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Volumn 181, Issue 1, 1999, Pages 74-82

Integrins interact with focal adhesions through multiple distinct pathways

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; BETA1 INTEGRIN; CELL PROTEIN; INTEGRIN; UNCLASSIFIED DRUG;

EID: 0032774768     PISSN: 00219541     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1097-4652(199910)181:1<74::AID-JCP8>3.0.CO;2-H     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 0028343192 scopus 로고
    • Transmembrane signal transduction by integrin cytoplasmic domains expressed in single subunit chimeras
    • Akiyama SK, Yamada SS, Yamada KM, LaFlamme SE. 1994. Transmembrane signal transduction by integrin cytoplasmic domains expressed in single subunit chimeras. J Biol Chem 269:15961-15964.
    • (1994) J Biol Chem , vol.269 , pp. 15961-15964
    • Akiyama, S.K.1    Yamada, S.S.2    Yamada, K.M.3    LaFlamme, S.E.4
  • 3
    • 0027154651 scopus 로고
    • Ligand-dependent and -independent integrin focal contact localization: The role of the α chain cytoplasmic domain
    • Briesewitz R, Kern A, Marcantonio EE. 1993. Ligand-dependent and -independent integrin focal contact localization: the role of the α chain cytoplasmic domain. Mol Biol Cell 4:593-604.
    • (1993) Mol Biol Cell , vol.4 , pp. 593-604
    • Briesewitz, R.1    Kern, A.2    Marcantonio, E.E.3
  • 4
    • 0029157259 scopus 로고
    • Assembly and function of integrin receptors is dependent on opposing α and β cytoplasmic domains
    • Briesewitz R, Kern A, Marcantonio EE. 1995. Assembly and function of integrin receptors is dependent on opposing α and β cytoplasmic domains. Mol Biol Cell 6:997-1010.
    • (1995) Mol Biol Cell , vol.6 , pp. 997-1010
    • Briesewitz, R.1    Kern, A.2    Marcantonio, E.E.3
  • 5
    • 0029821677 scopus 로고    scopus 로고
    • The membrane-cytoplasm interface of integrin α subunits is critical for receptor latency
    • Briesewitz R, Kern A, Smilenov LB, David FS, Marcantonio EE. 1996. The membrane-cytoplasm interface of integrin α subunits is critical for receptor latency. Mol Biol Cell 7:1499-1509.
    • (1996) Mol Biol Cell , vol.7 , pp. 1499-1509
    • Briesewitz, R.1    Kern, A.2    Smilenov, L.B.3    David, F.S.4    Marcantonio, E.E.5
  • 6
    • 0025326334 scopus 로고
    • Gene splicing by overlap extension: Tailor-made genes using PCR
    • Cai Z, Ho SN, Horton RM, Pease LR. 1990. Gene splicing by overlap extension: tailor-made genes using PCR. Biotechniques 5:528-535.
    • (1990) Biotechniques , vol.5 , pp. 528-535
    • Cai, Z.1    Ho, S.N.2    Horton, R.M.3    Pease, L.R.4
  • 7
    • 0030924021 scopus 로고    scopus 로고
    • ICAP-1, a novel β1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of β1 integrin
    • Chang DD, Wong C, Smith H, Liu J. 1997. ICAP-1, a novel β1 integrin cytoplasmic domain-associated protein, binds to a conserved and functionally important NPXY sequence motif of β1 integrin. J Cell Biol 138:1149-1157.
    • (1997) J Cell Biol , vol.138 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 8
    • 0028146157 scopus 로고
    • A point mutation in the integrin β3 cytoplasmic domain (S752→P) impairs bidirectional signaling through αIIbβ3 (platelet glycoprotein IIb-IIIa)
    • Chen YP, O'Toole TE, Ylänne J, Rosa JP, Ginsberg MH. 1994a. A point mutation in the integrin β3 cytoplasmic domain (S752→P) impairs bidirectional signaling through αIIbβ3 (platelet glycoprotein IIb-IIIa). Blood 84:1857-1865.
    • (1994) Blood , vol.84 , pp. 1857-1865
    • Chen, Y.P.1    O'Toole, T.E.2    Ylänne, J.3    Rosa, J.P.4    Ginsberg, M.H.5
  • 10
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka M, Burridge K. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J Cell Biol 133:1403-1415.
