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Volumn 287, Issue 15, 2012, Pages 12491-12500

Cross-talk between integrin α6β4 and Insulin-like Growth Factor-1 Receptor (IGF1R) through direct α6β4 binding to IGF1 and subsequent α6β4-IGF1-IGF1R ternary complex formation in anchorage-independent conditions

Author keywords

[No Author keywords available]

Indexed keywords

CANCER PROGRESSION; CELL SURVIVAL; CELL-MATRIX ADHESION; COLONY FORMATION; CURRENT MODELS; EXTRACELLULAR MATRIX PROTEIN; IN-VIVO; INSULIN-LIKE GROWTH FACTOR-1; INSULIN-LIKE GROWTH FACTOR-1 RECEPTORS; INTEGRINS; INTRACELLULAR SIGNALING; SOFT AGAR; TERNARY COMPLEX; THERAPEUTIC TARGETS;

EID: 84859515413     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.304170     Document Type: Article
Times cited : (43)

References (35)
  • 1
    • 34848845313 scopus 로고    scopus 로고
    • Modifying IGF1 activity: An approach to treat endocrine disorders, atherosclerosis, and cancer
    • Clemmons, D. R. (2007) Modifying IGF1 activity: an approach to treat endocrine disorders, atherosclerosis, and cancer. Nat. Rev. Drug Discov. 6, 821-833
    • (2007) Nat. Rev. Drug Discov. , vol.6 , pp. 821-833
    • Clemmons, D.R.1
  • 2
    • 11244352382 scopus 로고    scopus 로고
    • Interaction between insulin-like growth factor-I receptor and αVβ3 integrin linked signaling pathways: Cellular responses to changes in multiple signaling inputs
    • DOI 10.1210/me.2004-0376
    • Clemmons, D. R., and Maile, L. A. (2005) Interaction between insulin-like growth factor-1 receptor- and αvβ3 integrin-linked signaling pathways: cellular responses to changes in multiple signaling inputs. Mol. Endocrinol. 19, 1-11 (Pubitemid 40065954)
    • (2005) Molecular Endocrinology , vol.19 , Issue.1 , pp. 1-11
    • Clemmons, D.R.1    Maile, L.A.2
  • 3
    • 0029432433 scopus 로고
    • Cell migration: Interactions among integrins, IGFs and IGFBPs
    • Jones, J. I., Doerr, M. E., and Clemmons, D. R. (1995) Cell migration: interactions among integrins, IGFs and IGFBPs. Prog. Growth Factor Res. 6, 319-327
    • (1995) Prog. Growth Factor Res. , vol.6 , pp. 319-327
    • Jones, J.I.1    Doerr, M.E.2    Clemmons, D.R.3
  • 4
    • 0032530109 scopus 로고    scopus 로고
    • Blocking ligand occupancy of the αVβ3 integrin inhibits insulin-like growth factor I signaling in vascular smooth muscle cells
    • DOI 10.1073/pnas.95.19.11217
    • Zheng, B., and Clemmons, D. R. (1998) Blocking ligand occupancy of the αvβ3 integrin inhibits insulin-like growth factor-1 signaling in vascular smooth muscle cells. Proc. Natl. Acad. Sci. U.S.A. 95, 11217-11222 (Pubitemid 28450108)
    • (1998) Proceedings of the National Academy of Sciences of the United States of America , vol.95 , Issue.19 , pp. 11217-11222
    • Zheng, B.1    Clemmons, D.R.2
  • 5
    • 69949177417 scopus 로고    scopus 로고
    • The direct binding of insulin-like growth factor-1 (IGF-1) to integrin αvβ3 is involved in IGF-1 signaling
    • Saegusa, J., Yamaji, S., Ieguchi, K., Wu, C. Y., Lam, K. S., Liu, F. T., Takada, Y. K., and Takada, Y. (2009) The direct binding of insulin-like growth factor-1 (IGF-1) to integrin αvβ3 is involved in IGF-1 signaling. J. Biol. Chem. 284, 24106-24114
    • (2009) J. Biol. Chem. , vol.284 , pp. 24106-24114
    • Saegusa, J.1    Yamaji, S.2    Ieguchi, K.3    Wu, C.Y.4    Lam, K.S.5    Liu, F.T.6    Takada, Y.K.7    Takada, Y.8
