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Volumn 287, Issue 17, 2012, Pages 13752-13760

RhoGDI SUMOylation at Lys-138 increases its binding activity to Rho GTPase and its inhibiting cancer cell motility

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN POLYMERIZATION; BINDING ACTIVITIES; BINDING AFFINITIES; CANCER CELLS; CELL MOTILITY; COMPLEX FORMATIONS; CYTOSKELETONS; GTPASES; SUMOYLATION; X-LINKED INHIBITOR OF APOPTOSIS;

EID: 84859950102     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M111.337469     Document Type: Article
Times cited : (63)

References (26)
  • 1
    • 0032860424 scopus 로고    scopus 로고
    • Regulation of the cytoskeleton and cell adhesion by the Rho family GTPases in mammalian cells
    • DOI 10.1146/annurev.biochem.68.1.459
    • 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 (Pubitemid 29449200)
    • (1999) Annual Review of Biochemistry , vol.68 , pp. 459-486
    • Kaibuchi, K.1    Kuroda, S.2    Amano, M.3
  • 2
    • 0033058184 scopus 로고    scopus 로고
    • Rho guanine dissociation inhibitors. Pivotal molecules in cellular signaling
    • Olofsson, B. (1999) Rho guanine dissociation inhibitors. Pivotal molecules in cellular signaling. Cell. Signal. 11, 545-554
    • (1999) Cell. Signal. , vol.11 , pp. 545-554
    • Olofsson, B.1
  • 3
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • DOI 10.1038/nature01148
    • Etienne-Manneville, S., and Hall, A. (2002) Rho GTPases in cell biology. Nature 420, 629-635 (Pubitemid 36764489)
    • (2002) Nature , vol.420 , Issue.6916 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 4
    • 23944518413 scopus 로고    scopus 로고
    • RhoGDI: Multiple functions in the regulation of Rho family GTPase activities
    • DOI 10.1042/BJ20050104
    • Dovas, A., and Couchman, J. R. (2005) RhoGDI. Multiple functions in the regulation of Rho family GTPase activities. Biochem. J. 390, 1-9 (Pubitemid 41192225)
    • (2005) Biochemical Journal , vol.390 , Issue.1 , pp. 1-9
    • Dovas, A.1    Couchman, J.R.2
  • 5
    • 0037081858 scopus 로고    scopus 로고
    • Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes
    • DOI 10.1042/0264-6021:3610243
    • Forget, M. A., Desrosiers, R. R., Gingras, D., and Béliveau, R. (2002) Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes. Biochem. J. 361, 243-254 (Pubitemid 34174491)
    • (2002) Biochemical Journal , vol.361 , Issue.2 , pp. 243-254
    • Forget, M.-A.1    Desrosiers, R.R.2    Gingras, D.3    Beliveau, R.4
  • 6
    • 1442290184 scopus 로고    scopus 로고
    • Epidermal growth factor-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase
    • Tu, S., Wu, W. J., Wang, J., and Cerione, R. A. (2003) Epidermal growth factor-dependent regulation of Cdc42 is mediated by the Src tyrosine kinase. J. Biol. Chem. 278, 49293-49300
    • (2003) J. Biol. Chem. , vol.278 , pp. 49293-49300
    • Tu, S.1    Wu, W.J.2    Wang, J.3    Cerione, R.A.4
  • 8
    • 33750522653 scopus 로고    scopus 로고
    • Phosphorylation of RhoGDI by Src regulates Rho GTPase binding and cytosol-membrane cycling
    • DOI 10.1091/mbc.E06-06-0533
    • DerMardirossian, C., Rocklin, G., Seo, J. Y., and Bokoch, G. M. (2006) Phosphorylation of RhoGDI by Src regulates Rho GTPase binding and cytosol-membrane cycling. Mol. Biol. Cell 17, 4760-4768 (Pubitemid 44665745)
    • (2006) Molecular Biology of the Cell , vol.17 , Issue.11 , pp. 4760-4768
    • DerMardirossian, C.1    Rocklin, G.2    Seo, J.-Y.3    Bokoch, G.M.4
  • 10
    • 79955538129 scopus 로고    scopus 로고
    • X-linked inhibitor of apoptosis protein (XIAP) mediates cancer cell motility via Rho GDP dissociation inhibitor (RhoGDI)-dependent regulation of the cytoskeleton
    • Liu, J., Zhang, D., Luo, W., Yu, Y., Yu, J., Li, J., Zhang, X., Zhang, B., Chen, J., Wu, X. R., Rosas-Acosta, G., and Huang, C. (2011) X-linked inhibitor of apoptosis protein (XIAP) mediates cancer cell motility via Rho GDP dissociation inhibitor (RhoGDI)-dependent regulation of the cytoskeleton. J. Biol. Chem. 286, 15630-15640
    • (2011) J. Biol. Chem. , vol.286 , pp. 15630-15640
    • Liu, J.1    Zhang, D.2    Luo, W.3    Yu, Y.4    Yu, J.5    Li, J.6    Zhang, X.7    Zhang, B.8    Chen, J.9    Wu, X.R.10    Rosas-Acosta, G.11    Huang, C.12
  • 11
    • 1542335506 scopus 로고    scopus 로고
    • Uncoupling of the Signaling and Caspase-inhibitory Properties of X-linked Inhibitor of Apoptosis
    • DOI 10.1074/jbc.M312891200
    • Lewis, J., Burstein, E., Reffey, S. B., Bratton, S. B., Roberts, A. B., and Duckett, C. S. (2004) Uncoupling of the signaling and caspase-inhibitory properties of X-linked inhibitor of apoptosis. J. Biol. Chem. 279, 9023-9029 (Pubitemid 38295965)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.10 , pp. 9023-9029