    • (1996) J Cell Biol , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 11
    • 0028282476 scopus 로고
    • Regulation of the avidity of integrin α4β7 by the β7 cytoplasmic domain
    • Crowe DT, Chiu H, Fong S, Weissman IL. 1994. Regulation of the avidity of integrin α4β7 by the β7 cytoplasmic domain. J Biol Chem 269:14411-14418.
    • (1994) J Biol Chem , vol.269 , pp. 14411-14418
    • Crowe, D.T.1    Chiu, H.2    Fong, S.3    Weissman, I.L.4
  • 12
    • 0029050683 scopus 로고
    • Requirement of the NPXY motif in the integrin β3 cytoplasmic tail for melanoma cell migration in vitro and in vivo
    • Filardo EJ, Brooks PC, Deming SL, Damsky C, Cheresh DA. 1995. Requirement of the NPXY motif in the integrin β3 cytoplasmic tail for melanoma cell migration in vitro and in vivo. J Cell Biol 130: 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
    • 0027097004 scopus 로고
    • A chimeric N-cadherin/β1-integrin receptor which localizes to both cell-cell and cell-matrix adhesions
    • Geiger B, Salomon D, Takeichi M, Hynes RO. 1992. A chimeric N-cadherin/β1-integrin receptor which localizes to both cell-cell and cell-matrix adhesions. J Cell Sci 103:943-951.
    • (1992) J Cell Sci , vol.103 , pp. 943-951
    • Geiger, B.1    Salomon, D.2    Takeichi, M.3    Hynes, R.O.4
  • 14
    • 0026081049 scopus 로고
    • Isolation of a population of transiently transfected quiescent and senescent cells by magnetic affinity cell sorting
    • Giordano T, Howard TH, Coleman J, Sakamoto K, Howard BH. 1991. Isolation of a population of transiently transfected quiescent and senescent cells by magnetic affinity cell sorting. Exp Cell Res 192: 193-197.
    • (1991) Exp Cell Res , vol.192 , pp. 193-197
    • Giordano, T.1    Howard, T.H.2    Coleman, J.3    Sakamoto, K.4    Howard, B.H.5
  • 15
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein
    • Guan JL, Trevithick JE, Hynes RO. 1991. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell Regul 2:951-964.
    • (1991) Cell Regul , vol.2 , pp. 951-964
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 17
    • 0025014759 scopus 로고
    • Expression and function of chicken integrin β1 subunit and its cytoplasmic domain mutants in mouse NIH 3T3 cells
    • Hayashi Y, Haimovich B, Reszka A, Boettiger D, Horwitz A. 1990. Expression and function of chicken integrin β1 subunit and its cytoplasmic domain mutants in mouse NIH 3T3 cells. J Cell Biol 110:175-184.
    • (1990) J Cell Biol , vol.110 , pp. 175-184
    • Hayashi, Y.1    Haimovich, B.2    Reszka, A.3    Boettiger, D.4    Horwitz, A.5
  • 18
    • 0028091046 scopus 로고
    • Protein tyrosine phosphorylation induced by lysophosphatidic acid in Rat-1 fibroblasts
    • Hordijk PL, Verlaan I, van Corven EJ, Moolenaar WH. 1994. Protein tyrosine phosphorylation induced by lysophosphatidic acid in Rat-1 fibroblasts. J Biol Chem 269:645-651.
    • (1994) J Biol Chem , vol.269 , pp. 645-651
    • Hordijk, P.L.1    Verlaan, I.2    Van Corven, E.J.3    Moolenaar, W.H.4
  • 19
    • 0029048813 scopus 로고
    • The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity
    • Hughes PE, O'Toole TE, Ylänne J, Shattil S, Ginsberg MH. 1995. The conserved membrane-proximal region of an integrin cytoplasmic domain specifies ligand binding affinity. J Biol Chem 270:12411-12417.
    • (1995) J Biol Chem , vol.270 , pp. 12411-12417
    • Hughes, P.E.1    O'Toole, T.E.2    Ylänne, J.3    Shattil, S.4    Ginsberg, M.H.5
  • 21
    • 0026770377 scopus 로고
    • Integrins: Versatility, modulation, and signaling in cell adhesion
    • Hynes RO. 1992. Integrins: versatility, modulation, and signaling in cell adhesion. Cell 69:11-25.
