메뉴 건너뛰기




Volumn 32, Issue 2, 2000, Pages 171-188

Bi-directional signal transduction by integrin receptors

Author keywords

[No Author keywords available]

Indexed keywords

FOCAL ADHESION KINASE; INTEGRIN RECEPTOR; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE;

EID: 0033986923     PISSN: 13572725     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1357-2725(99)00043-6     Document Type: Article
Times cited : (137)

References (154)
  • 1
    • 0025218924 scopus 로고
    • VLA Proteins in the integrin family: Structures, functions, and their role on leukocytes
    • Hemler M.E. VLA Proteins in the integrin family: structures, functions, and their role on leukocytes. Annu. Rev. Immunol. 8:1990;365-400.
    • (1990) Annu. Rev. Immunol. , vol.8 , pp. 365-400
    • Hemler, M.E.1
  • 2
    • 0002550182 scopus 로고
    • Integrins as receptors for extracellular matrix
    • E.D. Hay. New York: Plenum Press
    • Ruoslahti E. Integrins as receptors for extracellular matrix. Hay E.D. Cell Biology of Extracellular Matrix. 2nd ed. 1991;343-363 Plenum Press, New York.
    • (1991) Cell Biology of Extracellular Matrix 2nd Ed. , pp. 343-363
    • Ruoslahti, E.1
  • 3
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signalling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation, and signalling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 4
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • Hynes R.O. Integrins: a family of cell surface receptors. Cell. 48:1987;549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 5
    • 0025205276 scopus 로고
    • Integrins and other cell adhesion molecules
    • Albelda S.M., Buck C.A. Integrins and other cell adhesion molecules. The FASEB Journal. 4:1990;2868-2880.
    • (1990) The FASEB Journal , vol.4 , pp. 2868-2880
    • Albelda, S.M.1    Buck, C.A.2
  • 7
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • Juliano R.L., Haskill S. Signal transduction from the extracellular matrix. J. Cell Biol. 120:(3):1993;577-585.
    • (1993) J. Cell Biol. , vol.120 , Issue.3 , pp. 577-585
    • Juliano, R.L.1    Haskill, S.2
  • 8
    • 0027170760 scopus 로고
    • A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells
    • Schwartz M.A., Brown E.J., Fazeli B. A 50-kDa integrin-associated protein is required for integrin-regulated calcium entry in endothelial cells. J. Biol. Chem. 268:1993;19931-19934.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19931-19934
    • Schwartz, M.A.1    Brown, E.J.2    Fazeli, B.3
  • 9
    • 0025182959 scopus 로고
    • Adhesion receptors of the immune system
    • Springer T.A. Adhesion receptors of the immune system. Nature. 346:1990;425-434.
    • (1990) Nature , vol.346 , pp. 425-434
    • Springer, T.A.1
  • 15
    • 0025720737 scopus 로고
    • Cell type-specific integrin variants with alternative α chain cytoplasmic domains
    • Tamura R.N., Copper H.M., Collo G., Quaranta V. Cell type-specific integrin variants with alternative α chain cytoplasmic domains. Proc. Natl. Acad. Sci. U.S.A. 88:1991;10183-10187.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 10183-10187
    • Tamura, R.N.1    Copper, H.M.2    Collo, G.3    Quaranta, V.4
  • 16
    • 0030272735 scopus 로고    scopus 로고
    • Integrin cytoplasmic interactions and bidirectional transmembrane signalling
    • Dedhar S., Hannigan G.E. Integrin cytoplasmic interactions and bidirectional transmembrane signalling. Curr. Opin. Cell Biol. 8:1996;657-669.
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 657-669
    • Dedhar, S.1    Hannigan, G.E.2
  • 17
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin - A transmembrane linkage
    • Horwitz A., Duggan K., Buck C., Beckerle M.C., Burridge K. Interaction of plasma membrane fibronectin receptor with talin - a transmembrane linkage. Nature. 320:1986;531-533.
    • (1986) Nature , vol.320 , pp. 531-533
    • Horwitz, A.1    Duggan, K.2    Buck, C.3    Beckerle, M.C.4    Burridge, K.5
  • 18
    • 0024150623 scopus 로고
    • Focal adhesions: Transmembrane junctions between the extracellular matrix and the cytoskeleton
    • Burridge K., Fath K., Kelly T., Nuckolls C., Turner C. Focal adhesions: transmembrane junctions between the extracellular matrix and the cytoskeleton. Annu. Rev. Cell. Biol. 4:1988;487-525.
    • (1988) Annu. Rev. Cell. Biol. , vol.4 , pp. 487-525
    • Burridge, K.1    Fath, K.2    Kelly, T.3    Nuckolls, C.4    Turner, C.5
  • 23
    • 0033033953 scopus 로고    scopus 로고
    • The role of integrins in immune-mediated diseases of the nervous system
    • Archelos J.J., Previtali S.C., Hartung P. The role of integrins in immune-mediated diseases of the nervous system. Trends Neurosci. 22:1999;30-38.
