메뉴 건너뛰기




Volumn 17, Issue 11, 2006, Pages 4827-4836

Integrin signaling through Arg activates p190RhoGAP by promoting its binding to p120RasGAP and recruitment to the membrane

Author keywords

[No Author keywords available]

Indexed keywords

ABELSON KINASE; ACTIN; ENZYME INHIBITOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; INTEGRIN; PROTEIN CDC42; PROTEIN P120; PROTEIN P190; RAC1 PROTEIN; RHO GUANOSINE TRIPHOSPHATASE; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 33750527971     PISSN: 10591524     EISSN: None     Source Type: Journal    
DOI: 10.1091/mbc.E06-02-0132     Document Type: Article
Times cited : (102)

References (46)
  • 1
    • 0035158377 scopus 로고    scopus 로고
    • RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity
    • Arthur, W. T., and Burridge, K. (2001). RhoA inactivation by p190RhoGAP regulates cell spreading and migration by promoting membrane protrusion and polarity. Mol. Biol. Cell 12, 2711-2720.
    • (2001) Mol. Biol. Cell , vol.12 , pp. 2711-2720
    • Arthur, W.T.1    Burridge, K.2
  • 2
    • 0036400641 scopus 로고    scopus 로고
    • Regulation of Rho family GTPases by cell-cell and cell-matrix adhesion
    • Arthur, W. T., Noren, N. K., and Burridge, K. (2002). Regulation of Rho family GTPases by cell-cell and cell-matrix adhesion. Biol. Res. 35, 239-246.
    • (2002) Biol. Res. , vol.35 , pp. 239-246
    • Arthur, W.T.1    Noren, N.K.2    Burridge, K.3
  • 3
    • 0034659526 scopus 로고    scopus 로고
    • Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism
    • Arthur, W. T., Petch, L. A., and Burridge, K. (2000). Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism. Curr. Biol. 10, 719-722.
    • (2000) Curr. Biol. , vol.10 , pp. 719-722
    • Arthur, W.T.1    Petch, L.A.2    Burridge, K.3
  • 6
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage
    • Burridge, K., and Wennerberg, K. (2004). Rho and Rac take center stage. Cell 116, 167-179.
    • (2004) Cell , vol.116 , pp. 167-179
    • Burridge, K.1    Wennerberg, K.2
  • 7
    • 0029153801 scopus 로고
    • c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation
    • Chang, J. H., Gill, S., Settleman, J., and Parsons, S. J. (1995). c-Src regulates the simultaneous rearrangement of actin cytoskeleton, p190RhoGAP, and p120RasGAP following epidermal growth factor stimulation. J. Cell Biol. 130, 355-368.
    • (1995) J. Cell Biol. , vol.130 , pp. 355-368
    • Chang, J.H.1    Gill, S.2    Settleman, J.3    Parsons, S.J.4
  • 8
    • 0035819026 scopus 로고    scopus 로고
    • Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase
    • Dorey, K., Engen, J. R., Kretzschmar, J., Wilm, M., Neubauer, G., Schindler, T., and Superti-Furga, G. (2001). Phosphorylation and structure-based functional studies reveal a positive and a negative role for the activation loop of the c-Abl tyrosine kinase. Oncogene 20, 8075-8084.
    • (2001) Oncogene , vol.20 , pp. 8075-8084
    • Dorey, K.1    Engen, J.R.2    Kretzschmar, J.3    Wilm, M.4    Neubauer, G.5    Schindler, T.6    Superti-Furga, G.7
  • 9
    • 0034634476 scopus 로고    scopus 로고
    • The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain
    • Drugan, J. K., Rogers-Graham, K., Gilmer, T., Campbell, S., and Clark, G. J. (2000). The Ras/p120 GTPase-activating protein (GAP) interaction is regulated by the p120 GAP pleckstrin homology domain. J. Biol. Chem. 275, 35021-35027.
    • (2000) J. Biol. Chem. , vol.275 , pp. 35021-35027
    • Drugan, J.K.1    Rogers-Graham, K.2    Gilmer, T.3    Campbell, S.4    Clark, G.J.5
  • 10
    • 0036467581 scopus 로고    scopus 로고
    • Advances in Rho-dependent actin regulation and oncogenic transformation
    • Frame, M. C., and Brunton, V. G. (2002). Advances in Rho-dependent actin regulation and oncogenic transformation. Curr. Opin. Genet. Dev. 12, 36-43.
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 36-43
    • Frame, M.C.1    Brunton, V.G.2
  • 11
    • 0028987698 scopus 로고