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 23
    • 0031005461 scopus 로고    scopus 로고
    • Affinity modulation of platelet integrin αIIbβ3 by β3-endonexin, a selective binding partner of the β3 integrin cytoplasmic tail
    • Kashiwagi H, Schwartz MA, Eigenthaler M, Davis KA, Ginsberg MH, Shattil SJ. 1997. Affinity modulation of platelet integrin αIIbβ3 by β3-endonexin, a selective binding partner of the β3 integrin cytoplasmic tail. J Cell Biol 137:1433-1443.
    • (1997) J Cell Biol , vol.137 , pp. 1433-1443
    • Kashiwagi, H.1    Schwartz, M.A.2    Eigenthaler, M.3    Davis, K.A.4    Ginsberg, M.H.5    Shattil, S.J.6
  • 24
    • 0027223986 scopus 로고
    • Lysophosphatidic acid induces tyrosine phosphorylation and activation of MAP-kinase and focal adhesion kinase in cultured Swiss 3T3 cells
    • Kumagai N, Morii N, Fujisawa K, Yoshimasa T, Nakao K, Narumiya S. 1993. Lysophosphatidic acid induces tyrosine phosphorylation and activation of MAP-kinase and focal adhesion kinase in cultured Swiss 3T3 cells. FEBS Lett 329:273-276.
    • (1993) FEBS Lett , vol.329 , pp. 273-276
    • Kumagai, N.1    Morii, N.2    Fujisawa, K.3    Yoshimasa, T.4    Nakao, K.5    Narumiya, S.6
  • 25
    • 0026535449 scopus 로고
    • Regulation of fibronectin receptor distribution
    • LaFlamme SE, Akiyama SK, Yamada KM. 1992. Regulation of fibronectin receptor distribution. J Cell Biol 117:437-447.
    • (1992) J Cell Biol , vol.117 , pp. 437-447
    • LaFlamme, S.E.1    Akiyama, S.K.2    Yamada, K.M.3
  • 26
    • 0027994108 scopus 로고
    • Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly
    • LaFlamme SE, Thomas LA, Yamada SS, Yamada KM. 1994. Single subunit chimeric integrins as mimics and inhibitors of endogenous integrin functions in receptor localization, cell spreading and migration, and matrix assembly. J Cell Biol 126:1287-1298.
    • (1994) J Cell Biol , vol.126 , pp. 1287-1298
    • LaFlamme, S.E.1    Thomas, L.A.2    Yamada, S.S.3    Yamada, K.M.4
  • 27
    • 0028238346 scopus 로고
    • Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed β1 cytoplasmic domain
    • Lukashev ME, Sheppard D, Pytela R. 1994. Disruption of integrin function and induction of tyrosine phosphorylation by the autonomously expressed β1 cytoplasmic domain. J Biol Chem 269:18311-18314.
    • (1994) J Biol Chem , vol.269 , pp. 18311-18314
    • Lukashev, M.E.1    Sheppard, D.2    Pytela, R.3
  • 28
    • 0030953445 scopus 로고    scopus 로고
    • Integrin-mediated activation of focal adhesion kinase is independent of focal adhesion formation or integrin activation
    • Lyman S, Gilmore A, Burridge K, Gidwitz S, White GC. 1997. Integrin-mediated activation of focal adhesion kinase is independent of focal adhesion formation or integrin activation. J Biol Chem 272: 22538-22547.
    • (1997) J Biol Chem , vol.272 , pp. 22538-22547
    • Lyman, S.1    Gilmore, A.2    Burridge, K.3    Gidwitz, S.4    White, G.C.5
  • 29
    • 0025463383 scopus 로고
    • Mapping of the functional determinants of the integrin β1 cytoplasmic domain by site directed mutagenesis
    • Marcantonio EE, Guan JL, Trevithick JE, Hynes RO. 1990. Mapping of the functional determinants of the integrin β1 cytoplasmic domain by site directed mutagenesis. Cell Regul 1:597-604.