  • 6
    • 33645380797 scopus 로고    scopus 로고
    • Ligand-binding specificities of laminin-binding integrins: A comprehensive survey of laminin-integrin interactions using recombinant α3β1, α6β1, α7β1, and α6β4 integrins
    • Nishiuchi, R., Takagi, J., Hayashi, M., Ido, H., Yagi, Y., Sanzen, N., Tsuji, T., Yamada, M., and Sekiguchi, K. (2006) Ligand-binding specificities of laminin-binding integrins: a comprehensive survey of laminin-integrin interactions using recombinant α3β1, α6β1, α7β1, and α6β4 integrins. Matrix Biol. 25, 189-197
    • (2006) Matrix Biol. , vol.25 , pp. 189-197
    • Nishiuchi, R.1    Takagi, J.2    Hayashi, M.3    Ido, H.4    Yagi, Y.5    Sanzen, N.6    Tsuji, T.7    Yamada, M.8    Sekiguchi, K.9
  • 7
    • 0030856555 scopus 로고    scopus 로고
    • Changing ligand specificities of αvβ1 and αvβ3 integrins by swapping a short diverse sequence of the β subunit
    • DOI 10.1074/jbc.272.32.19794
    • Takagi, J., Kamata, T., Meredith, J., Puzon-McLaughlin, W., and Takada, Y. (1997) Changing ligand specificities of αvβ1 and αvβ3 integrins by swapping a short diverse sequence of the β subunit. J. Biol. Chem. 272, 19794-19800 (Pubitemid 27340072)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.32 , pp. 19794-19800
    • Takagi, J.1    Kamata, T.2    Meredith, J.3    Puzon-McLaughlin, W.4    Takada, Y.5
  • 9
    • 77957765881 scopus 로고    scopus 로고
    • Direct binding of the EGF-like domain of neuregulin-1 to integrins (αvβ3 and α6β4) is involved in neuregulin-1/ErbB signaling
    • Ieguchi, K., Fujita, M., Ma, Z., Davari, P., Taniguchi, Y., Sekiguchi, K., Wang, B., Takada, Y. K., and Takada, Y. (2010) Direct binding of the EGF-like domain of neuregulin-1 to integrins (αvβ3 and α6β4) is involved in neuregulin-1/ErbB signaling. J. Biol. Chem. 285, 31388-31398
    • (2010) J. Biol. Chem. , vol.285 , pp. 31388-31398
    • Ieguchi, K.1    Fujita, M.2    Ma, Z.3    Davari, P.4    Taniguchi, Y.5    Sekiguchi, K.6    Wang, B.7    Takada, Y.K.8    Takada, Y.9
  • 10
    • 0021878620 scopus 로고
    • Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein
    • Brown, P. J., and Juliano, R. L. (1985) Selective inhibition of fibronectin-mediated cell adhesion by monoclonal antibodies to a cell-surface glycoprotein. Science 228, 1448-1451 (Pubitemid 15041325)
    • (1985) Science , vol.228 , Issue.4706 , pp. 1448-1451
    • Brown, P.J.1    Juliano, R.L.2
  • 11
    • 0023714090 scopus 로고
    • Monoclonal antibodies to distinctive epitopes on the α and β subunits of the fibronectin receptor
    • Brown, P. J., and Juliano, R. L. (1988) Monoclonal antibodies to distinctive epitopes on the α and β subunits of the fibronectin receptor. Exp. Cell Res. 177, 303-318
    • (1988) Exp. Cell Res. , vol.177 , pp. 303-318
    • Brown, P.J.1    Juliano, R.L.2
  • 12
    • 0029078999 scopus 로고
    • A microplate assay for quantitation of anchorage-independent growth of transformed cells
    • Fukazawa, H., Mizuno, S., and Uehara, Y. (1995) A microplate assay for quantitation of anchorage-independent growth of transformed cells. Anal. Biochem. 228, 83-90
    • (1995) Anal. Biochem. , vol.228 , pp. 83-90
    • Fukazawa, H.1    Mizuno, S.2    Uehara, Y.3
  • 13
    • 0030913268 scopus 로고    scopus 로고
    • Structural interlock between ligand-binding site and stalk-like region of β1 integrin revealed by a monoclonal antibody recognizing conformation-dependent epitope
