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Volumn 5, Issue , 2014, Pages

Spatial control of Cdc42 signalling by a GM130-RasGRF complex regulates polarity and tumorigenesis

Author keywords

[No Author keywords available]

Indexed keywords

GOLGI MATRIX PROTEIN 130; GUANINE NUCLEOTIDE EXCHANGE FACTOR; PROTEIN; PROTEIN CDC42; RAS PROTEIN; SMALL INTERFERING RNA; UNCLASSIFIED DRUG; UVOMORULIN; AUTOANTIGEN; CADHERIN; CDH1 PROTEIN, HUMAN; GOLGIN SUBFAMILY A MEMBER 2; MEMBRANE PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE 3; RASGRF1 PROTEIN, HUMAN; RASGRF2 PROTEIN, HUMAN; RHO GUANINE NUCLEOTIDE EXCHANGE FACTOR;

EID: 84923250091     PISSN: None     EISSN: 20411723     Source Type: Journal    
DOI: 10.1038/ncomms5839     Document Type: Article
Times cited : (77)

References (41)
  • 1
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42 - The centre of polarity
    • Etienne-Manneville, S. Cdc42 - the centre of polarity. J. Cell Sci. 117, 1291-1300 (2004).
    • (2004) J. Cell Sci. , vol.117 , pp. 1291-1300
    • Etienne-Manneville, S.1
  • 2
    • 84866037962 scopus 로고    scopus 로고
    • Tumour type-dependent function of the Par3 polarity protein in skin tumorigenesis
    • Iden, S. et al. Tumour type-dependent function of the Par3 polarity protein in skin tumorigenesis. Cancer Cell 22, 389-403 (2012).
    • (2012) Cancer Cell , vol.22 , pp. 389-403
    • Iden, S.1
  • 3
    • 84869000970 scopus 로고    scopus 로고
    • Loss of the Par3 polarity protein promotes breast tumorigenesis and metastasis
    • McCaffrey
    • McCaffrey, Luke M., Montalbano, J., Mihai, C. & Macara, Ian G. Loss of the Par3 polarity protein promotes breast tumorigenesis and metastasis. Cancer Cell 22, 601-614 (2012).
    • (2012) Cancer Cell , vol.22 , pp. 601-614
    • Luke, M.1    Montalbano, J.2    Mihai, C.3    Macara, I.G.4
  • 4
    • 84873410310 scopus 로고    scopus 로고
    • Loss of Par3 promotes breast cancer metastasis by compromising cell-cell cohesion
    • Xue, B., Krishnamurthy, K., Allred, D. C. & Muthuswamy, S. K. Loss of Par3 promotes breast cancer metastasis by compromising cell-cell cohesion. Nat. Cell Biol. 15, 189-200 (2012).
    • (2012) Nat. Cell Biol. , vol.15 , pp. 189-200
    • Xue, B.1    Krishnamurthy, K.2    Allred, D.C.3    Muthuswamy, S.K.4
  • 5
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian Cdc42 is a brefeldin a-sensitive component of the Golgi apparatus
    • Erickson, J. W., Zhang, C.-j., Kahn, R. A., Evans, T. & Cerione, R. A. Mammalian Cdc42 is a brefeldin a-sensitive component of the Golgi apparatus. J. Biol. Chem. 271, 26850-26854 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 26850-26854
    • Erickson, J.W.1    Zhang, C.-J.2    Kahn, R.A.3    Evans, T.4    Cerione, R.A.5
  • 6
    • 4644266043 scopus 로고    scopus 로고
    • Activation of endogenous Cdc42 visualized in living cells
    • Nalbant, P., Hodgson, L., Kraynov, V., Toutchkine, A. & Hahn, K. M. Activation of endogenous Cdc42 visualized in living cells. Science 305, 1615-1619 (2004).