    • (1990) Cell Regul , vol.1 , pp. 597-604
    • Marcantonio, E.E.1    Guan, J.L.2    Trevithick, J.E.3    Hynes, R.O.4
  • 30
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamoto S, Akiyama SK, Yamada KM. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science 267:883-885.
    • (1995) Science , vol.267 , pp. 883-885
    • Miyamoto, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 31
    • 0028954275 scopus 로고
    • Regulation of integrin affinity states through an NPXY motif in the beta subunit cytoplasmic domain
    • O'Toole TE, Ylänne J, Culley BM. 1995. Regulation of integrin affinity states through an NPXY motif in the beta subunit cytoplasmic domain. J Biol Chem 270:8553-8558.
    • (1995) J Biol Chem , vol.270 , pp. 8553-8558
    • O'Toole, T.E.1    Ylänne, J.2    Culley, B.M.3
  • 32
    • 0029148903 scopus 로고
    • Conserved regions in the cytoplasmic domains of the leukocyte integrin αlβ2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association
    • Pardi R, Bossi G, Inverardi L, Rovida E, Bender JR. 1995. Conserved regions in the cytoplasmic domains of the leukocyte integrin αLβ2 are involved in endoplasmic reticulum retention, dimerization, and cytoskeletal association. J Immunol 155:1252-1263.
    • (1995) J Immunol , vol.155 , pp. 1252-1263
    • Pardi, R.1    Bossi, G.2    Inverardi, L.3    Rovida, E.4    Bender, J.R.5
  • 33
    • 0029953173 scopus 로고    scopus 로고
    • Regulation of conformation and ligand binding function of integrin α5β1 by the β1 cytoplasmic domain
    • Puzon-McLaughlin W, Yednock TA, Takada Y. 1996. Regulation of conformation and ligand binding function of integrin α5β1 by the β1 cytoplasmic domain. J Biol Chem 271:16580-16585.
    • (1996) J Biol Chem , vol.271 , pp. 16580-16585
    • Puzon-McLaughlin, W.1    Yednock, T.A.2    Takada, Y.3
  • 34
    • 0026642556 scopus 로고
    • Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association
    • Reszka AA, Hayashi Y, Horwitz AF. 1992. Identification of amino acid sequences in the integrin β1 cytoplasmic domain implicated in cytoskeletal association. J Cell Biol 117:1321-1330.
    • (1992) J Cell Biol , vol.117 , pp. 1321-1330
    • Reszka, A.A.1    Hayashi, Y.2    Horwitz, A.F.3
  • 36
    • 0031596163 scopus 로고    scopus 로고
    • Use of a β1 integrin-deficient human T cell to identify β1 integrin cytoplasmic domain sequences critical for integrin function
    • Romzek NC, Harris ES, Dell CL, Skronek J, Hasse E, Reynolds PJ, Hunt SW, Shimizu Y. 1998. Use of a β1 integrin-deficient human T cell to identify β1 integrin cytoplasmic domain sequences critical for integrin function. Mol Biol Cell 9:2715-2727.
    • (1998) Mol Biol Cell , vol.9 , pp. 2715-2727
    • Romzek, N.C.1    Harris, E.S.2    Dell, C.L.3    Skronek, J.4    Hasse, E.5    Reynolds, P.J.6    Hunt, S.W.7    Shimizu, Y.8
  • 37
    • 0032549860 scopus 로고    scopus 로고
    • Modulation of β1A integrin functions by tyrosine residues in the β1 cytoplasmic domain
    • Sakai T, Zhang Q, Fässler R, Mosher DF. 1998a. Modulation of β1A integrin functions by tyrosine residues in the β1 cytoplasmic domain. J Cell Biol 141:527-538.
    • (1998) J Cell Biol , vol.141 , pp. 527-538
    • Sakai, T.1    Zhang, Q.2    Fässler, R.3    Mosher, D.F.4
  • 38
    • 0032584382 scopus 로고    scopus 로고
    • Restoration of β1A integrins is required for lysophosphatidic acid-induced migration of β1-null mouse fibroblastic cells
    • Sakai T, Peyruchaud O, Fassler R, Mosher DF. 1998b. Restoration of β1A integrins is required for lysophosphatidic acid-induced migration of β1-null mouse fibroblastic cells. J Biol Chem 273:19378-19382.
