메뉴 건너뛰기




Volumn 290, Issue 7, 2015, Pages 4149-4162

Epidermal growth factor activates the Rho GTPase-activating protein (GAP) deleted in liver cancer 1 via focal adhesion kinase and protein phosphatase 2A

Author keywords

[No Author keywords available]

Indexed keywords

ADHESION; AMINO ACIDS; CHEMICAL ACTIVATION; DISEASES; ENZYMES; GROWTH KINETICS; PHOSPHATASES;

EID: 84928946687     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M114.616839     Document Type: Article
Times cited : (21)

References (44)
  • 1
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe, A. B., and Hall, A. (2005) Rho GTPases: biochemistry and biology. Annu. Rev. Cell Dev. Biol. 21, 247-269
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 2
    • 0035516140 scopus 로고    scopus 로고
    • Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk
    • Geiger, B., Bershadsky, A., Pankov, R., and Yamada, K. M. (2001) Transmembrane crosstalk between the extracellular matrix-cytoskeleton crosstalk. Nat. Rev. Mol. Cell Biol. 2, 793-805
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 793-805
    • Geiger, B.1    Bershadsky, A.2    Pankov, R.3    Yamada, K.M.4
  • 4
    • 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
  • 5
    • 0029166671 scopus 로고
    • Rho, rac and cdc42 GTPases: Regulators of actin structures, cell adhesion and motility
    • Nobes, C. D., and Hall, A. (1995) Rho, rac and cdc42 GTPases: regulators of actin structures, cell adhesion and motility. Biochem. Soc. Trans. 23, 456-459
    • (1995) Biochem. Soc. Trans. , vol.23 , pp. 456-459
    • Nobes, C.D.1    Hall, A.2
  • 6
    • 46249127761 scopus 로고    scopus 로고
    • DLC1: A significant GAP in the cancer genome
    • Lahoz, A., and Hall, A. (2008) DLC1: a significant GAP in the cancer genome. Genes Dev. 22, 1724-1730
    • (2008) Genes Dev. , vol.22 , pp. 1724-1730
    • Lahoz, A.1    Hall, A.2
  • 7
    • 0344844475 scopus 로고    scopus 로고
    • Genetic and epigenetic alterations of DLC-1 gene in hepatocellular carcinoma
    • Wong, C. M., Lee, J. M., Ching, Y. P., Jin, D. Y., and Ng, I. O. (2003) Genetic and epigenetic alterations of DLC-1 gene in hepatocellular carcinoma. Cancer Res. 63, 7646-7651
    • (2003) Cancer Res. , vol.63 , pp. 7646-7651
    • Wong, C.M.1    Lee, J.M.2    Ching, Y.P.3    Jin, D.Y.4    Ng, I.O.5
  • 9
    • 57749113537 scopus 로고    scopus 로고
    • Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration
    • Kim, T. Y., Healy, K. D., Der, C. J., Sciaky, N., Bang, Y. J., and Juliano, R. L. (2008) Effects of structure of Rho GTPase-activating protein DLC-1 on cell morphology and migration. J. Biol. Chem. 283, 32762-32770
    • (2008) J. Biol. Chem. , vol.283 , pp. 32762-32770
    • Kim, T.Y.1    Healy, K.D.2    Der, C.J.3    Sciaky, N.4    Bang, Y.J.5    Juliano, R.L.6
  • 10
    • 48149111026 scopus 로고    scopus 로고
    • DLC1 suppresses distant dissemination of human hepatocellular carcinoma cells in nude mice through reduction of RhoA GTPase activity, actin cytoskeletal disruption and down-regulation of genes involved in metastasis
    • Zhou, X., Zimonjic, D. B., Park, S. W., Yang, X. Y., Durkin, M. E., and Popescu, N. C. (2008) DLC1 suppresses distant dissemination of human hepatocellular carcinoma cells in nude mice through reduction of RhoA GTPase activity, actin cytoskeletal disruption and down-regulation of genes involved in metastasis. Int. J. Oncol. 32, 1285-1291
    • (2008) Int. J. Oncol. , vol.32 , pp. 1285-1291
    • Zhou, X.1    Zimonjic, D.B.2    Park, S.W.3    Yang, X.Y.4    Durkin, M.E.5    Popescu, N.C.6