    • Takagi, J., Isobe, T., Takada, Y., and Saito, Y. (1997) Structural interlock between ligand-binding site and stalk-like region of β1 integrin revealed by a monoclonal antibody recognizing conformation-dependent epitope. J. Biochem. 121, 914-921 (Pubitemid 27236910)
    • (1997) Journal of Biochemistry , vol.121 , Issue.5 , pp. 914-921
    • Takagi, J.1    Isobe, T.2    Takada, Y.3    Saito, Y.4
  • 15
    • 0034678063 scopus 로고    scopus 로고
    • 3
    • DOI 10.1074/jbc.275.11.7795
    • Puzon-McLaughlin, W., Kamata, T., and Takada, Y. (2000) Multiple discontinuous ligand-mimetic antibody-binding sites define a ligand-binding pocket in integrin αIIbß3. J. Biol. Chem. 275, 7795-7802 (Pubitemid 30159685)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 7795-7802
    • Puzon-McLaughlin, W.1    Kamata, T.2    Takada, Y.3
  • 17
    • 0030028186 scopus 로고    scopus 로고
    • The roles of integrins and extracellular matrix proteins in the insulin-like growth factor-1-stimulated chemotaxis of human breast cancer cells
    • Doerr, M. E., and Jones, J. I. (1996) The roles of integrins and extracellular matrix proteins in the insulin-like growth factor-1-stimulated chemotaxis of human breast cancer cells. J. Biol. Chem. 271, 2443-2447
    • (1996) J. Biol. Chem. , vol.271 , pp. 2443-2447
    • Doerr, M.E.1    Jones, J.I.2
  • 18
    • 27644496163 scopus 로고    scopus 로고
    • Mobilization and activation of a signaling competent α6β4 integrin underlies its contribution to carcinoma progression
    • DOI 10.1007/s10555-005-5133-4
    • Lipscomb, E. A., and Mercurio, A. M. (2005) Mobilization and activation of a signaling-competent α6β4 integrin underlies its contribution to carcinoma progression. Cancer Metastasis Rev. 24, 413-423 (Pubitemid 41569981)
    • (2005) Cancer and Metastasis Reviews , vol.24 , Issue.3 , pp. 413-423
    • Lipscomb, E.A.1    Mercurio, A.M.2
  • 19
    • 70849083491 scopus 로고    scopus 로고
    • Integrin signal masks growth promotion activity of HB-EGF in monolayer cell cultures
    • Mizushima, H., Wang, X., Miyamoto, S., and Mekada, E. (2009) Integrin signal masks growth promotion activity of HB-EGF in monolayer cell cultures. J. Cell Sci. 122, 4277-4286
    • (2009) J. Cell Sci. , vol.122 , pp. 4277-4286
    • Mizushima, H.1    Wang, X.2    Miyamoto, S.3    Mekada, E.4
  • 20
    • 0018140371 scopus 로고
    • Role of cell shape in growth control
    • DOI 10.1038/273345a0
    • Folkman, J., and Moscona, A. (1978) Role of cell shape in growth control. Nature 273, 345-349 (Pubitemid 8344174)
    • (1978) Nature , vol.273 , Issue.5661 , pp. 345-349
    • Folkman, J.1    Moscona, A.2
  • 21
    • 0031572320 scopus 로고    scopus 로고
    • Modulation of myoepithelial-associated α6β4 integrin in a breast cancer cell line alters invasive potential
    • DOI 10.1006/excr.1997.3662
    • Jones, J. L., Royall, J. E., Critchley, D. R., and Walker, R. A. (1997) Modulation of myoepithelial-associated α6β4 integrin in a breast cancer cell line alters invasive potential. Exp. Cell Res. 235, 325-333 (Pubitemid 27398390)
    • (1997) Experimental Cell Research , vol.235 , Issue.2 , pp. 325-333
    • Jones, J.L.1    Royall, J.E.2    Critchley, D.R.3    Walker, R.A.4
  • 22
    • 39749084606 scopus 로고    scopus 로고
    • Analysis of integrin β4 expression in human breast cancer: Association with basal-like tumors and prognostic significance
