메뉴 건너뛰기




Volumn 254, Issue 1, 2000, Pages 55-63

Expression of integrin subunit β1B in integrin β1-deficient GD25 cells does not interfere with αVβ3 functions

Author keywords

Cell adhesion; Fibronectin; Integrin; Signaling; Vitronectin

Indexed keywords

BETA1 INTEGRIN; FIBRONECTIN; FOCAL ADHESION KINASE; MANGANESE; PAXILLIN; PEPTIDE; PROTEIN P130; PROTEIN SUBUNIT; VITRONECTIN;

EID: 0034627799     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1006/excr.1999.4722     Document Type: Article
Times cited : (53)

References (50)
  • 2
    • 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
  • 4
    • 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 S. E., Thomas L. A., Yamada S. S., Yamada K. M. 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. 126:1994;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
  • 6
    • 0028170368 scopus 로고
    • Integrin α 2 cytoplasmic domain deletion effects: Loss of adhesive activity parallels ligand-independent recruitment into focal adhesions
    • Kawaguchi S., Bergelson J. M., Finberg R. W., Hemler M. E. Integrin α 2 cytoplasmic domain deletion effects: Loss of adhesive activity parallels ligand-independent recruitment into focal adhesions. Mol. Biol. Cell. 5:1994;977-988.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 977-988
    • Kawaguchi, S.1    Bergelson, J.M.2    Finberg, R.W.3    Hemler, M.E.4
  • 7
    • 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
  • 9
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein
    • Guan J. L., Trevithick J. E., Hynes R. O. Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa 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
  • 10
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks S. K., Calalb M. B., Harper M. C., ad Patel S. K. Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc. Natl. Acad. Sci. USA. 89:1992;8487-8491.
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 8487-8491
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Ad Patel, S.K.4
  • 12
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller M. D., Hildebrand J. D., Shannon J. D., Fox J. W., Vines R. R., Parsons J. T. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol. Cell. Biol. 14:1994;1680-1688.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 13
    • 0028877919 scopus 로고
    • Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases
    • Calalb M. B., Polte T. R., Hanks S. K. Tyrosine phosphorylation of focal adhesion kinase at sites in the catalytic domain regulates kinase activity: A role for Src family kinases. Mol. Cell. Biol. 15:1995;954-963.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 954-963
    • Calalb, M.B.1    Polte, T.R.2    Hanks, S.K.3
  • 14
    • 0029166094 scopus 로고
    • Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase
    • Bellis S. L., Miller J. T., Turner C. E. Characterization of tyrosine phosphorylation of paxillin in vitro by focal adhesion kinase. J. Biol. Chem. 270:1995;17437-17441.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17437-17441
    • Bellis, S.L.1    Miller, J.T.2    Turner, C.E.3
  • 15
    • 0029034873 scopus 로고
    • Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs
    • Nojima Y., Morino N., Mimura T., Hamasaki K., Furuya H., Sakai R., Sato T., Tachibana K., Morimoto C., Yazaki Y. Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130Cas, a Src homology 3-containing molecule having multiple Src homology 2-binding motifs. J. Biol. Chem. 270:1995;15398-15402.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15398-15402
    • Nojima, Y.1    Morino, N.2    Mimura, T.3    Hamasaki, K.4    Furuya, H.5    Sakai, R.6    Sato, T.7    Tachibana, K.8    Morimoto, C.9    Yazaki, Y.10
  • 16
    • 0027939187 scopus 로고
    • Integrin-mediated cell adhesion activates mitogen-activated protein kinases
    • Chen Q., Kinch M. S., Lin T. H., Burridge K., Juliano R. L. 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.L.5
  • 17
    • 0030926774 scopus 로고    scopus 로고
    • Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/Mitogen-activated protein kinase through interactions with and activation of c-Src
    • Schlaepfer D. D., Hunter T. Focal adhesion kinase overexpression enhances ras-dependent integrin signaling to ERK2/Mitogen-activated protein kinase through interactions with and activation of c-Src. J. Biol. Chem. 272:1997;13189-13195.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13189-13195
    • Schlaepfer, D.D.1    Hunter, T.2
  • 19
    • 0030874021 scopus 로고    scopus 로고
    • Integrin-mediated activation of MAP kinase is independent of FAK: Evidence for dual integrin signaling pathways in fibroblasts
    • Lin T. H., Aplin A. E., Shen Y., Chen Q., Schaller M., Romer L., Aukhil I., Juliano R. L. Integrin-mediated activation of MAP kinase is independent of FAK: Evidence for dual integrin signaling pathways in fibroblasts. J. Cell Biol. 136:1997;1385-1395.
    • (1997) J. Cell Biol. , vol.136 , pp. 1385-1395
    • Lin, T.H.1    Aplin, A.E.2    Shen, Y.3    Chen, Q.4    Schaller, M.5    Romer, L.6    Aukhil, I.7    Juliano, R.L.8
  • 20
    • 0029808477 scopus 로고    scopus 로고
    • Dissociation of mitogen-activated protein kinase activation from p125 focal adhesion kinase tyrosine phosphorylation in Swiss 3T3 cells stimulated by bombesin, lysophosphatidic acid, and platelet-derived growth factor
    • Seufferlein T., Withers D. J., Mann D., Rozengurt E. Dissociation of mitogen-activated protein kinase activation from p125 focal adhesion kinase tyrosine phosphorylation in Swiss 3T3 cells stimulated by bombesin, lysophosphatidic acid, and platelet-derived growth factor. Mol. Biol. Cell. 7:1996;1865-1875.
    • (1996) Mol. Biol. Cell , vol.7 , pp. 1865-1875
    • Seufferlein, T.1    Withers, D.J.2    Mann, D.3    Rozengurt, E.4
  • 21
    • 0027454485 scopus 로고
    • Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain
    • Otey C. A., Vasquez G. B., Burridge K., Erickson B. W. Mapping of the α-actinin binding site within the β1 integrin cytoplasmic domain. J. Biol. Chem. 268:1993;21193-21197.
    • (1993) J. Biol. Chem. , vol.268 , pp. 21193-21197
    • Otey, C.A.1    Vasquez, G.B.2    Burridge, K.3    Erickson, B.W.4
  • 23
    • 0032483459 scopus 로고    scopus 로고
    • Filamin binds to the cytoplasmic domain of the β1-integrin: Identification of amino acids responsible for this interaction
    • Loo D. T., Kanner S. B., Aruffo A. Filamin binds to the cytoplasmic domain of the β1-integrin: Identification of amino acids responsible for this interaction. J. Biol. Chem. 273:1998;23304-23312.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23304-23312
    • Loo, D.T.1    Kanner, S.B.2    Aruffo, A.3
  • 24
    • 0022534722 scopus 로고
    • Interaction of plasma membrane fibronectin receptor with talin: A transmembrane linkage
    • Horwitz A., Duggan K., Buck C., Berkerle 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    Berkerle, M.C.4    Burridge, K.5
  • 25
    • 0031893954 scopus 로고    scopus 로고
    • Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit
    • Lilental J., Chang D. D. Rack1, a receptor for activated protein kinase C, interacts with integrin β subunit. J. Biol. Chem. 273:1998;2379-2383.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2379-2383
    • Lilental, J.1    Chang, D.D.2
  • 26
    • 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
  • 27
    • 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 D. D., Wong C., Smith H., Liu J. 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. 138:1997;1149-1157.
    • (1997) J. Cell Biol. , vol.138 , pp. 1149-1157
    • Chang, D.D.1    Wong, C.2    Smith, H.3    Liu, J.4
  • 28
    • 17944392616 scopus 로고    scopus 로고
    • Paxillin association in vitro with integrin cytoplasmic domain peptides
    • Tanaka T., Yamaguchi R., Sabe H., Sekiguchi K., Healy J. M. Paxillin association in vitro with integrin cytoplasmic domain peptides. FEBS Lett. 399:1996;53-58.
    • (1996) FEBS Lett. , vol.399 , pp. 53-58
    • Tanaka, T.1    Yamaguchi, R.2    Sabe, H.3    Sekiguchi, K.4    Healy, J.M.5
