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Volumn 14, Issue 4, 2013, Pages 7089-7108

Roles of Rho GTPases in intracellular transport and cellular transformation

Author keywords

Actin cytoskeleton; Cellular transformation; Rho GTPases; Vesicle trafficking; Viral transport

Indexed keywords

ACTIN RELATED PROTEIN 2-3 COMPLEX; IQ MOTIF CONTAINING GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN 1; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PHOSPHOLIPASE D1; PROTEIN CDC42; RAC1 PROTEIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; RHOA GUANINE NUCLEOTIDE BINDING PROTEIN; SYNAPTOJANIN; SYNAPTOJANIN 2; UNCLASSIFIED DRUG; VIRUS PROTEIN;

EID: 84876004101     PISSN: 16616596     EISSN: 14220067     Source Type: Journal    
DOI: 10.3390/ijms14047089     Document Type: Review
Times cited : (94)

References (132)
  • 1
    • 50149083752 scopus 로고    scopus 로고
    • Mammalian Rho GTPases: New insights into their functions from in vivo studies
    • Heasman, S.J.; Ridley, A.J. Mammalian Rho GTPases: New insights into their functions from in vivo studies. Nat. Rev. Mol. Cell Biol. 2008, 9, 690-701.
    • (2008) Nat. Rev. Mol. Cell Biol. , vol.9 , pp. 690-701
    • Heasman, S.J.1    Ridley, A.J.2
  • 2
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. Rho GTPases and the actin cytoskeleton. Science 1998, 279, 509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 3
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N.; Hall, A. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 1997, 9, 86-92.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 4
    • 0027732538 scopus 로고
    • Proteins regulating Ras and its relatives
    • Boguski, M.S.; McCormick, F. Proteins regulating Ras and its relatives. Nature 1993, 366, 643-654.
    • (1993) Nature , vol.366 , pp. 643-654
    • Boguski, M.S.1    McCormick, F.2
  • 5
    • 0034308228 scopus 로고    scopus 로고
    • Rho family GTPases: More than simple switches
    • Symons, M.; Settleman, J. Rho family GTPases: More than simple switches. Trends Cell Biol. 2000, 10, 415-419.
    • (2000) Trends Cell Biol. , vol.10 , pp. 415-419
    • Symons, M.1    Settleman, J.2
  • 6
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe, A.B.; Hall, A. Rho GTPases: Biochemistry and biology. Annu. Rev. Cell Dev. Biol. 2005, 21, 247-269.
    • (2005) Annu. Rev. Cell Dev. Biol. , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 7
    • 0038056187 scopus 로고    scopus 로고
    • Control of vesicular trafficking by Rho GTPases
    • Symons, M.; Rusk, N. Control of vesicular trafficking by Rho GTPases. Curr. Biol. 2003, 13, 409-418.
    • (2003) Curr. Biol. , vol.13 , pp. 409-418
    • Symons, M.1    Rusk, N.2
  • 8
    • 49849098669 scopus 로고    scopus 로고
    • The ghost in the machine: Small GTPases as spatial regulators of exocytosis
    • Wu, H.; Rossi, G.; Brennwald, P. The ghost in the machine: small GTPases as spatial regulators of exocytosis. Trends Cell Biol. 2008, 18, 397-404.
    • (2008) Trends Cell Biol. , vol.18 , pp. 397-404
    • Wu, H.1    Rossi, G.2    Brennwald, P.3
  • 9
    • 84866418051 scopus 로고    scopus 로고
    • Topological and functional properties of the small GTPases protein interaction network
    • Delprato, A. Topological and functional properties of the small GTPases protein interaction network. PLoS One 2012, 7, e44882.
    • (2012) PLoS One , vol.7
    • Delprato, A.1
  • 13
    • 33845699085 scopus 로고    scopus 로고
    • Actin regulation in endocytosis
    • Smythe, E.; Ayscough, K.R. Actin regulation in endocytosis. J. Cell Sci. 2006, 119, 4589-4598.