    • Mutation-deletion analysis of a Ca(2+)-dependent phospholipid binding (CaLB) domain within p120 GAP, a GTPase-activating protein for p21 ras
    • Gawler, D. J., Zhang, L. J., and Moran, M. F. (1995a). Mutation-deletion analysis of a Ca(2+)-dependent phospholipid binding (CaLB) domain within p120 GAP, a GTPase-activating protein for p21 ras. Biochem. J. 307, 487-491.
    • (1995) Biochem. J. , vol.307 , pp. 487-491
    • Gawler, D.J.1    Zhang, L.J.2    Moran, M.F.3
  • 12
    • 0028901758 scopus 로고
    • CaLB: A 43 amino acid calcium-dependent membrane/phospholipid binding domain in p120 Ras GTPase-activating protein
    • Gawler, D. J., Zhang, L. J., Reedijk, M., Tung, P. S., and Moran, M. F. (1995b). CaLB: a 43 amino acid calcium-dependent membrane/phospholipid binding domain in p120 Ras GTPase-activating protein. Oncogene 10, 817-825.
    • (1995) Oncogene , vol.10 , pp. 817-825
    • Gawler, D.J.1    Zhang, L.J.2    Reedijk, M.3    Tung, P.S.4    Moran, M.F.5
  • 13
    • 0033552615 scopus 로고    scopus 로고
    • Induction of cell scattering by expression of betal integrins in beta1-deficient epithelial cells requires activation of members of the rho family of GTPases and downregulation of cadherin and catenin function
    • Gimond, C., van Der Flierqq, A., van Delft, S., Brakebusch, C., Kuikman, I., Collard, J. G., Fassler, R., and Sonnenberg, A. (1999). Induction of cell scattering by expression of betal integrins in beta1-deficient epithelial cells requires activation of members of the rho family of GTPases and downregulation of cadherin and catenin function. J. Cell Biol. 147, 1325-1340.
    • (1999) J. Cell Biol. , vol.147 , pp. 1325-1340
    • Gimond, C.1    Van Der Flierqq, A.2    Van Delft, S.3    Brakebusch, C.4    Kuikman, I.5    Collard, J.G.6    Fassler, R.7    Sonnenberg, A.8
  • 14
    • 1942509343 scopus 로고    scopus 로고
    • Adhesion-dependent regulation of p190RhoGAP in the developing brain by the Abl-related gene tyrosine kinase
    • Hernandez, S. E., Settleman, J., and Koleske, A. J. (2004). Adhesion-dependent regulation of p190RhoGAP in the developing brain by the Abl-related gene tyrosine kinase. Curr. Biol. 14, 691-696.
    • (2004) Curr. Biol. , vol.14 , pp. 691-696
    • Hernandez, S.E.1    Settleman, J.2    Koleske, A.J.3
  • 15
    • 0031030898 scopus 로고    scopus 로고
    • Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: A conformational mechanism for SH3 domain regulation
    • Hu, K. Q., and Settleman, J. (1997). Tandem SH2 binding sites mediate the RasGAP-RhoGAP interaction: a conformational mechanism for SH3 domain regulation. EMBO J. 16, 473-483.
    • (1997) EMBO J. , vol.16 , pp. 473-483
    • Hu, K.Q.1    Settleman, J.2
  • 16
    • 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
  • 18
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • Kaibuchi, K., Kuroda, S., and Amano, M. (1999). Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells. Annu. Rev. Biochem. 68, 459-486.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 19
    • 0035844250 scopus 로고    scopus 로고
    • Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes
    • Kain, K. H., and Klemke, R. L. (2001). Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes. J. Biol. Chem. 276, 16185-16192.
    • (2001) J. Biol. Chem. , vol.276 , pp. 16185-16192
    • Kain, K.H.1    Klemke, R.L.2
  • 21
    • 0035189835 scopus 로고    scopus 로고
    • Regulation of extracellular signal-regulated kinase activity by p120 RasGAP does not involve its pleckstrin homology or calcium-dependent lipid binding domains but does require these domains to regulate cell proliferation
    • Koehler, J. A., and Moran, M. F. (2001). Regulation of extracellular signal-regulated kinase activity by p120 RasGAP does not involve its pleckstrin homology or calcium-dependent lipid binding domains but does require these domains to regulate cell proliferation. Cell Growth Differ. 12, 551-561.
    • (2001) Cell Growth Differ. , vol.12 , pp. 551-561
    • Koehler, J.A.1    Moran, M.F.2
  • 23
    • 0034308176 scopus 로고    scopus 로고