    • (1999) Trends Neurosci. , vol.22 , pp. 30-38
    • Archelos, J.J.1    Previtali, S.C.2    Hartung, P.3
  • 24
    • 0027373782 scopus 로고
    • 1 integrin-mediated cell spreading on fibronectin
    • 1 integrin-mediated cell spreading on fibronectin. J. Biol. Chem. 268:1993;21459-21462.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21459-21462
    • Vuori, K.1    Ruoslahti, E.2
  • 25
    • 0024828456 scopus 로고
    • Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes
    • van Kooyk Y., van de Wiel-van Kemenade P., Weder P., Kuijpers T.W., Figdor C.G. Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes. Nature. 342:1989;811-813.
    • (1989) Nature , vol.342 , pp. 811-813
    • Van Kooyk, Y.1    Van De Wiel-Van, K.P.2    Weder, P.3    Kuijpers, T.W.4    Figdor, C.G.5
  • 28
    • 0030872850 scopus 로고    scopus 로고
    • Adhesive interactions in the immune system
    • Brown E.J. Adhesive interactions in the immune system. Trends in Cell Biology. 7:1997;289-295.
    • (1997) Trends in Cell Biology , vol.7 , pp. 289-295
    • Brown, E.J.1
  • 29
    • 0030878409 scopus 로고    scopus 로고
    • Perspectives series: Cell adhesion in vascular biology. Integrin signaling in vascular biology
    • Shattil S.J., Ginsberg M.H. Perspectives series: cell adhesion in vascular biology. Integrin signaling in vascular biology. J. Clin. Invest. 100:1997;1-5.
    • (1997) J. Clin. Invest. , vol.100 , pp. 1-5
    • Shattil, S.J.1    Ginsberg, M.H.2
  • 30
    • 0028446566 scopus 로고
    • The dynamic regulation of integrin adhesiveness
    • Diamond M.S., Springer T.A. The dynamic regulation of integrin adhesiveness. Curr. Biol. 4:1994;506-517.
    • (1994) Curr. Biol. , vol.4 , pp. 506-517
    • Diamond, M.S.1    Springer, T.A.2
  • 31
    • 0029913643 scopus 로고    scopus 로고
    • Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes
    • Kucik D.F., Dustin M.L., Miller J.M., Brown E.J. Adhesion-activating phorbol ester increases the mobility of leukocyte integrin LFA-1 in cultured lymphocytes. J. Clin. Invest. 97:1996;2139-2144.
    • (1996) J. Clin. Invest. , vol.97 , pp. 2139-2144
    • Kucik, D.F.1    Dustin, M.L.2    Miller, J.M.3    Brown, E.J.4
  • 32
    • 0025990521 scopus 로고
    • The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 β subunit: Sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site
    • Hibbs M.L., Jakes S., Stacker S.A., Wallace R.W., Springer T.A. The cytoplasmic domain of the integrin lymphocyte function-associated antigen 1 β subunit: sites required for binding to intercellular adhesion molecule 1 and the phorbol ester-stimulated phosphorylation site. J. Exp. Med. 174:1991;1227-1238.
    • (1991) J. Exp. Med. , vol.174 , pp. 1227-1238
    • Hibbs, M.L.1    Jakes, S.2    Stacker, S.A.3    Wallace, R.W.4    Springer, T.A.5
  • 37
    • 0027398448 scopus 로고
    • A subpopulation of Mac-1 (CD11b/CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen
    • Diamond M.S., Springer T.A. A subpopulation of Mac-1 (CD11b/CD18) molecules mediates neutrophil adhesion to ICAM-1 and fibrinogen. J. Cell Biol. 120:1993;545-556.
    • (1993) J. Cell Biol. , vol.120 , pp. 545-556
    • Diamond, M.S.1    Springer, T.A.2
  • 39
    • 0028786294 scopus 로고
    • Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix
    • Wu C., Keivens V.M., O'Toole T.E., McDonald J.A., Ginsberg M.H. Integrin activation and cytoskeletal interaction are essential for the assembly of a fibronectin matrix. Cell. 83:1995;715-724.
    • (1995) Cell , vol.83 , pp. 715-724
    • Wu, C.1    Keivens, V.M.2    O'Toole, T.E.3    McDonald, J.A.4    Ginsberg, M.H.5
  • 40
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes P.E., O'Toole T.E., Ylanne J., Shattil S.J., Ginsberg M.H. The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J. Biol. Chem. 270:1995;12411-12417.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylanne, J.3    Shattil, S.J.4    Ginsberg, M.H.5
  • 41
    • 0032523064 scopus 로고    scopus 로고
    • Integrin signaling: The platelet paradigm
    • Shattil S.J., Kashiwagi H., Pampori N. Integrin signaling: the platelet paradigm. Blood. 91:1998;2645-2657.
    • (1998) Blood , vol.91 , pp. 2645-2657
    • Shattil, S.J.1    Kashiwagi, H.2    Pampori, N.3
  • 42
    • 0032497918 scopus 로고    scopus 로고
    • Glycoprotein IIb/IIIa integrin blockade
    • Madan M., Berkowitz S.D., Tcheng E. Glycoprotein IIb/IIIa integrin blockade. Circulation. 98:1998;2629-2635.