    • (2006) J. Cell Sci. , vol.119 , pp. 4589-4598
    • Smythe, E.1    Ayscough, K.R.2
  • 14
    • 34547959158 scopus 로고    scopus 로고
    • Actin in membrane trafficking
    • Lanzetti, L. Actin in membrane trafficking. Curr. Opin. Cell Biol. 2007, 19, 453-458.
    • (2007) Curr. Opin. Cell Biol. , vol.19 , pp. 453-458
    • Lanzetti, L.1
  • 15
    • 3242671847 scopus 로고    scopus 로고
    • Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex
    • Ho, H.Y.H.; Rohatgi, R.; Lebensohn, A.M.; Li, J.; Gygi, S.P.; Kirschner, M.W. Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 2004, 118, 203-216.
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.H.1    Rohatgi, R.2    Lebensohn, A.M.3    Li, J.4    Gygi, S.P.5    Kirschner, M.W.6
  • 17
    • 1442274703 scopus 로고    scopus 로고
    • Cdc42: New roads to travel
    • Cerione, R.A. Cdc42: New roads to travel. Trends Cell Biol. 2004, 14, 127-132.
    • (2004) Trends Cell Biol. , vol.14 , pp. 127-132
    • Cerione, R.A.1
  • 18
    • 33751252276 scopus 로고    scopus 로고
    • Cancer metastasis: Building a framework
    • Gupta, G.P.; Massagué, J. Cancer metastasis: Building a framework. Cell 2006, 127, 679-695.
    • (2006) Cell , vol.127 , pp. 679-695
    • Gupta, G.P.1    Massagué, J.2
  • 19
    • 0034997092 scopus 로고    scopus 로고
    • Rho proteins: Linking signaling with membrane trafficking
    • Ridley, A.J. Rho proteins: linking signaling with membrane trafficking. Traffic 2001, 2, 303-310.
    • (2001) Traffic , vol.2 , pp. 303-310
    • Ridley, A.J.1
  • 20
    • 44449178868 scopus 로고    scopus 로고
    • Rho GTPases in cancer cell biology
    • Vega, F.M.; Ridley, A.J. Rho GTPases in cancer cell biology. FEBS Lett. 2008, 582, 2093-2101.
    • (2008) FEBS Lett. , vol.582 , pp. 2093-2101
    • Vega, F.M.1    Ridley, A.J.2
  • 21
    • 33748994545 scopus 로고    scopus 로고
    • Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking
    • Ridley, A.J. Rho GTPases and actin dynamics in membrane protrusions and vesicle trafficking. Trends Cell Biol. 2006, 16, 522-529.
    • (2006) Trends Cell Biol. , vol.16 , pp. 522-529
    • Ridley, A.J.1
  • 22
    • 67349209489 scopus 로고    scopus 로고
    • MyoGEF regulates the invasion activity of MDA-MB-231 breast cancer cells through activation of RhoA and RhoC
    • Wu, D.; Asiedu, M.; Wei, Q. MyoGEF regulates the invasion activity of MDA-MB-231 breast cancer cells through activation of RhoA and RhoC. Oncogene 2009, 28, 2219-2230.
    • (2009) Oncogene , vol.28 , pp. 2219-2230
    • Wu, D.1    Asiedu, M.2    Wei, Q.3
  • 23
    • 77957832252 scopus 로고    scopus 로고
    • The function of two Rho family GTPases is determined by distinct patterns of cell surface localization
    • Wu, H.; Brennwald, P. The function of two Rho family GTPases is determined by distinct patterns of cell surface localization. Mol. Cell. Biol. 2010, 30, 5207-5217.
    • (2010) Mol. Cell. Biol. , vol.30 , pp. 5207-5217
    • Wu, H.1    Brennwald, P.2
  • 24
    • 0032740682 scopus 로고    scopus 로고
    • The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity
    • Adamo, J.E.; Rossi, G.; Brennwald, P. The Rho GTPase Rho3 has a direct role in exocytosis that is distinct from its role in actin polarity. Mol. Biol. Cell. 1999, 10, 4121-4133.