    • DOI 10.1158/1078-0432.CCR-07-4116
    • Lu, S., Simin, K., Khan, A., and Mercurio, A. M. (2008) Analysis of integrin β4 expression in human breast cancer: association with basal-like tumors and prognostic significance. Clin. Cancer Res. 14, 1050-1058 (Pubitemid 351302550)
    • (2008) Clinical Cancer Research , vol.14 , Issue.4 , pp. 1050-1058
    • Lu, S.1    Simin, K.2    Khan, A.3    Mercurio, A.M.4
  • 23
    • 0022976007 scopus 로고
    • Expression of tumor antigen correlated with metastatic potential of Lewis lung carcinoma and B16 melanoma clones in mice
    • Falcioni, R., Kennel, S. J., Giacomini, P., Zupi, G., and Sacchi, A. (1986) Expression of tumor antigen correlated with metastatic potential of Lewis lung carcinoma and B16 melanoma clones in mice. Cancer Res. 46, 5772-5778 (Pubitemid 17177984)
    • (1986) Cancer Research , vol.46 , Issue.11 , pp. 5772-5778
    • Falcioni, R.1    Kennel, S.J.2    Giacomini, P.3
  • 24
    • 0032908323 scopus 로고    scopus 로고
    • Structure and function of hemidesmosomes: More than simple adhesion complexes
    • DOI 10.1046/j.1523-1747.1999.00546.x
    • Borradori, L., and Sonnenberg, A. (1999) Structure and function of hemidesmosomes: more than simple adhesion complexes. J. Invest. Dermatol. 112, 411-418 (Pubitemid 29171928)
    • (1999) Journal of Investigative Dermatology , vol.112 , Issue.4 , pp. 411-418
    • Borradori, L.1    Sonnenberg, A.2
  • 25
    • 0142061975 scopus 로고    scopus 로고
    • Use of RNA interference to inhibit integrin (α6β4)-mediated invasion and migration of breast carcinoma cells
    • DOI 10.1023/A:1025819521707
    • Lipscomb, E. A., Dugan, A. S., Rabinovitz, I., and Mercurio, A. M. (2003) Use of RNA interference to inhibit integrin α6β4-mediated invasion and migration of breast carcinoma cells. Clin. Exp. Metastasis 20, 569-576 (Pubitemid 37297186)
    • (2003) Clinical and Experimental Metastasis , vol.20 , Issue.6 , pp. 569-576
    • Lipscomb, E.A.1    Dugan, A.S.2    Rabinovitz, I.3    Mercurio, A.M.4
  • 26
    • 33745186855 scopus 로고    scopus 로고
    • Loss of β4 integrin subunit reduces the tumorigenicity of MCF-7 mammary cells and causes apoptosis upon hormone deprivation
    • Bon, G., Folgiero, V., Bossi, G., Felicioni, L., Marchetti, A., Sacchi, A., and Falcioni, R. (2006) Loss of β4 integrin subunit reduces the tumorigenicity of MCF-7 mammary cells and causes apoptosis upon hormone deprivation. Clin. Cancer Res. 12, 3280-3287
    • (2006) Clin. Cancer Res. , vol.12 , pp. 3280-3287
    • Bon, G.1    Folgiero, V.2    Bossi, G.3    Felicioni, L.4    Marchetti, A.5    Sacchi, A.6    Falcioni, R.7
  • 28
    • 0034615933 scopus 로고    scopus 로고
    • 4 integrin and ErbB-2 receptor is required to promote phosphatidylinositol 3-kinase-dependent invasion
    • DOI 10.1074/jbc.275.14.10604
    • Gambaletta, D., Marchetti, A., Benedetti, L., Mercurio, A. M., Sacchi, A., and Falcioni, R. (2000) Cooperative signaling between α6β4 integrin and ErbB2 receptor is required to promote phosphatidylinositol 3-kinase-dependent invasion. J. Biol. Chem. 275, 10604-10610 (Pubitemid 30202127)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.14 , pp. 10604-10610
    • Gambaletta, D.1    Marchetti, A.2    Benedetti, L.3    Mercurio, A.M.4    Sacchi, A.5    Falcioni, R.6
  • 29
    • 33746764457 scopus 로고    scopus 로고