    • (1998) Circulation , vol.98 , pp. 2629-2635
    • Madan, M.1    Berkowitz, S.D.2    Tcheng, E.3
  • 43
    • 0029062761 scopus 로고
    • Mechanisms of disease: Platelet glycoprotein IIb/IIIa receptors in cardiovascular medicine
    • Lefkovits J., Plow E.F., Topol E.J. Mechanisms of disease: platelet glycoprotein IIb/IIIa receptors in cardiovascular medicine. N. Engl. J. Med. 332:1995;1553.
    • (1995) N. Engl. J. Med. , vol.332 , pp. 1553
    • Lefkovits, J.1    Plow, E.F.2    Topol, E.J.3
  • 44
    • 0030999134 scopus 로고    scopus 로고
    • Platelet GPIIb/IIIa antagonists: The first anti-integrin receptor therapeutics
    • Coller B.S. Platelet GPIIb/IIIa antagonists: the first anti-integrin receptor therapeutics. J. Clin. Invest. 99:1997;1467.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1467
    • Coller, B.S.1
  • 46
    • 0029916875 scopus 로고    scopus 로고
    • 3-(GPIIb IIIa) tyrosine phosphorylation induced by platelet aggregation
    • 3-(GPIIb IIIa) tyrosine phosphorylation induced by platelet aggregation. J. Biol. Chem. 271:1996;10811-10815.
    • (1996) J. Biol. Chem. , vol.271 , pp. 10811-10815
    • Law, D.A.1    Nannizzi-Alaimo, L.2    Phillips, D.R.3
  • 50
    • 0031034352 scopus 로고    scopus 로고
    • Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness
    • [published erratum appears in Nature 1997 July 10;388(6638):210]
    • Palecek S.P., Loftus J.C., Ginsberg M.H., Lauffenburger D.A., Horwitz A.F. Integrin-ligand binding properties govern cell migration speed through cell-substratum adhesiveness. Nature. 385:1997;537-540. [published erratum appears in Nature 1997 July 10;388(6638):210].
    • (1997) Nature , vol.385 , pp. 537-540
    • Palecek, S.P.1    Loftus, J.C.2    Ginsberg, M.H.3    Lauffenburger, D.A.4    Horwitz, A.F.5
  • 51
    • 0024443411 scopus 로고
    • T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1
    • Dustin M.L., Springer T.A. T-cell receptor cross-linking transiently stimulates adhesiveness through LFA-1. Nature. 341:1989;619-624.
    • (1989) Nature , vol.341 , pp. 619-624
    • Dustin, M.L.1    Springer, T.A.2
  • 52
    • 0025363922 scopus 로고
    • Regulated expression and binding of three VLA integrin receptors on T cells
    • Shimizu Y., van Seventer G., Horgan K.J., Shaw S. Regulated expression and binding of three VLA integrin receptors on T cells. Nature. 354:1990;250-253.
    • (1990) Nature , vol.354 , pp. 250-253
    • Shimizu, Y.1    Van Seventer, G.2    Horgan, K.J.3    Shaw, S.4
  • 53
    • 0028221289 scopus 로고
    • Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor alpha-receptor
    • Vassbotn F.S., Havnen O.K., Heldin C.H., Holmsen H. Negative feedback regulation of human platelets via autocrine activation of the platelet-derived growth factor alpha-receptor. J. Biol. Chem. 269:1994;13874-13879.
    • (1994) J. Biol. Chem. , vol.269 , pp. 13874-13879
    • Vassbotn, F.S.1    Havnen, O.K.2    Heldin, C.H.3    Holmsen, H.4
  • 55
    • 0028335948 scopus 로고
    • Anchorage independence, integrins and apoptosis
    • Ruoslahti E., Reed J. Anchorage independence, integrins and apoptosis. Cell. 77:1994;477-478.
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.2
  • 56
    • 0030870247 scopus 로고    scopus 로고
    • The extracellular matrix and mitogenic growth factors control G1 phase cyclins and cyclin-dependent kinase inhibitors
    • Bottazzi M.E., Assoian R.K. The extracellular matrix and mitogenic growth factors control G1 phase cyclins and cyclin-dependent kinase inhibitors. Trends in Cell Biology. 7:1997;348-352.
    • (1997) Trends in Cell Biology , vol.7 , pp. 348-352
    • Bottazzi, M.E.1    Assoian, R.K.2
  • 57
    • 0027451706 scopus 로고
    • The extracellular matrix as a survival factor
    • Meredith J., Bazeli B., Schwartz M. The extracellular matrix as a survival factor. Mol. Biol. Cell. 4:1993;953-961.
    • (1993) Mol. Biol. Cell. , vol.4 , pp. 953-961
    • Meredith, J.1    Bazeli, B.2    Schwartz, M.3
  • 58
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch S.M., Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124:1994;619-626.
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 59
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • Boudreau N., Sympson C.J., Werb Z., Bissell M.J. Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix. Science. 267:1995;891-893.