    • (2004) Science , vol.305 , pp. 1615-1619
    • Nalbant, P.1    Hodgson, L.2    Kraynov, V.3    Toutchkine, A.4    Hahn, K.M.5
  • 7
    • 79251585226 scopus 로고    scopus 로고
    • Signalling to and from the secretory pathway
    • Farhan, H. & Rabouille, C. Signalling to and from the secretory pathway. J. Cell Sci. 124, 171-180 (2011).
    • (2011) J. Cell Sci. , vol.124 , pp. 171-180
    • Farhan, H.1    Rabouille, C.2
  • 8
    • 65249115901 scopus 로고    scopus 로고
    • A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing
    • Yadav, S., Puri, S. & Linstedt, A. D. A primary role for Golgi positioning in directed secretion, cell polarity, and wound healing. Mol. Biol. Cell 20, 1728-1736 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1728-1736
    • Yadav, S.1    Puri, S.2    Linstedt, A.D.3
  • 9
    • 0029098537 scopus 로고
    • Calcium activation of Ras mediated by neuronal exchange factor Ras-GRF
    • Farnsworth, C. L. et al. Calcium activation of Ras mediated by neuronal exchange factor Ras-GRF. Nature 376, 524-527 (1995).
    • (1995) Nature , vol.376 , pp. 524-527
    • Farnsworth, C.L.1
  • 10
    • 78651379505 scopus 로고    scopus 로고
    • The RasGrf family of mammalian guanine nucleotide exchange factors
    • Fernández-Medarde, A. & Santos, E. The RasGrf family of mammalian guanine nucleotide exchange factors. Biochim. Biophys. Acta 1815, 170-188 (2011).
    • (2011) Biochim. Biophys. Acta , vol.1815 , pp. 170-188
    • Fernández-Medarde, A.1    Santos, E.2
  • 11
    • 0034714244 scopus 로고    scopus 로고
    • The Rho family GTPase Cdc42 regulates the activation of Ras/MAP kinase by the exchange factor Ras-GRF
    • Arozarena, I. et al. The Rho family GTPase Cdc42 regulates the activation of Ras/MAP kinase by the exchange factor Ras-GRF. J. Biol. Chem. 275, 26441-26448 (2000).
    • (2000) J. Biol. Chem. , vol.275 , pp. 26441-26448
    • Arozarena, I.1
  • 12
    • 0035877781 scopus 로고    scopus 로고
    • Maintenance of Cdc42 GDP-bound state by Rho-GDI inhibits MAP kinase activation by the exchange factor Ras-GRF: Evidence for Ras-GRF function being inhibited by Cdc42-GDP but unaffected by Cdc42-GTP
    • Arozarena, I., Matallanas, D. & Crespo, P. Maintenance of Cdc42 GDP-bound state by Rho-GDI inhibits MAP kinase activation by the exchange factor Ras-GRF: evidence for Ras-GRF function being inhibited by Cdc42-GDP but unaffected by Cdc42-GTP. J. Biol. Chem. 276, 21878-21884 (2001).
    • (2001) J. Biol. Chem. , vol.276 , pp. 21878-21884
    • Arozarena, I.1    Matallanas, D.2    Crespo, P.3
  • 13
    • 79959976109 scopus 로고    scopus 로고
    • RasGRF suppresses Cdc42-mediated tumour cell movement, cytoskeletal dynamics and transformation
    • Calvo, F. et al. RasGRF suppresses Cdc42-mediated tumour cell movement, cytoskeletal dynamics and transformation. Nat. Cell Biol. 13, 819-826 (2011).
    • (2011) Nat. Cell Biol. , vol.13 , pp. 819-826
    • Calvo, F.1
  • 14
    • 0036724188 scopus 로고    scopus 로고
    • Activation of Rac and Cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells
    • Itoh, R. E. et al. Activation of Rac and Cdc42 video imaged by fluorescent resonance energy transfer-based single-molecule probes in the membrane of living cells. Mol. Cell Biol. 22, 6582-6591 (2002).