    • (1999) Mol. Biol. Cell. , vol.10 , pp. 4121-4133
    • Adamo, J.E.1    Rossi, G.2    Brennwald, P.3
  • 26
    • 13544273548 scopus 로고    scopus 로고
    • Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10
    • Cheng, J.; Wang, H.; Guggino, W.B. Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10. J. Biol. Chem. 2005, 280, 3731-3739.
    • (2005) J. Biol. Chem. , vol.280 , pp. 3731-3739
    • Cheng, J.1    Wang, H.2    Guggino, W.B.3
  • 27
    • 57349129589 scopus 로고    scopus 로고
    • Primary granule exocytosis in human neutrophils is regulated by Rac-dependent actin remodeling
    • Mitchell, T.; Lo, A.; Logan, M.R.; Lacy, P.; Eitzen, G. Primary granule exocytosis in human neutrophils is regulated by Rac-dependent actin remodeling. Am. J. Physiol. Cell Physiol. 2008, 295, 1354-1365.
    • (2008) Am. J. Physiol. Cell Physiol. , vol.295 , pp. 1354-1365
    • Mitchell, T.1    Lo, A.2    Logan, M.R.3    Lacy, P.4    Eitzen, G.5
  • 29
    • 70450222906 scopus 로고    scopus 로고
    • Rif proteins take to the RhoD: Rho GTPases at the crossroads of actin dynamics and membrane trafficking
    • Gad, A.K.B.; Aspenström, P. Rif proteins take to the RhoD: Rho GTPases at the crossroads of actin dynamics and membrane trafficking. Cell. Signal. 2010, 22, 183-189.
    • (2010) Cell. Signal. , vol.22 , pp. 183-189
    • Gad, A.K.B.1    Aspenström, P.2
  • 30
    • 34250820511 scopus 로고    scopus 로고
    • RhoB-dependent modulation of postendocytic traffic in polarized Madin-Darby canine kidney cells
    • Rondanino, C.; Rojas, R.; Ruiz, W.G.; Wang, E.; Hughey, R.P.; Dunn, K.W.; Apodaca, G. RhoB-dependent modulation of postendocytic traffic in polarized Madin-Darby canine kidney cells. Traffic 2007, 8, 932-949.
    • (2007) Traffic , vol.8 , pp. 932-949
    • Rondanino, C.1    Rojas, R.2    Ruiz, W.G.3    Wang, E.4    Hughey, R.P.5    Dunn, K.W.6    Apodaca, G.7
  • 31
    • 4344619948 scopus 로고    scopus 로고
    • Farnesyltransferase inhibitors disrupt EGF receptor traffic through modulation of the RhoB GTPase
    • Wherlock, M.; Gampel, A.; Futter, C.; Mellor, H. Farnesyltransferase inhibitors disrupt EGF receptor traffic through modulation of the RhoB GTPase. J. Cell Sci. 2004, 117, 3221-3231.
    • (2004) J. Cell Sci. , vol.117 , pp. 3221-3231
    • Wherlock, M.1    Gampel, A.2    Futter, C.3    Mellor, H.4
  • 34
    • 51649127581 scopus 로고    scopus 로고
    • Increased Rac1b expression sustains colorectal tumor cell survival
    • Matos, P.; Jordan, P. Increased Rac1b expression sustains colorectal tumor cell survival. Mol. Cancer Res. 2008, 6, 1178-1184.
    • (2008) Mol. Cancer Res. , vol.6 , pp. 1178-1184
    • Matos, P.1    Jordan, P.2
  • 35
    • 11244313840 scopus 로고    scopus 로고
    • Rac1b, a tumor associated, constitutively active Rac1 splice variant, promotes cellular transformation
    • Singh, A.; Karnoub, A.E.; Palmby, T.R.; Lengyel, E.; Sondek, J.; Der, C.J. Rac1b, a tumor associated, constitutively active Rac1 splice variant, promotes cellular transformation. Oncogene 2004, 23, 9369-9380.