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 61
    • 0026768210 scopus 로고
    • Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution
    • Talhouk R.S., Bissell M.J., Werb Z. Coordinated expression of extracellular matrix-degrading proteinases and their inhibitors regulates mammary epithelial function during involution. J. Cell Biol. 118:1992;1271-1282.
    • (1992) J. Cell Biol. , vol.118 , pp. 1271-1282
    • Talhouk, R.S.1    Bissell, M.J.2    Werb, Z.3
  • 62
    • 0028818755 scopus 로고
    • Signals for death and survival: A two-step mechanism for cavitation in the vertebrate embryo
    • Coucouvanis E., Martin G.R. Signals for death and survival: a two-step mechanism for cavitation in the vertebrate embryo. Cell. 83:1995;279-287.
    • (1995) Cell , vol.83 , pp. 279-287
    • Coucouvanis, E.1    Martin, G.R.2
  • 63
    • 0030028947 scopus 로고    scopus 로고
    • Cytoskeletal integrity is required throughout the mitogen stimulation phase of the cell cycle and mediates the anchorage-dependent expression of cyclin D1
    • Bohmer R.M., Scharf E., Assoian R.K. Cytoskeletal integrity is required throughout the mitogen stimulation phase of the cell cycle and mediates the anchorage-dependent expression of cyclin D1. Mol. Biol. Cell. 7:1996;101-111.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 101-111
    • Bohmer, R.M.1    Scharf, E.2    Assoian, R.K.3
  • 64
    • 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., Assoian R.K. 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. 133:1996;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
  • 65
    • 0030027049 scopus 로고    scopus 로고
    • Dependence of cyclin E-CDK2 kinase activity on cell anchorage
    • Fang F., Orend G., Watanabe N., Hunter T., Ruoslahti E. Dependence of cyclin E-CDK2 kinase activity on cell anchorage. Science. 271:1996;499-502.
    • (1996) Science , vol.271 , pp. 499-502
    • Fang, F.1    Orend, G.2    Watanabe, N.3    Hunter, T.4    Ruoslahti, E.5
  • 66
    • 0028904784 scopus 로고
    • Integrin-dependent activation of MAP kinase: A link to shape-dependent cell proliferation
    • Zhu X., Assoian R.K. Integrin-dependent activation of MAP kinase: a link to shape-dependent cell proliferation. Mol. Biol. Cell. 6:1995;273-282.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 273-282
    • Zhu, X.1    Assoian, R.K.2
  • 67
    • 0030584077 scopus 로고    scopus 로고
    • The adaptor protein Shc couples a class of integrins to the control of cell cycle progression
    • Wary K.K., Mainiero F., Isakoff S.J., Marcantonio E.E., Giancotti F.G. The adaptor protein Shc couples a class of integrins to the control of cell cycle progression. Cell. 87:1996;733-743.
    • (1996) Cell , vol.87 , pp. 733-743
    • Wary, K.K.1    Mainiero, F.2    Isakoff, S.J.3    Marcantonio, E.E.4    Giancotti, F.G.5
  • 69
    • 0030458602 scopus 로고    scopus 로고
    • A role for Jun-N-terminal kinase in anoikis; Suppression by bcl-2 and crmA
    • Frisch S.M., Vuori K., Kelaita D., Sicks S. A role for Jun-N-terminal kinase in anoikis; suppression by bcl-2 and crmA. J. Cell Biol. 135:1996;1377-1382.
    • (1996) J. Cell Biol. , vol.135 , pp. 1377-1382
    • Frisch, S.M.1    Vuori, K.2    Kelaita, D.3    Sicks, S.4
  • 70
    • 0030695034 scopus 로고    scopus 로고
    • 2-terminal kinase and induction of apoptosis after detachment of epithelial cells
    • 2-terminal kinase and induction of apoptosis after detachment of epithelial cells. J. Cell Biol. 139:1997;1017-1023.
    • (1997) J. Cell Biol. , vol.139 , pp. 1017-1023
    • Khwaja, A.1    Downward, J.2
  • 72
    • 0028040019 scopus 로고
    • Bcl-2 and the regulation of programmed cell death
    • Reed J.C. Bcl-2 and the regulation of programmed cell death. J. Cell Biol. 124:1994;1-6.
    • (1994) J. Cell Biol. , vol.124 , pp. 1-6
    • Reed, J.C.1
  • 73
    • 0030755579 scopus 로고    scopus 로고
    • The regulation of anoikis: MEKK-1 activation requires cleavage by caspases
    • Cardone M.H., Salvesen G.S., Widmann C., Johnson G., Frisch S.M. The regulation of anoikis: MEKK-1 activation requires cleavage by caspases. Cell. 90:1997;315-323.
    • (1997) Cell , vol.90 , pp. 315-323
    • Cardone, M.H.1    Salvesen, G.S.2    Widmann, C.3    Johnson, G.4    Frisch, S.M.5
  • 79
    • 0025741870 scopus 로고
    • Calcium signaling capacity of the CDIIb/CD18 integrin on human neutrophils
    • Ng-Sikorski J., Andersson R., Patarroyo M., Andersson T. Calcium signaling capacity of the CDIIb/CD18 integrin on human neutrophils. Exp. Cell Res. 195:1991;504-508.