    • β4 Integrin Amplifies ErbB2 Signaling to Promote Mammary Tumorigenesis
    • DOI 10.1016/j.cell.2006.05.047, PII S009286740600907X
    • Guo, W., Pylayeva, Y., Pepe, A., Yoshioka, T., Muller, W. J., Inghirami, G., and Giancotti, F. G. (2006) β4 integrin amplifies ErbB2 signaling to promote mammary tumorigenesis. Cell 126, 489-502 (Pubitemid 44163602)
    • (2006) Cell , vol.126 , Issue.3 , pp. 489-502
    • Guo, W.1    Pylayeva, Y.2    Pepe, A.3    Yoshioka, T.4    Muller, W.J.5    Inghirami, G.6    Giancotti, F.G.7
  • 30
    • 3543011958 scopus 로고    scopus 로고
    • 4 integrin can function independently to promote carcinoma invasion
    • DOI 10.1074/jbc.M403809200
    • Chung, J., Yoon, S. O., Lipscomb, E. A., and Mercurio, A. M. (2004) The Met receptor and α6β4 integrin can function independently to promote carcinoma invasion. J. Biol. Chem. 279, 32287-32293 (Pubitemid 39014679)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.31 , pp. 32287-32293
    • Chung, J.1    Yoon, S.-O.2    Lipscomb, E.A.3    Mercurio, A.M.4
  • 31
    • 11244304502 scopus 로고    scopus 로고
    • Palmitoylation supports assembly and function of integrin-tetraspanin complexes
    • DOI 10.1083/jcb.200404100
    • Yang, X., Kovalenko, O. V., Tang, W., Claas, C., Stipp, C. S., and Hemler, M. E. (2004) Palmitoylation supports assembly and function of integrintetraspanin complexes. J. Cell Biol. 167, 1231-1240 (Pubitemid 40066636)
    • (2004) Journal of Cell Biology , vol.167 , Issue.6 , pp. 1231-1240
    • Yang, X.1    Kovalenko, O.V.2    Tang, W.3    Claas, C.4    Stipp, C.S.5    Hemler, M.E.6
  • 32
    • 1542676834 scopus 로고    scopus 로고
    • The interacting binding domains of the β4 integrin and calcium- activated chloride channels (CLCAs) in metastasis
    • Abdel-Ghany, M., Cheng, H. C., Elble, R. C., Lin, H., DiBiasio, J., and Pauli, B. U. (2003) The interacting binding domains of the β4 integrin and calcium- activated chloride channels (CLCAs) in metastasis. J. Biol. Chem. 278, 49406-49416
    • (2003) J. Biol. Chem. , vol.278 , pp. 49406-49416
    • Abdel-Ghany, M.1    Cheng, H.C.2    Elble, R.C.3    Lin, H.4    DiBiasio, J.5    Pauli, B.U.6
  • 33
    • 0027248518 scopus 로고
    • 1 subunit using activating and inhibiting antibodies
    • Takada, Y., and Puzon, W. (1993) Identification of a regulatory region of integrin β1 subunit using activating and inhibiting antibodies. J. Biol. Chem. 268, 17597-17601 (Pubitemid 23237006)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.23 , pp. 17597-17601
    • Takada, Y.1    Puzon, W.2
  • 34
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes, R. O. (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110, 673-687
    • (2002) Cell , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 35
    • 0032528060 scopus 로고    scopus 로고
    • Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain
    • DOI 10.1093/emboj/17.14.3940
    • Murgia, C., Blaikie, P., Kim, N., Dans, M., Petrie, H. T., and Giancotti, F. G. (1998) Cell cycle and adhesion defects in mice carrying a targeted deletion of the integrin β4 cytoplasmic domain. EMBO J. 17, 3940-3951 (Pubitemid 28333980)
    • (1998) EMBO Journal , vol.17 , Issue.14 , pp. 3940-3951
    • Murgia, C.1    Blaikie, P.2    Kim, N.3    Dans, M.4    Petrie, H.T.5    Giancotti, F.G.6


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