    • (2004) Oncogene , vol.23 , pp. 9369-9380
    • Singh, A.1    Karnoub, A.E.2    Palmby, T.R.3    Lengyel, E.4    Sondek, J.5    Der, C.J.6
  • 36
    • 0015954720 scopus 로고
    • Genetic control of the cell division cycle in yeast
    • Hartwell, L.H.; Culotti, J.; Pringle, J.R.; Reid, B.J. Genetic control of the cell division cycle in yeast. Science 1974, 183, 46-51.
    • (1974) Science , vol.183 , pp. 46-51
    • Hartwell, L.H.1    Culotti, J.2    Pringle, J.R.3    Reid, B.J.4
  • 37
    • 0025363198 scopus 로고
    • Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity
    • Johnson, D.I.; Pringle, J.R. Molecular characterization of CDC42, a Saccharomyces cerevisiae gene involved in the development of cell polarity. J. Cell Biol. 1990, 111, 143-152.
    • (1990) J. Cell Biol. , vol.111 , pp. 143-152
    • Johnson, D.I.1    Pringle, J.R.2
  • 38
    • 0033126052 scopus 로고    scopus 로고
    • Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells
    • Kroschewski, R.; Hall, A.; Mellman, I. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat. Cell Biol. 1999, 1, 8-13.
    • (1999) Nat. Cell Biol. , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 39
    • 0033983938 scopus 로고    scopus 로고
    • Regulation of endocytic traffic by Rho family GTPases
    • Ellis, S.; Mellor, H. Regulation of endocytic traffic by Rho family GTPases. Trends Cell Biol. 2000, 10, 85-88.
    • (2000) Trends Cell Biol. , vol.10 , pp. 85-88
    • Ellis, S.1    Mellor, H.2
  • 41
    • 0036232040 scopus 로고    scopus 로고
    • GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway
    • Sabharanjak, S.; Sharma, P.; Parton, R.G.; Mayor, S. GPI-anchored proteins are delivered to recycling endosomes via a distinct cdc42-regulated, clathrin-independent pinocytic pathway. Dev. Cell 2002, 2, 411-423.
    • (2002) Dev. Cell , vol.2 , pp. 411-423
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 42
    • 34249090252 scopus 로고    scopus 로고
    • Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway
    • Chadda, R.; Howes, M.T.; Plowman, S.J.; Hancock, J.F.; Parton, R.G.; Mayor, S. Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway. Traffic 2007, 8, 702-717.
    • (2007) Traffic , vol.8 , pp. 702-717
    • Chadda, R.1    Howes, M.T.2    Plowman, S.J.3    Hancock, J.F.4    Parton, R.G.5    Mayor, S.6
  • 43
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis
    • Mayor, S.; Pagano, R.E. Pathways of clathrin-independent endocytosis. Nat. Rev. Mol. Cell Biol. 2007, 8, 603-612.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 603-612
    • Mayor, S.1    Pagano, R.E.2
  • 44
    • 0038392873 scopus 로고    scopus 로고
    • Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP
    • Cory, G.O.C.; Cramer, R.; Blanchoin, L.; Ridley, A.J. Phosphorylation of the WASP-VCA domain increases its affinity for the Arp2/3 complex and enhances actin polymerization by WASP. Mol. Cell 2003, 11, 1229-1239.
    • (2003) Mol. Cell , vol.11 , pp. 1229-1239
    • Cory, G.O.C.1    Cramer, R.2    Blanchoin, L.3    Ridley, A.J.4
  • 45
    • 77957916873 scopus 로고    scopus 로고
    • Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: Implications for endocytosis
    • Bu, W.; Lim, K.B.; Yu, Y.H.; Chou, A.M.; Sudhaharan, T.; Ahmed, S. Cdc42 interaction with N-WASP and Toca-1 regulates membrane tubulation, vesicle formation and vesicle motility: implications for endocytosis. PLoS One 2010, 5, e12153.
    • (2010) PLoS One , vol.5
    • Bu, W.1    Lim, K.B.2    Yu, Y.H.3    Chou, A.M.4    Sudhaharan, T.5    Ahmed, S.6
  • 46
    • 0001264854 scopus 로고    scopus 로고
    • The γ-subunit of the coatomer complex binds Cdc42 to mediate transformation
    • Wu, W.J.; Erickson, J.W.; Lin, R.; Cerione, R.A. The γ-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 2000, 405, 800-804.