    • (1991) Exp. Cell Res. , vol.195 , pp. 504-508
    • Ng-Sikorski, J.1    Andersson, R.2    Patarroyo, M.3    Andersson, T.4
  • 80
    • 0027397549 scopus 로고
    • Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium
    • Schwartz M.A. Spreading of human endothelial cells on fibronectin or vitronectin triggers elevation of intracellular free calcium. J. Cell Biol. 120:1992;1003-1009.
    • (1992) J. Cell Biol. , vol.120 , pp. 1003-1009
    • Schwartz, M.A.1
  • 82
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kD protein
    • Guan J.L., Trevithick J.E., Hynes R.O. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120 kD protein. Cell Regul. 2:1991;951-964.
    • (1991) Cell Regul. , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 83
    • 0025946283 scopus 로고
    • Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by integrin clustering
    • Kornberg L.J., Earp H.S., Turner C.E., Prockop C., Juliano R.L. Signal transduction by integrins: Increased protein tyrosine phosphorylation caused by integrin clustering. Proc. Natl. Acad. Sci. U.S.A. 88:1991;8392-8396.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 8392-8396
    • Kornberg, L.J.1    Earp, H.S.2    Turner, C.E.3    Prockop, C.4    Juliano, R.L.5
  • 86
    • 0027176804 scopus 로고
    • Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown
    • McNamee H.P., Ingber D.E., Schwartz M.A. Adhesion to fibronectin stimulates inositol lipid synthesis and enhances PDGF-induced inositol lipid breakdown. J. Cell Biol. 121:1993;673-678.
    • (1993) J. Cell Biol. , vol.121 , pp. 673-678
    • McNamee, H.P.1    Ingber, D.E.2    Schwartz, M.A.3
  • 87
    • 0029827248 scopus 로고    scopus 로고
    • Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin-dependent pathway
    • Schwartz M.A., Toksoz D., Khosravi-Far R. Transformation by Rho exchange factor oncogenes is mediated by activation of an integrin-dependent pathway. EMBO J. 15:1996;6525-6530.
    • (1996) EMBO J. , vol.15 , pp. 6525-6530
    • Schwartz, M.A.1    Toksoz, D.2    Khosravi-Far, R.3
  • 88
    • 0030913673 scopus 로고    scopus 로고
    • Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway
    • Khwaja A., Rodriguez-Viciana P., Wennstrom S., Warne P.H., Downward J. Matrix adhesion and Ras transformation both activate a phosphoinositide 3-OH kinase and protein kinase B/Akt cellular survival pathway. EMBO J. 16:1997;2783-2793.
    • (1997) EMBO J. , vol.16 , pp. 2783-2793
    • Khwaja, A.1    Rodriguez-Viciana, P.2    Wennstrom, S.3    Warne, P.H.4    Downward, J.5
  • 89
    • 0028557342 scopus 로고
    • Extracellular matrix-dependent tissue-specific gene expression in mammary epithelial cells requires both physical and biochemical signal transduction
    • Roskelley C.D., Desprez P.Y., Bissell M.J. Extracellular matrix-dependent tissue-specific gene expression in mammary epithelial cells requires both physical and biochemical signal transduction. Proc. Natl. Acad. Sci. U.S.A. 91:1994;12378-12382.
    • (1994) Proc. Natl. Acad. Sci. U.S.A. , vol.91 , pp. 12378-12382
    • Roskelley, C.D.1    Desprez, P.Y.2    Bissell, M.J.3
  • 90
    • 0029119564 scopus 로고
    • A hierarchy of ECM-mediated signalling regulates tissue-specific gene expression
    • Roskelley C.D., Srebrow A., Bissell M.J. A hierarchy of ECM-mediated signalling regulates tissue-specific gene expression. Curr. Opin. Cell Biol. 7:1995;736-747.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 736-747
    • Roskelley, C.D.1    Srebrow, A.2    Bissell, M.J.3
  • 91
    • 0026756730 scopus 로고
    • Integrins as a primary signal transduction molecule regulating monocyte immediate-early gene induction
    • Yurochko A.D., Liu D.Y., Eierman D., Haskill S. Integrins as a primary signal transduction molecule regulating monocyte immediate-early gene induction. Proc. Natl. Acad. Sci. U.S.A. 89:1992;9034-9038.
    • (1992) Proc. Natl. Acad. Sci. U.S.A. , vol.89 , pp. 9034-9038
    • Yurochko, A.D.1    Liu, D.Y.2    Eierman, D.3    Haskill, S.4
  • 92
    • 0029079272 scopus 로고
    • Components of the nuclear signalling cascade that regulate collagenase gene expression in response to integrin-derived signals
    • Tremble P., Damsky C.H., Werb Z. Components of the nuclear signalling cascade that regulate collagenase gene expression in response to integrin-derived signals. J. Cell. Biol. 129:1995;1707-1720.