  • 29
    • 0032590074 scopus 로고    scopus 로고
    • Interaction of the integrin β1 cytoplasmic domain with ICAP-1 protein
    • Zhang X. A., Hemler M. E. Interaction of the integrin β1 cytoplasmic domain with ICAP-1 protein. J. Biol. Chem. 274:1999;11-19.
    • (1999) J. Biol. Chem. , vol.274 , pp. 11-19
    • Zhang, X.A.1    Hemler, M.E.2
  • 30
    • 0026739356 scopus 로고
    • A alternative form of the integrin β1 subunit with a variant cytoplasmic domain
    • Languino L. R., Ruoslahti E. A alternative form of the integrin β1 subunit with a variant cytoplasmic domain. J. Biol. Chem. 267:1992;7116-7120.
    • (1992) J. Biol. Chem. , vol.267 , pp. 7116-7120
    • Languino, L.R.1    Ruoslahti, E.2
  • 31
    • 0028984183 scopus 로고
    • A novel β1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscle
    • van der Flier A., Kuikman I., Baudoin C., van der Neut R., Sonnenberg A. A novel β1 integrin isoform produced by alternative splicing: Unique expression in cardiac and skeletal muscle. FEBS Lett. 369:1995;340-344.
    • (1995) FEBS Lett. , vol.369 , pp. 340-344
    • Van Der Flier, A.1    Kuikman, I.2    Baudoin, C.3    Van Der Neut, R.4    Sonnenberg, A.5
  • 32
    • 0028978745 scopus 로고
    • Novel isoform of β1 integrin expressed in skeletal and cardiac muscle
    • Zhidkova N. I., Belkin A. M., Mayne R. Novel isoform of β1 integrin expressed in skeletal and cardiac muscle. Biochem. Biophys. Res. Commun. 214:1995;279-285.
    • (1995) Biochem. Biophys. Res. Commun. , vol.214 , pp. 279-285
    • Zhidkova, N.I.1    Belkin, A.M.2    Mayne, R.3
  • 33
    • 0025203926 scopus 로고
    • A human integrin β1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing
    • Altruda F., Cervella P., Tarone G., Botta C., Balzac F., Stefanuto G., Silengo L. A human integrin β1 subunit with a unique cytoplasmic domain generated by alternative mRNA processing. Gene. 95:1990;261-266.
    • (1990) Gene , vol.95 , pp. 261-266
    • Altruda, F.1    Cervella, P.2    Tarone, G.3    Botta, C.4    Balzac, F.5    Stefanuto, G.6    Silengo, L.7
  • 35
    • 0032521631 scopus 로고    scopus 로고
    • Identification of β1C-2, a novel variant of the integrin β1 subunit generated by utilization of an alternative splice acceptor site in exon C
    • Svineng G., Fässler R., Johansson S. Identification of β1C-2, a novel variant of the integrin β1 subunit generated by utilization of an alternative splice acceptor site in exon C. Biochem. J. 330:1998;1255-1263.
    • (1998) Biochem. J. , vol.330 , pp. 1255-1263
    • Svineng, G.1    Fässler, R.2    Johansson, S.3
  • 37
    • 0029837731 scopus 로고    scopus 로고
    • Genomic organization of the mouse β1 gene: Conservation of the β1D but not of the β1B and β1C integrin splice variants
    • Baudoin C., van der Flier A., Borradori L., Sonnenberg A. Genomic organization of the mouse β1 gene: Conservation of the β1D but not of the β1B and β1C integrin splice variants. Cell Adhes. Commun. 4:1996;1-11.
    • (1996) Cell Adhes. Commun. , vol.4 , pp. 1-11
    • Baudoin, C.1    Van Der Flier, A.2    Borradori, L.3    Sonnenberg, A.4
  • 38
  • 39
    • 0026523350 scopus 로고
    • Separation of fibronectin from a plasma gelatinase using immobilized metal affinity chromatography
    • Smilenov L., Forsberg E., Zeligman I., Sparrman M., Johansson S. Separation of fibronectin from a plasma gelatinase using immobilized metal affinity chromatography. FEBS Lett. 302:1992;227-230.
    • (1992) FEBS Lett. , vol.302 , pp. 227-230
    • Smilenov, L.1    Forsberg, E.2    Zeligman, I.3    Sparrman, M.4    Johansson, S.5
  • 40
    • 0024059120 scopus 로고
    • Novel purification of vitronectin from human plasma by heparin affinity chromatography
    • Yatohgo T., Izumi M., Kashiwagi H., Hayashi M. Novel purification of vitronectin from human plasma by heparin affinity chromatography. Cell Struct. Funct. 13:1988;281-292.
    • (1988) Cell Struct. Funct. , vol.13 , pp. 281-292
    • Yatohgo, T.1    Izumi, M.2    Kashiwagi, H.3    Hayashi, M.4
  • 41