    • (2000) Nature , vol.405 , pp. 800-804
    • Wu, W.J.1    Erickson, J.W.2    Lin, R.3    Cerione, R.A.4
  • 48
    • 70350111046 scopus 로고    scopus 로고
    • Retrograde Shiga toxin trafficking is regulated by ARHGAP21 and Cdc42
    • Hehnly, H.; Longhini, K.M.; Chen, J.L.; Stamnes, M. Retrograde Shiga toxin trafficking is regulated by ARHGAP21 and Cdc42. Mol. Biol. Cell. 2009, 20, 4303-4312.
    • (2009) Mol. Biol. Cell. , vol.20 , pp. 4303-4312
    • Hehnly, H.1    Longhini, K.M.2    Chen, J.L.3    Stamnes, M.4
  • 50
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R.; Ma, L.; Miki, H.; Lopez, M.; Kirchhausen, T.; Takenawa, T.; Kirschner, M.W. The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 1999, 97, 221-231.
    • (1999) Cell , vol.97 , pp. 221-231
    • Rohatgi, R.1    Ma, L.2    Miki, H.3    Lopez, M.4    Kirchhausen, T.5    Takenawa, T.6    Kirschner, M.W.7
  • 52
    • 2442494215 scopus 로고    scopus 로고
    • Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes
    • Chen, J.L.; Lacomis, L.; Erdjument-Bromage, H.; Tempst, P.; Stamnes, M. Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes. FEBS Lett. 2004, 566, 281-286.
    • (2004) FEBS Lett. , vol.566 , pp. 281-286
    • Chen, J.L.1    Lacomis, L.2    Erdjument-Bromage, H.3    Tempst, P.4    Stamnes, M.5
  • 53
    • 77956454496 scopus 로고    scopus 로고
    • Cdc42 and vesicle trafficking in polarized cells
    • Harris, K.P.; Tepass, U. Cdc42 and vesicle trafficking in polarized cells. Traffic 2010, 11, 1272-1279.
    • (2010) Traffic , vol.11 , pp. 1272-1279
    • Harris, K.P.1    Tepass, U.2
  • 54
    • 33747612463 scopus 로고    scopus 로고
    • Intersectin-1L nucleotide exchange factor regulates secretory granule exocytosis by activating Cdc42
    • Malacombe, M.; Ceridono, M.; Calco, V.; Chasserot-Golaz, S.; McPherson, P.S.; Bader, M.F.; Gasman, S. Intersectin-1L nucleotide exchange factor regulates secretory granule exocytosis by activating Cdc42. EMBO J. 2006, 25, 3494-3503.
    • (2006) EMBO J. , vol.25 , pp. 3494-3503
    • Malacombe, M.1    Ceridono, M.2    Calco, V.3    Chasserot-Golaz, S.4    McPherson, P.S.5    Bader, M.F.6    Gasman, S.7
  • 55
    • 0742288060 scopus 로고    scopus 로고
    • Regulated exocytosis in neuroendocrine cells: A role for subplasmalemmal Cdc42/N-WASP-induced actin filaments
    • Gasman, S.; Chasserot-Golaz, S.; Malacombe, M.; Way, M.; Bader, M.F. Regulated exocytosis in neuroendocrine cells: A role for subplasmalemmal Cdc42/N-WASP-induced actin filaments. Mol. Biol. Cell. 2004, 15, 520-531.
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 520-531
    • Gasman, S.1    Chasserot-Golaz, S.2    Malacombe, M.3    Way, M.4    Bader, M.F.5
  • 56
    • 23844522255 scopus 로고    scopus 로고
    • Membrane trafficking at the ER/Golgi interface: Functional implications of RhoA and Rac1
    • Matas, O.B.; Fritz, S.; Luna, A.; Egea, G. Membrane trafficking at the ER/Golgi interface: Functional implications of RhoA and Rac1. Eur. J. Cell Biol. 2005, 84, 699-707.
