal kinase (JNK) in CACO-2 cells. Cytokine 37, 163-170
    • (2007) Cytokine , vol.37 , pp. 163-170
    • Stulic, M.1    Lubin, F.D.2    O'Donnell, P.M.3    Tammariello, S.P.4    McGee, D.W.5
  • 148
    • 33847611278 scopus 로고    scopus 로고
    • Integrin regulation of mammary gland development
    • Danen, E, ed, pp, Landes Bioscience, Georgetown, TX, U.S.A
    • Naylor, M. J. and Streuli, C. H. (2006) Integrin regulation of mammary gland development. In Integrins and Development (Danen, E., ed.), pp. 176-185, Landes Bioscience, Georgetown, TX, U.S.A.
    • (2006) Integrins and Development , pp. 176-185
    • Naylor, M.J.1    Streuli, C.H.2
  • 149
    • 34247551118 scopus 로고    scopus 로고
    • The alveolar switch: Coordinating the proliferative cues and cell fate decisions that drive the formation of lobuloalveoli from ductal epithelium
    • Oakes, S. R., Hilton, H. N. and Ormandy, C. J. (2006) The alveolar switch: coordinating the proliferative cues and cell fate decisions that drive the formation of lobuloalveoli from ductal epithelium. Breast Cancer Res. 8, 207
    • (2006) Breast Cancer Res , vol.8 , pp. 207
    • Oakes, S.R.1    Hilton, H.N.2    Ormandy, C.J.3
  • 150
    • 0032540383 scopus 로고    scopus 로고
    • Regulation of mammary differentiation by extracellular matrix involves protein-tyrosine phosphatases
    • Edwards, G. M., Wilford, F. H., Liu, X., Hennighausen, L., Djiane, J. and Streuli, C. H. (1998) Regulation of mammary differentiation by extracellular matrix involves protein-tyrosine phosphatases. J. Biol. Chem. 273, 9495-9500
    • (1998) J. Biol. Chem , vol.273 , pp. 9495-9500
    • Edwards, G.M.1    Wilford, F.H.2    Liu, X.3    Hennighausen, L.4    Djiane, J.5    Streuli, C.H.6
  • 151
    • 33747423320 scopus 로고    scopus 로고
    • Rac1 links integrin-mediated adhesion to the control of lactational differentiation in mammary epithelia
    • Akhtar, N. and Streuli, C. H. (2006) Rac1 links integrin-mediated adhesion to the control of lactational differentiation in mammary epithelia. J. Cell Biol. 173, 781-793
    • (2006) J. Cell Biol , vol.173 , pp. 781-793
    • Akhtar, N.1    Streuli, C.H.2
  • 154
    • 66149121885 scopus 로고    scopus 로고
    • Molecular dissection of integrin signalling proteins in the control of mammary epithelial development and differentiation
    • doi:10.1242/ dev.028423
    • Akhtar, N., Marlow, R., Lambert, E., Schatzmann, F., Lowe, E. T., Cheung, J., Katz, E., Li, W., Wu, C., Dedhar, S. et al. (2009) Molecular dissection of integrin signalling proteins in the control of mammary epithelial development and differentiation. Development, doi:10.1242/ dev.028423
    • (2009) Development
    • Akhtar, N.1    Marlow, R.2    Lambert, E.3    Schatzmann, F.4    Lowe, E.T.5    Cheung, J.6    Katz, E.7    Li, W.8    Wu, C.9    Dedhar, S.10
  • 155
    • 0037936545 scopus 로고    scopus 로고
    • Essential functions of p21-activated kinase 1 in morphogenesis and differentiation of mammary glands
    • Wang, R. A., Vadlamudi, R. K., Bagheri-Yarmand, R., Beuvink, I., Hynes, N. E. and Kumar, R. (2003) Essential functions of p21-activated kinase 1 in morphogenesis and differentiation of mammary glands. J. Cell Biol. 161, 583-592
    • (2003) J. Cell Biol , vol.161 , pp. 583-592
    • Wang, R.A.1    Vadlamudi, R.K.2    Bagheri-Yarmand, R.3    Beuvink, I.4    Hynes, N.E.5    Kumar, R.6
  • 156
    • 59849098041 scopus 로고    scopus 로고
    • Sustained activation of STAT5 is essential for chromatin remodeling and maintenance of mammary-specific function
    • Xu, R., Nelson, C. M., Muschler, J. L., Veiseh, M., Vonderhaar, B. K. and Bissell, M. J. (2009) Sustained activation of STAT5 is essential for chromatin remodeling and maintenance of mammary-specific function. J. Cell Biol. 184, 57-66
    • (2009) J. Cell Biol , vol.184 , pp. 57-66
    • Xu, R.1    Nelson, C.M.2    Muschler, J.L.3    Veiseh, M.4    Vonderhaar, B.K.5    Bissell, M.J.6
  • 157
    • 0037385662 scopus 로고    scopus 로고
    • PKCε is a permissive link in integrin-dependent IFN-γ signalling that facilitates JAK phosphorylation of STAT1
    • Ivaska, J., Bosca, L. and Parker, P. J. (2003) PKCε is a permissive link in integrin-dependent IFN-γ signalling that facilitates JAK phosphorylation of STAT1. Nat. Cell Biol. 5, 363-369