    • 0022707292 scopus 로고
    • Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments
    • Woods A., Couchman J. R., Johansson S., Hook M. Adhesion and cytoskeletal organisation of fibroblasts in response to fibronectin fragments. EMBO J. 5:1986;665-670.
    • (1986) EMBO J. , vol.5 , pp. 665-670
    • Woods, A.1    Couchman, J.R.2    Johansson, S.3    Hook, M.4
  • 42
    • 0024385975 scopus 로고
    • Integrin-type fibronectin receptors of rat arterial smooth muscle cells: Isolation, partial characterization and role in cytoskeletal organisation and control of differentiated properties
    • Bottger B. A., Hedin U., Johansson S., Thyberg J. Integrin-type fibronectin receptors of rat arterial smooth muscle cells: Isolation, partial characterization and role in cytoskeletal organisation and control of differentiated properties. Differentiation. 41:1989;158-167.
    • (1989) Differentiation , vol.41 , pp. 158-167
    • Bottger, B.A.1    Hedin, U.2    Johansson, S.3    Thyberg, J.4
  • 43
    • 0028985980 scopus 로고
    • Lack of β1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts
    • Fässler R., Pfaff M., Murphy J., Noegel A. A., Johansson S., Timpl R., Albrecht R. Lack of β1 integrin gene in embryonic stem cells affects morphology, adhesion, and migration but not integration into the inner cell mass of blastocysts. J. Cell Biol. 128:1995;979-988.
    • (1995) J. Cell Biol. , vol.128 , pp. 979-988
    • Fässler, R.1    Pfaff, M.2    Murphy, J.3    Noegel, A.A.4    Johansson, S.5    Timpl, R.6    Albrecht, R.7
  • 45
    • 2642683511 scopus 로고    scopus 로고
    • Mutational analysis of the potential phosphorylation sites in the cytoplasmic domain of integrin β1A: Requirement for threonines 788-789 in receptor activation
    • Wennerberg K., Fässler R., Wärmegård B., Johansson S. Mutational analysis of the potential phosphorylation sites in the cytoplasmic domain of integrin β1A: Requirement for threonines 788-789 in receptor activation. J. Cell Sci. 111:1998;1117-1126.
    • (1998) J. Cell Sci. , vol.111 , pp. 1117-1126
    • Wennerberg, K.1    Fässler, R.2    Wärmegård, B.3    Johansson, S.4
  • 47
    • 0023730954 scopus 로고
    • Regulation of the fibronectin receptor affinity by divalent cations
    • Gailit J., Ruoslahti E. Regulation of the fibronectin receptor affinity by divalent cations. J. Biol. Chem. 263:1988;12927-12933.
    • (1988) J. Biol. Chem. , vol.263 , pp. 12927-12933
    • Gailit, J.1    Ruoslahti, E.2
  • 48
    • 0027421094 scopus 로고
    • A monoclonal antibody against an activation epitope on mouse integrin chain β1 blocks adhesion of lymphocytes to the endothelial integrin α6β1
    • Lenter M., Uhlig H., Hamann A., Jeno P., Imhof B., Vestweber D. A monoclonal antibody against an activation epitope on mouse integrin chain β1 blocks adhesion of lymphocytes to the endothelial integrin α6β1. Proc. Natl. Acad. Sci. USA. 90:1993;9051-9055.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 9051-9055
    • Lenter, M.1    Uhlig, H.2    Hamann, A.3    Jeno, P.4    Imhof, B.5    Vestweber, D.6
  • 49
    • 0028858576 scopus 로고
    • Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium
    • Bazzoni G., Shih D. T., Buck C. A., Hemler M. E. Monoclonal antibody 9EG7 defines a novel β1 integrin epitope induced by soluble ligand and manganese, but inhibited by calcium. J. Biol. Chem. 270:1995;25570-25577.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25570-25577
    • Bazzoni, G.1    Shih, D.T.2    Buck, C.A.3    Hemler, M.E.4
  • 50
    • 0032549671 scopus 로고    scopus 로고
    • Divalent cations and ligands induce conformational changes that are highly divergent among beta1 integrins
    • Bazzoni G., Ma L., Blue M. L., Hemler M. E. Divalent cations and ligands induce conformational changes that are highly divergent among beta1 integrins. J. Biol. Chem. 273:1998;6670-6678.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6670-6678
    • Bazzoni, G.1    Ma, L.2    Blue, M.L.3    Hemler, M.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.