  • 11
    • 67650395349 scopus 로고    scopus 로고
    • Overexpression of DLC-1 induces cell apoptosis and proliferation inhibition in the renal cell carcinoma
    • Zhang, T., Zheng, J., Jiang, N., Wang, G., Shi, Q., Liu, C., and Lu, Y. (2009) Overexpression of DLC-1 induces cell apoptosis and proliferation inhibition in the renal cell carcinoma. Cancer Lett. 283, 59-67
    • (2009) Cancer Lett. , vol.283 , pp. 59-67
    • Zhang, T.1    Zheng, J.2    Jiang, N.3    Wang, G.4    Shi, Q.5    Liu, C.6    Lu, Y.7
  • 12
    • 25444499134 scopus 로고    scopus 로고
    • Rho GTPase-activating protein deleted in liver cancer suppresses cell proliferation and invasion in hepatocellular carcinoma
    • Wong, C. M., Yam, J. W., Ching, Y. P., Yau, T. O., Leung, T. H., Jin, D. Y., and Ng, I. O. (2005) Rho GTPase-activating protein deleted in liver cancer suppresses cell proliferation and invasion in hepatocellular carcinoma. Cancer Res. 65, 8861-8868
    • (2005) Cancer Res. , vol.65 , pp. 8861-8868
    • Wong, C.M.1    Yam, J.W.2    Ching, Y.P.3    Yau, T.O.4    Leung, T.H.5    Jin, D.Y.6    Ng, I.O.7
  • 14
    • 68549130674 scopus 로고    scopus 로고
    • Role of DLC-1, a tumor suppressor protein with RhoGAP activity, in regulation of the cytoskeleton and cell motility
    • Kim, T. Y., Vigil, D., Der, C. J., and Juliano, R. L. (2009) Role of DLC-1, a tumor suppressor protein with RhoGAP activity, in regulation of the cytoskeleton and cell motility. Cancer Metastasis Rev. 28, 77-83
    • (2009) Cancer Metastasis Rev. , vol.28 , pp. 77-83
    • Kim, T.Y.1    Vigil, D.2    Der, C.J.3    Juliano, R.L.4
  • 16
    • 84863115497 scopus 로고    scopus 로고
    • Differential regulation of the activity of deleted in liver cancer 1 (DLC1) by tensins controls cell migration and transformation
    • Cao, X., Voss, C., Zhao, B., Kaneko, T., and Li, S. S. (2012) Differential regulation of the activity of deleted in liver cancer 1 (DLC1) by tensins controls cell migration and transformation. Proc. Natl. Acad. Sci. U.S.A. 109, 1455-1460
    • (2012) Proc. Natl. Acad. Sci. U.S.A. , vol.109 , pp. 1455-1460
    • Cao, X.1    Voss, C.2    Zhao, B.3    Kaneko, T.4    Li, S.S.5
  • 17
    • 33748994597 scopus 로고    scopus 로고
    • Interaction of deleted in liver cancer 1 with tensin2 in caveolae and implications in tumor suppression
    • Yam, J. W., Ko, F. C., Chan, C. Y., Jin, D. Y., and Ng, I. O. (2006) Interaction of deleted in liver cancer 1 with tensin2 in caveolae and implications in tumor suppression. Cancer Res. 66, 8367-8372
    • (2006) Cancer Res. , vol.66 , pp. 8367-8372
    • Yam, J.W.1    Ko, F.C.2    Chan, C.Y.3    Jin, D.Y.4    Ng, I.O.5
  • 19
    • 33846010146 scopus 로고    scopus 로고
    • The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1
    • Liao, Y. C., Si, L., deVere White, R. W., and Lo, S. H. (2007) The phosphotyrosine-independent interaction of DLC-1 and the SH2 domain of cten regulates focal adhesion localization and growth suppression activity of DLC-1. J. Cell Biol. 176, 43-49
    • (2007) J. Cell Biol. , vol.176 , pp. 43-49
    • Liao, Y.C.1    Si, L.2    DeVere White, R.W.3    Lo, S.H.4
  • 20
    • 80054725723 scopus 로고    scopus 로고
    • Full activity of the deleted in liver cancer 1 (DLC1) tumor suppressor depends on an LD-like motif that binds talin and focal adhesion kinase (FAK)
    • Li, G., Du, X., Vass, W. C., Papageorge, A. G., Lowy, D. R., and Qian, X. (2011) Full activity of the deleted in liver cancer 1 (DLC1) tumor suppressor depends on an LD-like motif that binds talin and focal adhesion kinase (FAK). Proc. Natl. Acad. Sci. U.S.A. 108, 17129-17134