    • (2003) Nat. Cell Biol , vol.5 , pp. 363-369
    • Ivaska, J.1    Bosca, L.2    Parker, P.J.3
  • 158
    • 0033565261 scopus 로고    scopus 로고
    • PKCα regulates β1 integrin-dependent cell motility through association and control of integrin traffic
    • Ng, T., Shima, D., Squire, A., Bastiaens, P. I., Gschmeissner, S., Humphries, M. J. and Parker, P. J. (1999) PKCα regulates β1 integrin-dependent cell motility through association and control of integrin traffic. EMBO J. 18, 3909-3923
    • (1999) EMBO J , vol.18 , pp. 3909-3923
    • Ng, T.1    Shima, D.2    Squire, A.3    Bastiaens, P.I.4    Gschmeissner, S.5    Humphries, M.J.6    Parker, P.J.7
  • 159
    • 0037099313 scopus 로고    scopus 로고
    • PKCε controls the traffic of β1 integrins in motile cells
    • Ivaska, J., Whelan, R. D., Watson, R. and Parker, P. J. (2002) PKCε controls the traffic of β1 integrins in motile cells. EMBO J. 21, 3608-3619
    • (2002) EMBO J , vol.21 , pp. 3608-3619
    • Ivaska, J.1    Whelan, R.D.2    Watson, R.3    Parker, P.J.4
  • 163
    • 34047257842 scopus 로고    scopus 로고
    • Cellular adhesion responses to the heparin-binding (HepII) domain of fibronectin require heparan sulfate with specific properties
    • Mahalingam, Y., Gallagher, J. T. and Couchman, J. R. (2007) Cellular adhesion responses to the heparin-binding (HepII) domain of fibronectin require heparan sulfate with specific properties. J. Biol. Chem. 282, 3221-3230
    • (2007) J. Biol. Chem , vol.282 , pp. 3221-3230
    • Mahalingam, Y.1    Gallagher, J.T.2    Couchman, J.R.3
  • 164
    • 0345169052 scopus 로고    scopus 로고
    • Syndecans: Proteoglycan regulators of cell-surface microdomains?
    • Couchman, J. R. (2003) Syndecans: proteoglycan regulators of cell-surface microdomains? Nat. Rev. Mol. Cell Biol. 4, 926-937
    • (2003) Nat. Rev. Mol. Cell Biol , vol.4 , pp. 926-937
    • Couchman, J.R.1
  • 167
    • 5444242206 scopus 로고    scopus 로고
    • The syndecan-1 ectodomain regulates αvβ3 integrin activity in human mammary carcinoma cells
    • Beauvais, D. M., Burbach, B. J. and Rapraeger, A. C. (2004) The syndecan-1 ectodomain regulates αvβ3 integrin activity in human mammary carcinoma cells. J. Cell Biol. 167, 171-181
    • (2004) J. Cell Biol , vol.167 , pp. 171-181
    • Beauvais, D.M.1    Burbach, B.J.2    Rapraeger, A.C.3
  • 168
    • 36448970493 scopus 로고    scopus 로고
    • Synergistic control of cell adhesion by integrins and syndecans
    • Morgan, M. R., Humphries, M. J. and Bass, M. D. (2007) Synergistic control of cell adhesion by integrins and syndecans. Nat. Rev. Mol. Cell Biol. 8, 957-969
    • (2007) Nat. Rev. Mol. Cell Biol , vol.8 , pp. 957-969
    • Morgan, M.R.1    Humphries, M.J.2    Bass, M.D.3
  • 169
    • 0032925217 scopus 로고    scopus 로고
    • Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13
    • Bloom, L., Ingham, K. C. and Hynes, R. O. (1999) Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13. Mol. Biol. Cell. 10, 1521-1536
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1521-1536
    • Bloom, L.1    Ingham, K.C.2    Hynes, R.O.3
  • 171
  • 174
    • 45349086241 scopus 로고    scopus 로고
    • p190RhoGAP is the convergence point of adhesion signals from α5β1 integrin and syndecan-4
    • Bass, M. D., Morgan, M. R., Roach, K. A., Settleman, J., Goryachev, A. B. and Humphries, M. J. (2008) p190RhoGAP is the convergence point of adhesion signals from α5β1 integrin and syndecan-4. J. Cell Biol. 181, 1013-1026
    • (2008) J. Cell Biol , vol.181 , pp. 1013-1026
    • Bass, M.D.1    Morgan, M.R.2    Roach, K.A.3    Settleman, J.4    Goryachev, A.B.5    Humphries, M.J.6
  • 175
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Kiosses, W. B. and Schwartz, M. A. (1999) Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578-585
    • (1999) EMBO J , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 176
    • 33746918654 scopus 로고    scopus 로고
    • PKCβ-dependent activation of RhoA by syndecan-4 during focal adhesion formation
    • Dovas, A., Yoneda, A. and Couchman, J. R. (2006) PKCβ-dependent activation of RhoA by syndecan-4 during focal adhesion formation. J. Cell Sci. 119, 2837-2846
    • (2006) J. Cell Sci , vol.119 , pp. 2837-2846
    • Dovas, A.1    Yoneda, A.2    Couchman, J.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.