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Volumn 16, Issue 4, 1997, Pages 165-171

Integrin signaling: Building connections beyond the focal contact?

Author keywords

Integrin; Protein protein interactions; Signaling

Indexed keywords

CYTOSKELETON PROTEIN; INTEGRIN; MEMBRANE PROTEIN; PHOSPHOTYROSINE;

EID: 0031257740     PISSN: 0945053X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0945-053X(97)90004-4     Document Type: Short Survey
Times cited : (12)

References (49)
  • 1
    • 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
  • 2
    • 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
  • 3
    • 0029856857 scopus 로고    scopus 로고
    • Inducible tyrosine phosphorylation of the β3 integrin requires the αv integrin cytoplasmic tail
    • Blystone S.D., Lindberg F.P., Williams M.P., McHugh K.P., Brown E.J. Inducible tyrosine phosphorylation of the β3 integrin requires the αv integrin cytoplasmic tail. J. Biol. Chem. 271:1996;31458-31462.
    • (1996) J. Biol. Chem. , vol.271 , pp. 31458-31462
    • Blystone, S.D.1    Lindberg, F.P.2    Williams, M.P.3    McHugh, K.P.4    Brown, E.J.5
  • 4
    • 0027154651 scopus 로고
    • Ligand-dependent and -independent integrin focal contact localization: The role of the α chain cytoplasmic domain
    • Briesewitz R., Kern A., Marcantonio E.E. Ligand-dependent and -independent integrin focal contact localization: the role of the α chain cytoplasmic domain. Mol. Biol. Cell. 4:1993;593-604.
    • (1993) Mol. Biol. Cell , vol.4 , pp. 593-604
    • Briesewitz, R.1    Kern, A.2    Marcantonio, E.E.3
  • 5
    • 0029827130 scopus 로고    scopus 로고
    • Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding
    • Brown M.C., Perrotta J.A., Turner C.E. Identification of LIM3 as the principal determinant of paxillin focal adhesion localization and characterization of a novel motif on paxillin directing vinculin and focal adhesion kinase binding. J. Cell Biol. 135:1996;1109-1123.
    • (1996) J. Cell Biol. , vol.135 , pp. 1109-1123
    • Brown, M.C.1    Perrotta, J.A.2    Turner, C.E.3
  • 8
  • 10
    • 17544369411 scopus 로고    scopus 로고
    • Mitogenic signaling by ret/ptc2 requires association with enigma via a LIM domain
    • Durick K., Wu R.-Y., Gill G.N., Taylor S.S. Mitogenic signaling by ret/ptc2 requires association with enigma via a LIM domain. J. Biol. Chem. 271:1996;12691-12694.
    • (1996) J. Biol. Chem. , vol.271 , pp. 12691-12694
    • Durick, K.1    Wu, R.-Y.2    Gill, G.N.3    Taylor, S.S.4
  • 12
    • 0029050683 scopus 로고
    • Requirement of the NPXY motif in the integrin β3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo
    • Filardo E.J., Brooks P.C., Deming S.L., Damsky C., Cheresh D.A. Requirement of the NPXY motif in the integrin β3 subunit cytoplasmic tail for melanoma cell migration in vitro and in vivo. J. Cell Biol. 130:1995;441-450.
    • (1995) J. Cell Biol. , vol.130 , pp. 441-450
    • Filardo, E.J.1    Brooks, P.C.2    Deming, S.L.3    Damsky, C.4    Cheresh, D.A.5
  • 13
    • 0029646094 scopus 로고
    • The enigma of LIM domains
    • Gill G.N. The enigma of LIM domains. Structure. 3:1995;1285-1289.
    • (1995) Structure , vol.3 , pp. 1285-1289
    • Gill, G.N.1
  • 16
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation and signaling in cell adhesion
    • Hynes R.O. Integrins: versatility, modulation and signaling in cell adhesion. Cell. 69:1992;11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 17
    • 0028017709 scopus 로고
    • Altered localization and cytoplasmic domain-binding properties of tyrosine-phosphorylated β1 integrin
    • Johansson M.W., Larsson E., Luning B., Pasquale E.B., Ruoslahti E. Altered localization and cytoplasmic domain-binding properties of tyrosine-phosphorylated β1 integrin. J. Cell Biol. 126:1994;1299-1309.
    • (1994) J. Cell Biol. , vol.126 , pp. 1299-1309
    • Johansson, M.W.1    Larsson, E.2    Luning, B.3    Pasquale, E.B.4    Ruoslahti, E.5
  • 18
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-triphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Karlund J.K., Guilherme A., Holik J.J., Virbasius J.V., Chawla A., Czech M.P. Signaling by phosphoinositide-3,4,5-triphosphate through proteins containing pleckstrin and Sec7 homology domains. Science. 275:1997;1927-1930.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Karlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 24
    • 0028323266 scopus 로고
    • Cell attachment to extracellular matrix substrates is inhibited upon downregulation of expression of calreticulin, an intracellular integrin α-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 α-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
  • 26
    • 0028285191 scopus 로고
    • Caveolae, caveolin, and caveolin-rich membrane domains: A signaling hypothesis