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 699-707
    • Matas, O.B.1    Fritz, S.2    Luna, A.3    Egea, G.4
  • 60
    • 83355166914 scopus 로고    scopus 로고
    • Identification of P-Rex1 as a novel Rac1-guanine nucleotide exchange factor (GEF) that promotes actin remodeling and GLUT4 protein trafficking in adipocytes
    • Balamatsias, D.; Kong, A.M.; Waters, J.E.; Sriratana, A.; Gurung, R.; Bailey, C.G.; Rasko, J.E.J.; Tiganis, T.; Macaulay, S.L.; Mitchell, C.A. Identification of P-Rex1 as a novel Rac1-guanine nucleotide exchange factor (GEF) that promotes actin remodeling and GLUT4 protein trafficking in adipocytes. J. Biol. Chem. 2011, 286, 43229-43240.
    • (2011) J. Biol. Chem. , vol.286 , pp. 43229-43240
    • Balamatsias, D.1    Kong, A.M.2    Waters, J.E.3    Sriratana, A.4    Gurung, R.5    Bailey, C.G.6    Rasko, J.E.J.7    Tiganis, T.8    McAulay, S.L.9    Mitchell, C.A.10
  • 61
    • 0034597599 scopus 로고    scopus 로고
    • Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis
    • Malecz, N.; McCabe, P.C.; Spaargaren, C.; Qiu, R.G.; Chuang, Y.; Symons, M. Synaptojanin 2, a novel Rac1 effector that regulates clathrin-mediated endocytosis. Curr. Biol. 2000, 10, 1383-1386.
    • (2000) Curr. Biol. , vol.10 , pp. 1383-1386
    • Malecz, N.1    McCabe, P.C.2    Spaargaren, C.3    Qiu, R.G.4    Chuang, Y.5    Symons, M.6
  • 62
    • 3342986329 scopus 로고    scopus 로고
    • Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments
    • Izumi, G.; Sakisaka, T.; Baba, T.; Tanaka, S.; Morimoto, K.; Takai, Y. Endocytosis of E-cadherin regulated by Rac and Cdc42 small G proteins through IQGAP1 and actin filaments. J. Cell Biol. 2004, 166, 237-248.
    • (2004) J. Cell Biol. , vol.166 , pp. 237-248
    • Izumi, G.1    Sakisaka, T.2    Baba, T.3    Tanaka, S.4    Morimoto, K.5    Takai, Y.6
  • 64
    • 70450246902 scopus 로고    scopus 로고
    • PIP5K-driven PtdIns (4, 5) P2 synthesis: Regulation and cellular functions
    • Van den Bout, I.; Divecha, N. PIP5K-driven PtdIns (4, 5) P2 synthesis: regulation and cellular functions. J. Cell Sci. 2009, 122, 3837-3850.
    • (2009) J. Cell Sci. , vol.122 , pp. 3837-3850
    • Van den Bout, I.1    Divecha, N.2
  • 67
    • 21144439797 scopus 로고    scopus 로고
    • A role for Rho and Rac in secretagogue-induced amylase release by pancreatic acini
    • Bi, Y.; Williams, J.A. A role for Rho and Rac in secretagogue-induced amylase release by pancreatic acini. Am. J. Physiol. Cell Physiol. 2005, 289, 22-32.
    • (2005) Am. J. Physiol. Cell Physiol. , vol.289 , pp. 22-32
    • Bi, Y.1    Williams, J.A.2
  • 68
    • 0032482379 scopus 로고    scopus 로고
    • EGF induces recycling membrane to form ruffles
    • Bretscher, M.S.; Aguado-Velasco, C. EGF induces recycling membrane to form ruffles. Curr. Biol. 1998, 8, 721-724.
    • (1998) Curr. Biol. , vol.8 , pp. 721-724
    • Bretscher, M.S.1    Aguado-Velasco, C.2
  • 69
    • 79151474591 scopus 로고    scopus 로고
    • The Rho guanine nucleotide exchange factors intersectin 1L and β-Pix control calcium-regulated exocytosis in neuroendocrine PC12 cells
    • Momboisse, F.; Ory, S.; Ceridono, M.; Calco, V.; Vitale, N.; Bader, M.F.; Gasman, S. The Rho guanine nucleotide exchange factors intersectin 1L and β-Pix control calcium-regulated exocytosis in neuroendocrine PC12 cells. Cell. Mol. Neurobiol. 2010, 30, 1327-1333.