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1
  • 15
    • 0042672950 scopus 로고    scopus 로고
    • Activity of Rho-family GTPases during cell division as visualized with FRET-based probes
    • Yoshizaki, H. et al. Activity of Rho-family GTPases during cell division as visualized with FRET-based probes. J. Cell Biol. 162, 223-232 (2003).
    • (2003) J. Cell Biol. , vol.162 , pp. 223-232
    • Yoshizaki, H.1
  • 16
    • 64149084265 scopus 로고    scopus 로고
    • GM130-dependent control of Cdc42 activity at the golgi regulates centrosome organization
    • Kodani, A., Kristensen, I., Huang, L. & Sütterlin, C. GM130-dependent control of Cdc42 activity at the golgi regulates centrosome organization. Mol. Biol. Cell 20, 1192-1200 (2009).
    • (2009) Mol. Biol. Cell , vol.20 , pp. 1192-1200
    • Kodani, A.1    Kristensen, I.2    Huang, L.3    Sütterlin, C.4
  • 17
    • 79953293527 scopus 로고    scopus 로고
    • Par6B and atypical PKC regulate mitotic spindle orientation during epithelial morphogenesis
    • Durgan, J., Kaji, N., Jin, D. & Hall, A. Par6B and atypical PKC regulate mitotic spindle orientation during epithelial morphogenesis. J. Biol. Chem. 286, 12461-12474 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 12461-12474
    • Durgan, J.1    Kaji, N.2    Jin, D.3    Hall, A.4
  • 18
    • 58149191544 scopus 로고    scopus 로고
    • Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis
    • Jaffe, A. B., Kaji, N., Durgan, J. & Hall, A. Cdc42 controls spindle orientation to position the apical surface during epithelial morphogenesis. J. Cell Biol. 183, 625-633 (2008).
    • (2008) J. Cell Biol. , vol.183 , pp. 625-633
    • Jaffe, A.B.1    Kaji, N.2    Durgan, J.3    Hall, A.4
  • 19
    • 84887519097 scopus 로고    scopus 로고
    • Microtubules that form the stationary lattice of muscle fibers are dynamic and nucleated at Golgi elements
    • Oddoux, S. et al. Microtubules that form the stationary lattice of muscle fibers are dynamic and nucleated at Golgi elements. J. Cell Biol. 203, 205-213 (2013).
    • (2013) J. Cell Biol. , vol.203 , pp. 205-213
    • Oddoux, S.1
  • 20
    • 0020804564 scopus 로고
    • Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation
    • Matlin, K. S. & Simons, K. Reduced temperature prevents transfer of a membrane glycoprotein to the cell surface but does not prevent terminal glycosylation. Cell 34, 233-243 (1983).
    • (1983) Cell , vol.34 , pp. 233-243
    • Matlin, K.S.1    Simons, K.2
  • 21
    • 19644377230 scopus 로고    scopus 로고
    • Polarized trafficking of E-cadherin is regulated by Rac1 and Cdc42 in Madin-Darby canine kidney cells
    • Wang, B., Wylie, F. G., Teasdale, R. D. & Stow, J. L. Polarized trafficking of E-cadherin is regulated by Rac1 and Cdc42 in Madin-Darby canine kidney cells. Am. J. Physiol. Cell Physiol. 288, C1411-C1419 (2005).
    • (2005) Am. J. Physiol. Cell Physiol. , vol.288 , pp. C1411-C1419
    • Wang, B.1    Wylie, F.G.2    Teasdale, R.D.3    Stow, J.L.4
  • 22
    • 33746863655 scopus 로고    scopus 로고
    • Tuba stimulates intracellular N-WASP-dependent actin assembly
    • Kovacs, E. M., Makar, R. S. & Gertler, F. B. Tuba stimulates intracellular N-WASP-dependent actin assembly. J. Cell Sci. 119, 2715-2726 (2006).