    • (1995) J. Cell. Biol. , vol.129 , pp. 1707-1720
    • Tremble, P.1    Damsky, C.H.2    Werb, Z.3
  • 94
    • 0029005762 scopus 로고
    • Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells
    • Lin T.H., Rosales C., Mondal K., Bolen J.B., Haskill S., Juliano R.L. Integrin-mediated tyrosine phosphorylation and cytokine message induction in monocytic cells. J. Biol. Chem. 270:1995;16189-16197.
    • (1995) J. Biol. Chem. , vol.270 , pp. 16189-16197
    • Lin, T.H.1    Rosales, C.2    Mondal, K.3    Bolen, J.B.4    Haskill, S.5    Juliano, R.L.6
  • 95
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen Q., Kinch M.S., Lin T.H., Burridge K., Juliano R. Integrin-mediated cell adhesion activates mitogen-activated protein kinases. J. Biol. Chem. 269:1994;26602-26605.
    • (1994) J. Biol. Chem. , vol.269 , pp. 26602-26605
    • Chen, Q.1    Kinch, M.S.2    Lin, T.H.3    Burridge, K.4    Juliano, R.5
  • 97
    • 0030766846 scopus 로고    scopus 로고
    • Growth factor activation of MAP kinase requires cell adhesion
    • Renshaw M.W., Ren X-D., Schwartz M.A. Growth factor activation of MAP kinase requires cell adhesion. The EMBO Journal. 16:1997;5592-5599.
    • (1997) The EMBO Journal , vol.16 , pp. 5592-5599
    • Renshaw, M.W.1    Ren, X.-D.2    Schwartz, M.A.3
  • 98
    • 0029670904 scopus 로고    scopus 로고
    • 1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF-receptors
    • 1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF-receptors. J. Cell Biol. 132:1996;741-752.
    • (1996) J. Cell Biol. , vol.132 , pp. 741-752
    • Sundberg, C.1    Rubin, K.2
  • 99
    • 0027203057 scopus 로고
    • v integrin associates with a 190-kDa protein that is phosphorylated on tyrosine in response to platelet-derived growth factor
    • v integrin associates with a 190-kDa protein that is phosphorylated on tyrosine in response to platelet-derived growth factor. J. Biol. Chem. 268:1993;17270-17276.
    • (1993) J. Biol. Chem. , vol.268 , pp. 17270-17276
    • Bartfeld, N.S.1    Pasquale, E.B.2    Geltosky, J.E.3    Languino, L.R.4
  • 100
    • 0028641601 scopus 로고
    • Association of insulin receptor substrate-1 with integrins
    • Vuori K., Ruoslahti E. Association of insulin receptor substrate-1 with integrins. Science. 266:1994;1576-1578.
    • (1994) Science , vol.266 , pp. 1576-1578
    • Vuori, K.1    Ruoslahti, E.2
  • 101
    • 0030814976 scopus 로고    scopus 로고
    • 3 integrin associates with activated insulin and PDGF receptors and potentiates the biological activity of PDGF
    • 3 integrin associates with activated insulin and PDGF receptors and potentiates the biological activity of PDGF. The EMBO Journal. 16:1997;5600-5607.
    • (1997) The EMBO Journal , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 102
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases
    • Hotchin N.A., Hall A. The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular rho/rac GTPases. J. Cell Biol. 131:(6part 2):1995;1857-1865.
    • (1995) J. Cell Biol. , vol.131 , Issue.6 PART 2 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 103
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson M.F., Ashworth A., Hall A. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science. 269:1995;1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 104
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 105
    • 0029828456 scopus 로고    scopus 로고
    • Involvement of the small GTPase rho in integrin-mediated activation of mitogen-activated protein kinase
    • Renshaw M.W., Toksoz D., Schwartz M.A. Involvement of the small GTPase rho in integrin-mediated activation of mitogen-activated protein kinase. J. Biol. Chem. 271:1996;21691-21694.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21691-21694
    • Renshaw, M.W.1    Toksoz, D.2    Schwartz, M.A.3
  • 106
    • 0021825489 scopus 로고
    • Isolation of a new human oncogene from a diffuse B-cell lymphoma
    • Eva A., Aaronson S.A. Isolation of a new human oncogene from a diffuse B-cell lymphoma. Nature. 316:1985;273-275.
    • (1985) Nature , vol.316 , pp. 273-275
    • Eva, A.1    Aaronson, S.A.2
  • 107
    • 0027972531 scopus 로고
    • Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products
    • Toksoz D., Williams D.A. Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products. Oncogene. 9:1994;621-628.
    • (1994) Oncogene , vol.9 , pp. 621-628
    • Toksoz, D.1    Williams, D.A.2
  • 110
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto S., Akiyama S.K., Yamada K.M. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science. 267:1995;883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 111
    • 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., Yamada K.M. 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. 135:1996;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
  • 112
    • 0026069474 scopus 로고
    • Oncogenes and signal transduction
    • [published erratum appears in Cell 1991 May 3; 65(5): following 914]
    • Cantley L.C., Auger K.R., Carpenter C., Duckworth B., Graziani A., Kapeller R., Soltoff S. Oncogenes and signal transduction. Cell. 64:1991;281-302. [published erratum appears in Cell 1991 May 3; 65(5): following 914].