    • (2010) Cell. Mol. Neurobiol. , vol.30 , pp. 1327-1333
    • Momboisse, F.1    Ory, S.2    Ceridono, M.3    Calco, V.4    Vitale, N.5    Bader, M.F.6    Gasman, S.7
  • 70
    • 66949135462 scopus 로고    scopus 로고
    • Beta PIX-activated Rac1 stimulates the activation of phospholipase D, which is associated with exocytosis in neuroendocrine cells
    • Momboisse, F.; Lonchamp, E.; Calco, V.; Ceridono, M.; Vitale, N.; Bader, M.F.; Gasman, S. beta PIX-activated Rac1 stimulates the activation of phospholipase D, which is associated with exocytosis in neuroendocrine cells. J. Cell Sci. 2009, 122, 798-806.
    • (2009) J. Cell Sci. , vol.122 , pp. 798-806
    • Momboisse, F.1    Lonchamp, E.2    Calco, V.3    Ceridono, M.4    Vitale, N.5    Bader, M.F.6    Gasman, S.7
  • 71
    • 70349168448 scopus 로고    scopus 로고
    • Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement
    • Chen, Y.; Yang, Z.; Meng, M.; Zhao, Y.; Dong, N.; Yan, H.; Liu, L.; Ding, M.; Peng, H.B.; Shao, F. Cullin mediates degradation of RhoA through evolutionarily conserved BTB adaptors to control actin cytoskeleton structure and cell movement. Mol. Cell 2009, 35, 841-855.
    • (2009) Mol. Cell , vol.35 , pp. 841-855
    • Chen, Y.1    Yang, Z.2    Meng, M.3    Zhao, Y.4    Dong, N.5    Yan, H.6    Liu, L.7    Ding, M.8    Peng, H.B.9    Shao, F.10
  • 72
    • 6344231714 scopus 로고    scopus 로고
    • Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility
    • Wheeler, A.P.; Ridley, A.J. Why three Rho proteins? RhoA, RhoB, RhoC, and cell motility. Exp. Cell Res. 2004, 301, 43-49.
    • (2004) Exp. Cell Res. , vol.301 , pp. 43-49
    • Wheeler, A.P.1    Ridley, A.J.2
  • 75
    • 77956476200 scopus 로고    scopus 로고
    • RhoA/Rho kinase (ROCK) alters fetuin-A uptake and regulates calcification in bovine vascular smooth muscle cells (BVSMC)
    • Chen, N.X.; Chen, X.; O'Neill, K.D.; Atkinson, S.J.; Moe, S.M. RhoA/Rho kinase (ROCK) alters fetuin-A uptake and regulates calcification in bovine vascular smooth muscle cells (BVSMC). Am. J. Physiol. Renal. Physiol. 2010, 299, 674-680.
    • (2010) Am. J. Physiol. Renal. Physiol. , vol.299 , pp. 674-680
    • Chen, N.X.1    Chen, X.2    O'Neill, K.D.3    Atkinson, S.J.4    Moe, S.M.5
  • 76
    • 0035265834 scopus 로고    scopus 로고
    • Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway
    • Lamaze, C.; Dujeancourt, A.; Baba, T.; Lo, C.G.; Benmerah, A.; Dautry-Varsat, A. Interleukin 2 receptors and detergent-resistant membrane domains define a clathrin-independent endocytic pathway. Mol. Cell 2001, 7, 661-671.
    • (2001) Mol. Cell , vol.7 , pp. 661-671
    • Lamaze, C.1    Dujeancourt, A.2    Baba, T.3    Lo, C.G.4    Benmerah, A.5    Dautry-Varsat, A.6
  • 77
    • 77953615099 scopus 로고    scopus 로고
    • Compensatory endocytosis in bladder umbrella cells occurs through an integrin-regulated and RhoA-and dynamin-dependent pathway
    • Khandelwal, P.; Ruiz, W.G.; Apodaca, G. Compensatory endocytosis in bladder umbrella cells occurs through an integrin-regulated and RhoA-and dynamin-dependent pathway. EMBO J. 2010, 29, 1961-1975.