    • Lewis, J.1    Burstein, E.2    Reffey, S.B.3    Bratton, S.B.4    Roberts, A.B.5    Duckett, C.S.6
  • 12
    • 2342615480 scopus 로고    scopus 로고
    • X-Linked Inhibitor of Apoptosis Protein (XIAP) Is a Nonredundant Modulator of Tumor Necrosis Factor-Related Apoptosis-Inducing Ligand (TRAIL)-Mediated Apoptosis in Human Cancer Cells
    • DOI 10.1158/0008-5472.CAN-04-0046
    • Cummins, J. M., Kohli, M., Rago, C., Kinzler, K. W., Vogelstein, B., and Bunz, F. (2004) X-linked inhibitor of apoptosis protein (XIAP) is a nonredundant modulator of tumor necrosis factor-related apoptosis-inducing ligand (TRAIL)-mediated apoptosis in human cancer cells. Cancer Res. 64, 3006-3008 (Pubitemid 38581397)
    • (2004) Cancer Research , vol.64 , Issue.9 , pp. 3006-3008
    • Cummins, J.M.1    Kohli, M.2    Rago, C.3    Kinzler, K.W.4    Vogelstein, B.5    Bunz, F.6
  • 15
    • 33751221923 scopus 로고    scopus 로고
    • IKKβ programs to turn on the GADD45α-MKK4-JNK apoptotic cascade specifically via p50 NF-κB in arsenite response
    • DOI 10.1083/jcb.200602149
    • Song, L., Li, J., Zhang, D., Liu, Z. G., Ye, J., Zhan, Q., Shen, H. M., Whiteman, M., and Huang, C. (2006) IKKβ programs to turn on the GADD45α-MKK4-JNK apoptotic cascade specifically via p50 NF-κB in arsenite response. J. Cell Biol. 175, 607-617 (Pubitemid 44790614)
    • (2006) Journal of Cell Biology , vol.175 , Issue.4 , pp. 607-617
    • Song, L.1    Li, J.2    Zhang, D.3    Liu, Z.-G.4    Ye, J.5    Zhan, Q.6    Shen, H.-M.7    Whiteman, M.8    Huang, C.9
  • 16
    • 34147212027 scopus 로고    scopus 로고
    • p85α acts as a novel signal transducer for mediation of cellular apoptotic response to UV radiation
    • DOI 10.1128/MCB.00657-06
    • Song, L., Li, J., Ye, J., Yu, G., Ding, J., Zhang, D., Ouyang, W., Dong, Z., Kim, S. O., and Huang, C. (2007) p85α acts as a novel signal transducer for mediation of cellular apoptotic response to UV radiation. Mol. Cell. Biol. 27, 2713-2731 (Pubitemid 46581360)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.7 , pp. 2713-2731
    • Song, L.1    Li, J.2    Ye, J.3    Yu, G.4    Ding, J.5    Zhang, D.6    Ouyang, W.7    Dong, Z.8    Kim, S.O.9    Huang, C.10
  • 17
    • 14644402420 scopus 로고    scopus 로고
    • A universal stategy for proteomic studies of SUMO and other ubiquitin-like modifiers
    • DOI 10.1074/mcp.M400149-MCP200
    • Rosas-Acosta, G., Russell, W. K., Deyrieux, A., Russell, D. H., and Wilson, V. G. (2005) A universal strategy for proteomic studies of SUMO and other ubiquitin-like modifiers. Mol. Cell. Proteomics 4, 56-72 (Pubitemid 40309325)
    • (2005) Molecular and Cellular Proteomics , vol.4 , Issue.1 , pp. 56-72
    • Rosas-Acosta, G.1    Russell, W.K.2    Deyrieux, A.3    Russell, D.H.4    Wilson, V.G.5
  • 18
    • 73049115776 scopus 로고    scopus 로고
    • Identification of the nonstructural influenza A viral protein NS1A as a bona fide target of the small ubiquitin-like modifier by the use of dicistronic expression constructs
    • Pal, S., Rosas, J. M., and Rosas-Acosta, G. (2010) Identification of the nonstructural influenza A viral protein NS1A as a bona fide target of the small ubiquitin-like modifier by the use of dicistronic expression constructs. J. Virol. Methods 163, 498-504
    • (2010) J. Virol. Methods , vol.163 , pp. 498-504
    • Pal, S.1    Rosas, J.M.2    Rosas-Acosta, G.3
  • 19
    • 15944406765 scopus 로고    scopus 로고
    • SUMO. A history of modification
    • Hay, R. T. (2005) SUMO. A history of modification. Mol. Cell 18, 1-12
    • (2005) Mol. Cell , vol.18 , pp. 1-12
    • Hay, R.T.1
  • 20
    • 1342279419 scopus 로고    scopus 로고
    • SUMO modification of proteins other than transcription factors
    • Watts, F. Z. (2004) SUMO modification of proteins other than transcription factors. Semin. Cell Dev. Biol. 15, 211-220.
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 211-220
    • Watts, F.Z.1
  • 21
    • 33645801010 scopus 로고    scopus 로고
    • Wrestling with SUMO in a new arena
    • Wilson, V. G., and Rosas-Acosta, G. (2005) Wrestling with SUMO in a new arena. Sci. STKE 2005, pe32
    • (2005) Sci. STKE , vol.2005
    • Wilson, V.G.1    Rosas-Acosta, G.2
  • 23
  • 26
    • 4444301185 scopus 로고    scopus 로고
    • SUMO and ubiquitin in the nucleus. Differnt functions, similar mechanisms?
    • Gill, G. (2004) SUMO and ubiquitin in the nucleus. Different functions, similar mechanisms? Genes Dev. 18, 2046-2059
    • (2004) Genes Dev. , vol.18 , pp. 2046-2059
    • Gill, G.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.