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 17129-17134
    • Li, G.1    Du, X.2    Vass, W.C.3    Papageorge, A.G.4    Lowy, D.R.5    Qian, X.6
  • 21
    • 84865342852 scopus 로고    scopus 로고
    • Modularity and functional plasticity of scaffold proteins as p(l)acemakers in cell signaling
    • Pan, C. Q., Sudol, M., Sheetz, M., and Low, B. C. (2012) Modularity and functional plasticity of scaffold proteins as p(l)acemakers in cell signaling. Cell. Signal. 24, 2143-2165
    • (2012) Cell. Signal. , vol.24 , pp. 2143-2165
    • Pan, C.Q.1    Sudol, M.2    Sheetz, M.3    Low, B.C.4
  • 22
    • 84922678938 scopus 로고    scopus 로고
    • Concerted modulation of paxillin dynamics at focal adhesions by deleted in liver cancer-1 and focal adhesion kinase during early cell spreading
    • Kaushik, S., Ravi, A., Hameed, F. M., and Low, B. C. (2014) Concerted modulation of paxillin dynamics at focal adhesions by deleted in liver cancer-1 and focal adhesion kinase during early cell spreading. Cytoskeleton (Hoboken) 10.1002/cm.21201
    • (2014) Cytoskeleton (Hoboken)
    • Kaushik, S.1    Ravi, A.2    Hameed, F.M.3    Low, B.C.4
  • 23
    • 54249145175 scopus 로고    scopus 로고
    • Mutations in the focal adhesion targeting region of deleted in liver cancer-1 attenuate their expression and function
    • Liao, Y. C., Shih, Y. P., and Lo, S. H. (2008) Mutations in the focal adhesion targeting region of deleted in liver cancer-1 attenuate their expression and function. Cancer Res. 68, 7718-7722
    • (2008) Cancer Res. , vol.68 , pp. 7718-7722
    • Liao, Y.C.1    Shih, Y.P.2    Lo, S.H.3
  • 25
    • 0034651747 scopus 로고    scopus 로고
    • A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation
    • Ito, A., Kataoka, T. R., Watanabe, M., Nishiyama, K., Mazaki, Y., Sabe, H., Kitamura, Y., and Nojima, H. (2000) A truncated isoform of the PP2A B56 subunit promotes cell motility through paxillin phosphorylation. EMBO J. 19, 562-571
    • (2000) EMBO J. , vol.19 , pp. 562-571
    • Ito, A.1    Kataoka, T.R.2    Watanabe, M.3    Nishiyama, K.4    Mazaki, Y.5    Sabe, H.6    Kitamura, Y.7    Nojima, H.8
  • 31
    • 71849099556 scopus 로고    scopus 로고
    • Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells
    • Takeuchi, T., Takahashi, N., Ishi, K., Kusayanagi, T., Kuramochi, K., and Sugawara, F. (2009) Antitumor antibiotic fostriecin covalently binds to cysteine-269 residue of protein phosphatase 2A catalytic subunit in mammalian cells. Bioorg. Med. Chem. 17, 8113-8122
    • (2009) Bioorg. Med. Chem. , vol.17 , pp. 8113-8122
    • Takeuchi, T.1    Takahashi, N.2    Ishi, K.3    Kusayanagi, T.4    Kuramochi, K.5    Sugawara, F.6
  • 32
    • 70349332774 scopus 로고    scopus 로고
    • Focal adhesion kinase: Switching between GAPs and GEFs in the regulation of cell motility
    • Tomar, A., and Schlaepfer, D. D. (2009) Focal adhesion kinase: switching between GAPs and GEFs in the regulation of cell motility. Curr. Opin. Cell Biol. 21, 676-683
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 676-683
    • Tomar, A.1    Schlaepfer, D.D.2
  • 33
    • 10344236528 scopus 로고    scopus 로고
    • Thrombospondin induces RhoA inactivation through FAK-dependent signaling to stimulate focal adhesion disassembly
    • Orr, A. W., Pallero, M. A., Xiong, W. C., and Murphy-Ullrich, J. E. (2004) Thrombospondin induces RhoA inactivation through FAK-dependent signaling to stimulate focal adhesion disassembly. J. Biol. Chem. 279, 48983-48992