    • Biochemical and cellular effects of c-Src kinase-selective pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors
    • Kraker, A. J., Hartl, B. G., Amar, A. M., Barvian, M. R., Showalter, H. D., and Moore, C. W. (2000). Biochemical and cellular effects of c-Src kinase-selective pyrido[2,3-d]pyrimidine tyrosine kinase inhibitors. Biochem. Pharmacol. 60, 885-898.
    • (2000) Biochem. Pharmacol. , vol.60 , pp. 885-898
    • Kraker, A.J.1    Hartl, B.G.2    Amar, A.M.3    Barvian, M.R.4    Showalter, H.D.5    Moore, C.W.6
  • 24
    • 2442505592 scopus 로고    scopus 로고
    • The Abl-related gene (Arg) requires its F-actin-microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion
    • Miller, A. L., Wang, Y., Mooseker, M. S., and Koleske, A. J. (2004). The Abl-related gene (Arg) requires its F-actin-microtubule cross-linking activity to regulate lamellipodial dynamics during fibroblast adhesion. J. Cell Biol. 165, 407-419.
    • (2004) J. Cell Biol. , vol.165 , pp. 407-419
    • Miller, A.L.1    Wang, Y.2    Mooseker, M.S.3    Koleske, A.J.4
  • 25
    • 21544462279 scopus 로고    scopus 로고
    • Integrin-dependent dendrite branch stabilization requires Abl family kinases
    • Moresco, E. M., Donaldson, S., Williamson, A., and Koleske, A. J. (2005). Integrin-dependent dendrite branch stabilization requires Abl family kinases. J. Neurosci. 25, 6105-6118.
    • (2005) J. Neurosci. , vol.25 , pp. 6105-6118
    • Moresco, E.M.1    Donaldson, S.2    Williamson, A.3    Koleske, A.J.4
  • 26
    • 0031594710 scopus 로고    scopus 로고
    • Activation of beta1 integrin signaling stimulates tyrosine phosphorylation of p190RhoGAP and membrane-protrusive activities at invadopodia
    • Nakahara, H., Mueller, S. C., Nomizu, M., Yamada, Y., Yeh, Y., and Chen, W. T. (1998). Activation of beta1 integrin signaling stimulates tyrosine phosphorylation of p190RhoGAP and membrane-protrusive activities at invadopodia. J. Biol. Chem. 273, 9-12.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9-12
    • Nakahara, H.1    Mueller, S.C.2    Nomizu, M.3    Yamada, Y.4    Yeh, Y.5    Chen, W.T.6
  • 27
    • 33646197411 scopus 로고    scopus 로고
    • Spatiotemporal dynamics of RhoA activity in migrating cells
    • Pertz, O., Hodgson, L., Klemke, R. L., and Hahn, K. M. (2006). Spatiotemporal dynamics of RhoA activity in migrating cells. Nature 440, 1069-1072.
    • (2006) Nature , vol.440 , pp. 1069-1072
    • Pertz, O.1    Hodgson, L.2    Klemke, R.L.3    Hahn, K.M.4
  • 28
    • 0033568349 scopus 로고    scopus 로고
    • Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF
    • Plattner, R., Kadlec, L., DeMali, K. A., Kazlauskas, A., and Pendergast, A. M. (1999). c-Abl is activated by growth factors and Src family kinases and has a role in the cellular response to PDGF. Genes Dev. 13, 2400-2411.
    • (1999) Genes Dev. , vol.13 , pp. 2400-2411
    • Plattner, R.1    Kadlec, L.2    Demali, K.A.3    Kazlauskas, A.4    Pendergast, A.M.5
  • 29
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Kiosses, W. B., and Schwartz, M. A. (1999). Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 30
    • 0033777071 scopus 로고    scopus 로고
    • Determination of GTP loading on Rho
    • Ren, X. D., and Schwartz, M. A. (2000). Determination of GTP loading on Rho. Methods Enzymol. 325, 264-272.
    • (2000) Methods Enzymol. , vol.325 , pp. 264-272
    • Ren, X.D.1    Schwartz, M.A.2
  • 31
    • 0034698754 scopus 로고    scopus 로고
    • Rho GTPases. Integrating integrin signaling
    • Ridley, A. (2000). Rho GTPases. Integrating integrin signaling. J. Cell Biol. 150, F107-F109.
    • (2000) J. Cell Biol. , vol.150
    • Ridley, A.1
  • 32
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley, A. J. (2001). Rho family proteins: coordinating cell responses. Trends Cell Biol. 11, 471-477.
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 33
    • 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., and Hall, A. (1992). The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70, 389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 34