    • Lisanti M.P., Scherer P.E., Tang Z., Sargiacomo M. Caveolae, caveolin, and caveolin-rich membrane domains: a signaling hypothesis. Trends Cell Biol. 4:1994;231-235.
    • (1994) Trends Cell Biol. , vol.4 , pp. 231-235
    • Lisanti, M.P.1    Scherer, P.E.2    Tang, Z.3    Sargiacomo, M.4
  • 27
    • 0025117790 scopus 로고
    • Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins
    • Lux S.E., John K.M., Bennett V. Analysis of cDNA for human erythrocyte ankyrin indicates a repeated structure with homology to tissue-differentiation and cell-cycle control proteins. Nature. 344:1990;36-42.
    • (1990) Nature , vol.344 , pp. 36-42
    • Lux, S.E.1    John, K.M.2    Bennett, V.3
  • 29
    • 0030230376 scopus 로고    scopus 로고
    • The PI/PTB domain: A new protein interaction domain involved in growth factor receptor signaling
    • Margolis B. The PI/PTB domain: a new protein interaction domain involved in growth factor receptor signaling. J. Lab. Clin. Med. 126:1996;235-241.
    • (1996) J. Lab. Clin. Med. , vol.126 , pp. 235-241
    • Margolis, B.1
  • 30
    • 0031041536 scopus 로고    scopus 로고
    • Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor
    • Meacci E., Tsai S.-C., Adamik R., Moss J., Vaughn M. Cytohesin-1, a cytosolic guanine nucleotide-exchange protein for ADP-ribosylation factor. Proc. Natl. Acad. Sci. USA. 94:1997;1745-1748.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1745-1748
    • Meacci, E.1    Tsai, S.-C.2    Adamik, R.3    Moss, J.4    Vaughn, M.5
  • 35
    • 0028954275 scopus 로고
    • Regulation of integrin affinity states through an NPXY motif in the β subunit cytoplasmic domain
    • O'Toole T.E., Ylänne J., Culley B.C. Regulation of integrin affinity states through an NPXY motif in the β subunit cytoplasmic domain. J. Biol. Chem. 270:1995;8553-8558.
    • (1995) J. Biol. Chem. , vol.270 , pp. 8553-8558
    • O'Toole, T.E.1    Ylänne, J.2    Culley, B.C.3
  • 36
    • 0028859279 scopus 로고
    • Protein modules and signaling networks
    • Pawson T. Protein modules and signaling networks. Nature. 373:1995;573-580.
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 37
    • 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 cytoplsmic domain of integrin alpha 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 cytoplsmic domain of integrin alpha subunits. Biochemistry. 30:1991;9859-9866.
    • (1991) Biochemistry , vol.30 , pp. 9859-9866
    • Rojiani, M.V.1    Finlay, B.B.2    Gray, V.3    Dedhar, S.4
  • 38
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains
    • Schaller M.D., Otey C.A., Hildebrand J.D., Parsons J.T. Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J. Cell Biol. 130:1995;1181-1187.
    • (1995) J. Cell Biol. , vol.130 , pp. 1181-1187
    • Schaller, M.D.1    Otey, C.A.2    Hildebrand, J.D.3    Parsons, J.T.4
  • 39
    • 0028134697 scopus 로고
    • The LIM domain is a modular protein-binding interface
    • Schmeichel K.L., Beckerle M.C. The LIM domain is a modular protein-binding interface. Cell. 79:1994;211-219.
    • (1994) Cell , vol.79 , pp. 211-219
    • Schmeichel, K.L.1    Beckerle, M.C.2
  • 42
    • 0029010308 scopus 로고
    • The phosphotyrosine interaction domain of shc recognizes tyrosine-phosphorylated NPXY motif
    • Songyang Z., Margolis B., Chaudhuri M., Shoelson S.E., Cantley L.C. The phosphotyrosine interaction domain of shc recognizes tyrosine-phosphorylated NPXY motif. J. Biol. Chem. 270:1995;14863-14866.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14863-14866
    • Songyang, Z.1    Margolis, B.2    Chaudhuri, M.3    Shoelson, S.E.4    Cantley, L.C.5
  • 43
    • 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
  • 44
    • 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
  • 46
    • 0028061406 scopus 로고
    • LIM domain recognition of a tyrosine-containing tight turn
    • Wu R.-Y., Gill G.N. LIM domain recognition of a tyrosine-containing tight turn. J. Biol. Chem. 269:1994;25085-25090.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25085-25090
    • Wu, R.-Y.1    Gill, G.N.2
  • 47
    • 0031050449 scopus 로고    scopus 로고
    • Molecular interactions in cell adhesion complexes
    • Yamada K.M., Geiger B. Molecular interactions in cell adhesion complexes. Curr. Opin. Cell Biol. 9:1997;76-85.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 76-85
    • Yamada, K.M.1    Geiger, B.2
  • 49
    • 0027263655 scopus 로고
    • Distinct functions of integrin α and β subunit cytoplasmic domains in cell spreading and formation of focal contacts
    • Ylänne J., Chen Y., O'Toole T.E., Loftus J.C., Takada Y., Ginsberg M.H. Distinct functions of integrin α and β subunit cytoplasmic domains in cell spreading and formation of focal contacts. J. Cell Biol. 122:1993;223-233.
    • (1993) J. Cell Biol. , vol.122 , pp. 223-233
    • Ylänne, J.1    Chen, Y.2    O'Toole, T.E.3    Loftus, J.C.4    Takada, Y.5    Ginsberg, M.H.6


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