    • (2004) J. Biol. Chem. , vol.279 , pp. 48983-48992
    • Orr, A.W.1    Pallero, M.A.2    Xiong, W.C.3    Murphy-Ullrich, J.E.4
  • 34
    • 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
  • 35
    • 0037421205 scopus 로고    scopus 로고
    • PTP α regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration
    • Zeng, L., Si, X., Yu, W. P., Le, H. T., Ng, K. P., Teng, R. M., Ryan, K., Wang, D. Z., Ponniah, S., and Pallen, C. J. (2003) PTP α regulates integrin-stimulated FAK autophosphorylation and cytoskeletal rearrangement in cell spreading and migration. J. Cell Biol. 160, 137-146
    • (2003) J. Cell Biol. , vol.160 , pp. 137-146
    • Zeng, L.1    Si, X.2    Yu, W.P.3    Le, H.T.4    Ng, K.P.5    Teng, R.M.6    Ryan, K.7    Wang, D.Z.8    Ponniah, S.9    Pallen, C.J.10
  • 36
    • 77957372620 scopus 로고    scopus 로고
    • Akt phosphorylation of deleted in liver cancer 1 abrogates its suppression of liver cancer tumorigenesis and metastasis
    • Ko, F. C., Chan, L. K., Tung, E. K., Lowe, S. W., Ng, I. O., and Yam, J. W. (2010) Akt phosphorylation of deleted in liver cancer 1 abrogates its suppression of liver cancer tumorigenesis and metastasis. Gastroenterology 139, 1397-1407.e1396
    • (2010) Gastroenterology , vol.139 , pp. 1397.e1396-1407.e1396
    • Ko, F.C.1    Chan, L.K.2    Tung, E.K.3    Lowe, S.W.4    Ng, I.O.5    Yam, J.W.6
  • 37
    • 65949099133 scopus 로고    scopus 로고
    • Deleted in liver cancer 1 (DLC1) utilizes a novel binding site for Tensin2 PTB domain interaction and is required for tumor-suppressive function
    • Chan, L. K., Ko, F. C., Ng, I. O., and Yam, J. W. (2009) Deleted in liver cancer 1 (DLC1) utilizes a novel binding site for Tensin2 PTB domain interaction and is required for tumor-suppressive function. PLoS ONE 4, e5572
    • (2009) PLoS ONE , vol.4 , pp. e5572
    • Chan, L.K.1    Ko, F.C.2    Ng, I.O.3    Yam, J.W.4
  • 38
    • 84875897562 scopus 로고    scopus 로고
    • PKA-induced dimerization of the RhoGAP DLC1 promotes its inhibition of tumorigenesis and metastasis
    • Ko, F. C., Chan, L. K., Sze, K. M., Yeung, Y. S., Tse, E. Y., Lu, P., Yu, M. H., Ng, I. O., and Yam, J. W. (2013) PKA-induced dimerization of the RhoGAP DLC1 promotes its inhibition of tumorigenesis and metastasis. Nat. Commun. 4, 1618
    • (2013) Nat. Commun. , vol.4 , pp. 1618
    • Ko, F.C.1    Chan, L.K.2    Sze, K.M.3    Yeung, Y.S.4    Tse, E.Y.5    Lu, P.6    Yu, M.H.7    Ng, I.O.8    Yam, J.W.9
  • 41
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: In command and control of cell motility
    • Mitra, S. K., Hanson, D. A., and Schlaepfer, D. D. (2005) Focal adhesion kinase: in command and control of cell motility. Nat. Rev. Mol. Cell Biol. 6, 56-68
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 42
    • 0035949694 scopus 로고    scopus 로고
    • Focal adhesion kinase is involved in mechanosensing during fibroblast migration
    • Wang, H. B., Dembo, M., Hanks, S. K., and Wang, Y. (2001) Focal adhesion kinase is involved in mechanosensing during fibroblast migration. Proc. Natl. Acad. Sci. U.S.A. 98, 11295-11300
    • (2001) Proc. Natl. Acad. Sci. U.S.A. , vol.98 , pp. 11295-11300
    • Wang, H.B.1    Dembo, M.2    Hanks, S.K.3    Wang, Y.4
  • 44
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer, D. D., Mitra, S. K., and Ilic, D. (2004) Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 1692, 77-102
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.