    • (2006) J. Cell Sci. , vol.119 , pp. 2715-2726
    • Kovacs, E.M.1    Makar, R.S.2    Gertler, F.B.3
  • 23
    • 1542677037 scopus 로고    scopus 로고
    • Tuba, a novel protein containing Bin/Amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton
    • Salazar, M. A. et al. Tuba, a novel protein containing Bin/Amphiphysin/Rvs and Dbl homology domains, links dynamin to regulation of the actin cytoskeleton. J. Biol. Chem. 278, 49031-49043 (2003).
    • (2003) J. Biol. Chem. , vol.278 , pp. 49031-49043
    • Salazar, M.A.1
  • 24
    • 0842304220 scopus 로고    scopus 로고
    • Activation of H-Ras in the endoplasmic reticulum by the RasGRF family guanine nucleotide exchange factors
    • Arozarena, I. et al. Activation of H-Ras in the endoplasmic reticulum by the RasGRF family guanine nucleotide exchange factors. Mol. Cell Biol. 24, 1516-1530 (2004).
    • (2004) Mol. Cell Biol. , vol.24 , pp. 1516-1530
    • Arozarena, I.1
  • 26
    • 84887273608 scopus 로고    scopus 로고
    • Epithelial plasticity: A common theme in embryonic and cancer cells
    • Nieto, M. A. Epithelial plasticity: a common theme in embryonic and cancer cells. Science 342, 1234850 (2013).
    • (2013) Science , vol.342 , pp. 1234850
    • Nieto, M.A.1
  • 27
    • 0020316410 scopus 로고
    • Polarization of the Golgi apparatus and the microtubule-organizing center in cultured fibroblasts at the edge of an experimental wound
    • Kupfer, A., Louvard, D. & Singer, S. J. Polarization of the Golgi apparatus and the microtubule-organizing center in cultured fibroblasts at the edge of an experimental wound. PNAS 79, 2603-2607 (1982).
    • (1982) PNAS , vol.79 , pp. 2603-2607
    • Kupfer, A.1    Louvard, D.2    Singer, S.J.3
  • 28
    • 39449124362 scopus 로고    scopus 로고
    • The Golgi protein GM130 regulates centrosome morphology and function
    • Kodani, A. & Sütterlin, C. The Golgi protein GM130 regulates centrosome morphology and function. Mol. Biol. Cell 19, 745-753 (2008).
    • (2008) Mol. Biol. Cell , vol.19 , pp. 745-753
    • Kodani, A.1    Sütterlin, C.2
  • 29
    • 84863205689 scopus 로고    scopus 로고
    • Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway
    • Simpson, J. C. et al. Genome-wide RNAi screening identifies human proteins with a regulatory function in the early secretory pathway. Nat. Cell Biol. 14, 764-774 (2012).
    • (2012) Nat. Cell Biol. , vol.14 , pp. 764-774
    • Simpson, J.C.1
  • 30
    • 43749087389 scopus 로고    scopus 로고
    • Coordination of Golgin tethering and SNARE assembly: GM130 binds syntaxin 5 in a p115-regulated manner
    • Diao, A., Frost, L., Morohashi, Y. & Lowe, M. Coordination of Golgin tethering and SNARE assembly: GM130 binds syntaxin 5 in a p115-regulated manner. J. Biol. Chem. 283, 6957-6967 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 6957-6967
    • Diao, A.1    Frost, L.2    Morohashi, Y.3    Lowe, M.4
  • 31
    • 34248176800 scopus 로고    scopus 로고
    • The biogenesis of the Golgi ribbon: The roles of membrane input from the ER and of GM130
    • Marra, P. et al. The biogenesis of the Golgi ribbon: the roles of membrane input from the ER and of GM130. Mol. Biol. Cell 18, 1595-1608 (2007).
    • (2007) Mol. Biol. Cell , vol.18 , pp. 1595-1608
    • Marra, P.1
  • 32
    • 33644756640 scopus 로고    scopus 로고
    • GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution
    • Puthenveedu, M. A., Bachert, C., Puri, S., Lanni, F. & Linstedt, A. D. GM130 and GRASP65-dependent lateral cisternal fusion allows uniform Golgi-enzyme distribution. Nat. Cell Biol. 8, 238-248 (2006).