    • 0031724591 scopus 로고    scopus 로고
    • Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr 1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation
    • Roof, R. W., Haskell, M. D., Dukes, B. D., Sherman, N., Kinter, M., and Parsons, S. J. (1998). Phosphotyrosine (p-Tyr)-dependent and -independent mechanisms of p190 RhoGAP-p120 RasGAP interaction: Tyr 1105 of p190, a substrate for c-Src, is the sole p-Tyr mediator of complex formation. Mol. Cell. Biol. 18, 7052-7063.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7052-7063
    • Roof, R.W.1    Haskell, M.D.2    Dukes, B.D.3    Sherman, N.4    Kinter, M.5    Parsons, S.J.6
  • 36
    • 0037508877 scopus 로고    scopus 로고
    • Two distinct phosphorylation pathways have additive effects on Abl family kinase activation
    • Tanis, K. Q., Veach, D., Duewel, H. S., Bornmann, W. G., and Koleske, A. J. (2003). Two distinct phosphorylation pathways have additive effects on Abl family kinase activation. Mol. Cell. Biol. 23, 3884-3896.
    • (2003) Mol. Cell. Biol. , vol.23 , pp. 3884-3896
    • Tanis, K.Q.1    Veach, D.2    Duewel, H.S.3    Bornmann, W.G.4    Koleske, A.J.5
  • 37
    • 0037175385 scopus 로고    scopus 로고
    • Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration
    • Tsubouchi, A., Sakakura, J., Yagi, R., Mazaki, Y., Schaefer, E., Yano, H., and Sabe, H. (2002). Localized suppression of RhoA activity by Tyr31/118-phosphorylated paxillin in cell adhesion and migration. J. Cell Biol. 159, 673-683.
    • (2002) J. Cell Biol. , vol.159 , pp. 673-683
    • Tsubouchi, A.1    Sakakura, J.2    Yagi, R.3    Mazaki, Y.4    Schaefer, E.5    Yano, H.6    Sabe, H.7
  • 38
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and D'Souza-Schorey, C. (1997). Rho GTPases and signaling networks. Genes Dev. 11, 2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 39
    • 0035724579 scopus 로고    scopus 로고
    • Function and interactions of integrins
    • van der Flier, A., and Sonnenberg, A. (2001). Function and interactions of integrins. Cell Tissue Res. 305, 285-298.
    • (2001) Cell Tissue Res. , vol.305 , pp. 285-298
    • Van Der Flier, A.1    Sonnenberg, A.2
  • 40
  • 42
    • 0037018155 scopus 로고    scopus 로고
    • Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension
    • Woodring, P. J., Litwack, E. D., O'Leary, D. D., Lucero, G. R., Wang, J. Y., and Hunter, T. (2002). Modulation of the F-actin cytoskeleton by c-Abl tyrosine kinase in cell spreading and neurite extension. J. Cell Biol. 156, 879-892.
    • (2002) J. Cell Biol. , vol.156 , pp. 879-892
    • Woodring, P.J.1    Litwack, E.D.2    O'Leary, D.D.3    Lucero, G.R.4    Wang, J.Y.5    Hunter, T.6
  • 43
    • 2542478972 scopus 로고    scopus 로고
    • c-Abl phosphorylates Dokl to promote filopodia during cell spreading
    • Woodring, P. J., et al. (2004). c-Abl phosphorylates Dokl to promote filopodia during cell spreading. J. Cell Biol. 165, 493-503.
    • (2004) J. Cell Biol. , vol.165 , pp. 493-503
    • Woodring, P.J.1
  • 44
    • 0034757893 scopus 로고    scopus 로고
    • Components of cell-matrix adhesions
    • Zamir, E., and Geiger, B. (2001a). Components of cell-matrix adhesions. J. Cell Sci. 114, 3577-3579.
    • (2001) J. Cell Sci. , vol.114 , pp. 3577-3579
    • Zamir, E.1    Geiger, B.2
  • 45
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir, E., and Geiger, B. (2001b). Molecular complexity and dynamics of cell-matrix adhesions. J. Cell Sci. 114, 3583-3590.
    • (2001) J. Cell Sci. , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 46
    • 0032515909 scopus 로고    scopus 로고
    • Regulation of RhoA GTP hydrolysis by the GTPase-activating proteins p190, p50RhoGAP, Bcr, and 3BP-1
    • Zhang, B., and Zheng, Y. (1998). Regulation of RhoA GTP hydrolysis by the GTPase-activating proteins p190, p50RhoGAP, Bcr, and 3BP-1. Biochemistry 37, 5249-5257.
    • (1998) Biochemistry , vol.37 , pp. 5249-5257
    • Zhang, B.1    Zheng, Y.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.