    • (1991) Cell , vol.64 , pp. 281-302
    • Cantley, L.C.1    Auger, K.R.2    Carpenter, C.3    Duckworth, B.4    Graziani, A.5    Kapeller, R.6    Soltoff, S.7
  • 113
    • 0030951798 scopus 로고    scopus 로고
    • Leukocyte adhesion - structure and function of human leukocyte 2-β integrins and their cellular ligands
    • Gahmberg C.G., Tolvanen M., Kotovuori P. Leukocyte adhesion - structure and function of human leukocyte 2-β integrins and their cellular ligands. Eur. J. Biochem. 245:1997;215-232.
    • (1997) Eur. J. Biochem. , vol.245 , pp. 215-232
    • Gahmberg, C.G.1    Tolvanen, M.2    Kotovuori, P.3
  • 115
    • 0025666501 scopus 로고
    • Integrin-associated protein: A 50-kD plasma membrane antigen physically and functionally associated with integrins
    • Brown E.J., Hooper L., Ho T., Gresham H. Integrin-associated protein: a 50-kD plasma membrane antigen physically and functionally associated with integrins. J. Cell. Bio. 111:1990;2785-2794.
    • (1990) J. Cell. Bio. , vol.111 , pp. 2785-2794
    • Brown, E.J.1    Hooper, L.2    Ho, T.3    Gresham, H.4
  • 117
    • 0024506758 scopus 로고
    • A novel member of the integrin receptor family mediates Arg-Gly-Asp- stimulated neutrophil phagocytosis
    • Gresham H.D., Goodwin J.L., Allen P.M., Anderson D.C., Brown E.J. A novel member of the integrin receptor family mediates Arg-Gly-Asp- stimulated neutrophil phagocytosis. J. Cell Biol. 108:1989;1935-1943.
    • (1989) J. Cell Biol. , vol.108 , pp. 1935-1943
    • Gresham, H.D.1    Goodwin, J.L.2    Allen, P.M.3    Anderson, D.C.4    Brown, E.J.5
  • 118
    • 0027218590 scopus 로고
    • Leukocyte response integrin and integrin-associated protein act as a signal transduction unit in generation of a phagocyte respiratory burst
    • Zhou M., Brown E.J. Leukocyte response integrin and integrin-associated protein act as a signal transduction unit in generation of a phagocyte respiratory burst. J. Exp. Med. 178:1993;1165-1174.
    • (1993) J. Exp. Med. , vol.178 , pp. 1165-1174
    • Zhou, M.1    Brown, E.J.2
  • 120
    • 0029909981 scopus 로고    scopus 로고
    • Decreased resistance to bacterial infection and granulocyte defects in IAP-deficient mice
    • Lindberg F.P., Bullard D.C., Caver T.E., Gresham H.D., Beaudet A.L., Brown E.J. Decreased resistance to bacterial infection and granulocyte defects in IAP-deficient mice. Science. 274:1996;795-798.
    • (1996) Science , vol.274 , pp. 795-798
    • Lindberg, F.P.1    Bullard, D.C.2    Caver, T.E.3    Gresham, H.D.4    Beaudet, A.L.5    Brown, E.J.6
  • 121
    • 0030062129 scopus 로고    scopus 로고
    • Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins)
    • Berditchevski F., Zutter M.M., Hemler M.E. Characterization of novel complexes on the cell surface between integrins and proteins with 4 transmembrane domains (TM4 proteins). Mol. Biol. Cell. 7:1996;193-207.
    • (1996) Mol. Biol. Cell. , vol.7 , pp. 193-207
    • Berditchevski, F.1    Zutter, M.M.2    Hemler, M.E.3
  • 122
    • 0031018172 scopus 로고    scopus 로고
    • A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase
    • Berditchevski F., Tolias K.F., Wong K., Carpenter C.L., Hemler M.E. A novel link between integrins, transmembrane-4 superfamily proteins (CD63 and CD81), and phosphatidylinositol 4-kinase. J. Biol. Chem. 272:1997;2595-2598.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2595-2598
    • Berditchevski, F.1    Tolias, K.F.2    Wong, K.3    Carpenter, C.L.4    Hemler, M.E.5
  • 123
    • 43949157634 scopus 로고
    • The ins and outs of the transmembrane 4 superfamily
    • Wright M.D., Tomlinson M.G. The ins and outs of the transmembrane 4 superfamily. Immunol. Today. 15:1994;588-594.
    • (1994) Immunol. Today , vol.15 , pp. 588-594
    • Wright, M.D.1    Tomlinson, M.G.2
  • 125
    • 0029103011 scopus 로고
    • A tetraspan membrane glycoprotein produced in the human intestinal epithelium and liver that can regulate cell density-dependent proliferation
    • Wice B.M., Gordon J.I. A tetraspan membrane glycoprotein produced in the human intestinal epithelium and liver that can regulate cell density-dependent proliferation. J. Biol. Chem. 270:1995;21907-21918.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21907-21918
    • Wice, B.M.1    Gordon, J.I.2
  • 127
    • 0029257377 scopus 로고
    • Signal transduction through integrins: A central role for focal adhesion kinase?