    • (2006) Nat. Cell Biol. , vol.8 , pp. 238-248
    • Puthenveedu, M.A.1    Bachert, C.2    Puri, S.3    Lanni, F.4    Linstedt, A.D.5
  • 33
    • 78650719288 scopus 로고    scopus 로고
    • Cdc42 localization and cell polarity depend on membrane traffic
    • Osmani, N., Peglion, F., Chavrier, P. & Etienne-Manneville, S. Cdc42 localization and cell polarity depend on membrane traffic. J. Cell Biol. 191, 1261-1269 (2010).
    • (2010) J. Cell Biol. , vol.191 , pp. 1261-1269
    • Osmani, N.1    Peglion, F.2    Chavrier, P.3    Etienne-Manneville, S.4
  • 34
    • 17344369066 scopus 로고    scopus 로고
    • Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics
    • Dubois, T. et al. Golgi-localized GAP for Cdc42 functions downstream of ARF1 to control Arp2/3 complex and F-actin dynamics. Nat. Cell Biol. 7, 353-364 (2005).
    • (2005) Nat. Cell Biol. , vol.7 , pp. 353-364
    • Dubois, T.1
  • 35
    • 84873497475 scopus 로고    scopus 로고
    • Computational analysis of Rho GTPase cycling
    • Falkenberg, C. V. & Loew, L. M. Computational analysis of Rho GTPase cycling. PLoS Comput. Biol. 9, e1002831 (2013).
    • (2013) PLoS Comput. Biol. , vol.9 , pp. e1002831
    • Falkenberg, C.V.1    Loew, L.M.2
  • 36
    • 56349125826 scopus 로고    scopus 로고
    • Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex
    • Kozubowski, L. et al. Symmetry-breaking polarization driven by a Cdc42p GEF-PAK complex. Curr. Biol. 18, 1719-1726 (2008).
    • (2008) Curr. Biol. , vol.18 , pp. 1719-1726
    • Kozubowski, L.1
  • 37
    • 79651475078 scopus 로고    scopus 로고
    • Modeling vesicle traffic reveals unexpected consequences for Cdc42p-mediated polarity establishment
    • Layton, A. T. et al. Modeling vesicle traffic reveals unexpected consequences for Cdc42p-mediated polarity establishment. Curr. Biol. 21, 184-194 (2011).
    • (2011) Curr. Biol. , vol.21 , pp. 184-194
    • Layton, A.T.1
  • 38
  • 39
    • 84860355037 scopus 로고    scopus 로고
    • Synchronization of secretory protein traffic in populations of cells
    • Boncompain, G. et al. Synchronization of secretory protein traffic in populations of cells. Nat. Methods 9, 493-498 (2012).
    • (2012) Nat. Methods , vol.9 , pp. 493-498
    • Boncompain, G.1
  • 40
    • 84859173050 scopus 로고    scopus 로고
    • Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%
    • Goedhart, J. et al. Structure-guided evolution of cyan fluorescent proteins towards a quantum yield of 93%. Nat. Commun. 3, 751 (2012).
    • (2012) Nat. Commun. , vol.3 , pp. 751
    • Goedhart, J.1
  • 41
    • 37549066863 scopus 로고    scopus 로고
    • Discovery of epigenetically silenced genes by methylated DNA immunoprecipitation in colon cancer cells
    • Jacinto, F. V., Ballestar, E., Ropero, S. & Esteller, M. Discovery of epigenetically silenced genes by methylated DNA immunoprecipitation in colon cancer cells. Cancer Res. 67, 11481-11486 (2007).
    • (2007) Cancer Res. , vol.67 , pp. 11481-11486
    • Jacinto, F.V.1    Ballestar, E.2    Ropero, S.3    Esteller, M.4


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