    • (1998) J Biol Chem , vol.273 , pp. 19378-19382
    • Sakai, T.1    Peyruchaud, O.2    Fassler, R.3    Mosher, D.F.4
  • 40
    • 0029150292 scopus 로고
    • Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains
    • Schaller MD, Otey CA, Hildebrand JD, Parsons JT. 1995. Focal adhesion kinase and paxillin bind to peptides mimicking β integrin cytoplasmic domains. J Cell Biol 130:1181-1187.
    • (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
  • 41
    • 0028173589 scopus 로고
    • Integrin β1 cytoplasmic domain dominant negative effects revealed by lysophosphatidic acid treatment
    • Smilenov LS, Briesewitz R, Marcantonio EE. 1994. Integrin β1 cytoplasmic domain dominant negative effects revealed by lysophosphatidic acid treatment. Mol Biol Cell 5:1215-1223.
    • (1994) Mol Biol Cell , vol.5 , pp. 1215-1223
    • Smilenov, L.S.1    Briesewitz, R.2    Marcantonio, E.E.3
  • 43
    • 0019989719 scopus 로고
    • Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter
    • Southern PJ, Berg P. 1982. Transformation of mammalian cells to antibiotic resistance with a bacterial gene under control of the SV40 early region promoter. J Mol Appl Genet 1:327-341.
    • (1982) J Mol Appl Genet , vol.1 , pp. 327-341
    • Southern, P.J.1    Berg, P.2
  • 44
    • 0031003706 scopus 로고    scopus 로고
    • The role of conserved amino acid motifs within the integrin β3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation
    • Tahiliani PD, Singh L, Auer KL, LaFlamme SE. 1997. The role of conserved amino acid motifs within the integrin β3 cytoplasmic domain in triggering focal adhesion kinase phosphorylation. J Biol Chem 272:7892-7898.
    • (1997) J Biol Chem , vol.272 , pp. 7892-7898
    • Tahiliani, P.D.1    Singh, L.2    Auer, K.L.3    LaFlamme, S.E.4
  • 45
    • 0022448122 scopus 로고
    • Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin
    • Tamkun JW, DeSimone DW, Fonda D, Patel RS, Buck C, Horwitz AF, Hynes RO. 1986. Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell 42:271-282.
    • (1986) Cell , vol.42 , pp. 271-282
    • Tamkun, J.W.1    DeSimone, D.W.2    Fonda, D.3    Patel, R.S.4    Buck, C.5    Horwitz, A.F.6    Hynes, R.O.7
  • 46
    • 0009482260 scopus 로고
    • Electrophoretic transfer from polyacrylamide gels to nitrocellulose sheets
    • Towbin H, Staehelin T, Gordon J. 1979. Electrophoretic transfer from polyacrylamide gels to nitrocellulose sheets. Proc Natl Acad Sci USA 76:4350-4354.
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350-4354
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 47
    • 0030840113 scopus 로고    scopus 로고
    • Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding
    • Yauch RL, Felsenfeld DP, Kraeft SK, Chen LB, Sheetz MP, Hemler ME. 1997. Mutational evidence for control of cell adhesion through integrin diffusion/clustering, independent of ligand binding. J Exp Med 186:1347-1355.
    • (1997) J Exp Med , vol.186 , pp. 1347-1355
    • Yauch, R.L.1    Felsenfeld, D.P.2    Kraeft, S.K.3    Chen, L.B.4    Sheetz, M.P.5    Hemler, M.E.6
  • 48
    • 0027263655 scopus 로고
    • Distinct functions of integrin α and β subunit cytoplasmic domains in cell spreading and formation of focal adhesions
    • Ylänne J, Chen YL, O'Toole TE, Loftus JC, Takada Y, Ginsberg MH. 1993. Distinct functions of integrin α and β subunit cytoplasmic domains in cell spreading and formation of focal adhesions. J Cell Biol 122:223-234.
    • (1993) J Cell Biol , vol.122 , pp. 223-234
    • Ylänne, J.1    Chen, Y.L.2    O'Toole, T.E.3    Loftus, J.C.4    Takada, Y.5    Ginsberg, M.H.6


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