    • Richardson A., Parsons J.T. Signal transduction through integrins: a central role for focal adhesion kinase? BioEssays. 17:1995;229-236.
    • (1995) BioEssays , vol.17 , pp. 229-236
    • Richardson, A.1    Parsons, J.T.2
  • 128
    • 0029741102 scopus 로고    scopus 로고
    • Inhibition of focal adhesion kinase (FAK) signalling in focal adhesions decreases cell motility and proliferation
    • Gilmore A.P., Romer L.H. Inhibition of focal adhesion kinase (FAK) signalling in focal adhesions decreases cell motility and proliferation. Mol. Cell. Biol. 7:1996;1209-1224.
    • (1996) Mol. Cell. Biol. , vol.7 , pp. 1209-1224
    • Gilmore, A.P.1    Romer, L.H.2
  • 131
    • 0028122650 scopus 로고
    • Focal adhesion kinase and associated proteins
    • Schaller M.D., Parsons J.T. Focal adhesion kinase and associated proteins. Curr. Opin. Cell Biol. 6:1994;705-710.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 705-710
    • Schaller, M.D.1    Parsons, J.T.2
  • 132
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to ras pathway by GRB-2 binding to focal adhesion kinase
    • Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P. Integrin-mediated signal transduction linked to ras pathway by GRB-2 binding to focal adhesion kinase. Nature. 372:1994;786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 133
    • 0031047981 scopus 로고    scopus 로고
    • Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs
    • Pólte T.R., Hanks S.K. Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs. J. Biol. Chem. 272:1997;5501-5509.
    • (1997) J. Biol. Chem. , vol.272 , pp. 5501-5509
    • Pólte, T.R.1    Hanks, S.K.2
  • 139
    • 0030924021 scopus 로고    scopus 로고
    • 1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin
    • 1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of beta1 integrin. J. Cell Biol. 138:1997;1149-1157.
    • (1997) J. Cell Biol. , vol.138 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 146
    • 0026069822 scopus 로고
    • In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin a subunits
    • Rojiani M.V., Finlay B.B., Gray V., Dedhar S. In vitro interaction of a polypeptide homologous to human Ro/SS-A antigen (calreticulin) with a highly conserved amino acid sequence in the cytoplasmic domain of integrin a subunits. Biochemistry. 30:(41):1991;9859-9866.
    • (1991) Biochemistry , vol.30 , Issue.41 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 147
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin a-subunit-binding protein
    • Leung-Hagesteijn C.Y., Milankov K., Michalak M., Wilkins J., Dedhar S. Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin a-subunit-binding protein. J. Cell Sci. 107:1994;589-600.
    • (1994) J. Cell Sci. , vol.107 , pp. 589-600
    • Leung-Hagesteijn, C.Y.1    Milankov, K.2    Michalak, M.3    Wilkins, J.4    Dedhar, S.5
  • 150
    • 0033562951 scopus 로고    scopus 로고
    • Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/dephosphorylation events
    • Coppolino M.G., Dedhar S. Ligand-specific, transient interaction between integrins and calreticulin during cell adhesion to extracellular matrix proteins is dependent upon phosphorylation/dephosphorylation events. Biochem. J. 340:1999;41-50.
    • (1999) Biochem. J. , vol.340 , pp. 41-50
    • Coppolino, M.G.1    Dedhar, S.2
  • 151
    • 0030272101 scopus 로고    scopus 로고
    • Integrin activation: The link between ligand binding and signal transduction
    • Humphries M.J. Integrin activation: the link between ligand binding and signal transduction. Curr. Opin. Cell. Biol. 8:1996;632-640.
    • (1996) Curr. Opin. Cell. Biol. , vol.8 , pp. 632-640
    • Humphries, M.J.1
  • 152
    • 0029969086 scopus 로고    scopus 로고
    • Getting integrins into shape: Recent insights into how integrin activity is regulated by conformational charge
    • Mould A.P. Getting integrins into shape: recent insights into how integrin activity is regulated by conformational charge. J. Cell. Sci. 109:1996;2613-2618.
    • (1996) J. Cell. Sci. , vol.109 , pp. 2613-2618
    • Mould, A.P.1
  • 153
    • 0025124607 scopus 로고
    • Lymphoid cells recognize an alternatively spliced segment of fibronection via the integrin receptor alpha 4 beta 1
    • Guan J.-L., Hynes R.O. Lymphoid cells recognize an alternatively spliced segment of fibronection via the integrin receptor alpha 4 beta 1. Cell. 60:1990;53-61.
    • (1990) Cell , vol.60 , pp. 53-61
    • Guan, J.-L.1    Hynes, R.O.2
  • 154
    • 0025992433 scopus 로고
    • Evidence that the signal-initiating membrane protein CD9 is associated with small GTP-binding proteins
    • Seehafer J.G., Show A.R. Evidence that the signal-initiating membrane protein CD9 is associated with small GTP-binding proteins. Biochem. Biophys. Res. Commun. 179:1991;401-406.
    • (1991) Biochem. Biophys. Res. Commun. , vol.179 , pp. 401-406
    • Seehafer, J.G.1    Show, A.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.