    • (2010) EMBO J. , vol.29 , pp. 1961-1975
    • Khandelwal, P.1    Ruiz, W.G.2    Apodaca, G.3
  • 78
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: Multifunctional kinases in cell behaviour
    • Riento, K.; Ridley, A.J. Rocks: multifunctional kinases in cell behaviour. Nat. Rev. Mol. Cell Biol. 2003, 4, 446-456.
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 80
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop, A.L.; Hall, A. Rho GTPases and their effector proteins. Biochem. J. 2000, 348, 241-255.
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 81
    • 84862003012 scopus 로고    scopus 로고
    • The transcription factor GCF2 is an upstream repressor of the small GTPase RhoA, regulating membrane protein trafficking, sensitivity to doxorubicin, and resistance to cisplatin
    • Shen, D.W.; Pouliot, L.M.; Gillet, J.P.; Ma, W.; Johnson, A.C.; Hall, M.D.; Gottesman, M.M. The transcription factor GCF2 is an upstream repressor of the small GTPase RhoA, regulating membrane protein trafficking, sensitivity to doxorubicin, and resistance to cisplatin. Mol. Pharm. 2012, 9, 1822-1833.
    • (2012) Mol. Pharm. , vol.9 , pp. 1822-1833
    • Shen, D.W.1    Pouliot, L.M.2    Gillet, J.P.3    Ma, W.4    Johnson, A.C.5    Hall, M.D.6    Gottesman, M.M.7
  • 85
    • 84861164214 scopus 로고    scopus 로고
    • Vesicular trafficking through cortical actin during exocytosis is regulated by the Rab27a effector JFC1/Slp1 and the RhoA-GTPase-activating protein Gem-interacting protein
    • Johnson, J.L.; Monfregola, J.; Napolitano, G.; Kiosses, W.B.; Catz, S.D. Vesicular trafficking through cortical actin during exocytosis is regulated by the Rab27a effector JFC1/Slp1 and the RhoA-GTPase-activating protein Gem-interacting protein. Mol. Biol. Cell. 2012, 23, 1902-1916.
    • (2012) Mol. Biol. Cell. , vol.23 , pp. 1902-1916
    • Johnson, J.L.1    Monfregola, J.2    Napolitano, G.3    Kiosses, W.B.4    Catz, S.D.5
  • 86
    • 84858980804 scopus 로고    scopus 로고
    • Transport of influenza virus neuraminidase (NA) to host cell surface is regulated by ARHGAP21 and Cdc42 proteins
    • Wang, S.; Li, H.; Chen, Y.; Wei, H.; Gao, G.F.; Liu, H.; Huang, S.; Chen, J.L. Transport of influenza virus neuraminidase (NA) to host cell surface is regulated by ARHGAP21 and Cdc42 proteins. J. Biol. Chem. 2012, 287, 9804-9816.
    • (2012) J. Biol. Chem. , vol.287 , pp. 9804-9816
    • Wang, S.1    Li, H.2    Chen, Y.3    Wei, H.4    Gao, G.F.5    Liu, H.6    Huang, S.7    Chen, J.L.8
  • 87
    • 33144460942 scopus 로고    scopus 로고
    • YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42
    • Hui, E.K.W.; Barman, S.; Tang, D.H.P.; France, B.; Nayak, D.P. YRKL sequence of influenza virus M1 functions as the L domain motif and interacts with VPS28 and Cdc42. J. Virol. 2006, 80, 2291-2308.
    • (2006) J. Virol. , vol.80 , pp. 2291-2308
    • Hui, E.K.W.1    Barman, S.2    Tang, D.H.P.3    France, B.4    Nayak, D.P.5
  • 88
    • 0031663239 scopus 로고    scopus 로고
    • Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family GTPases
    • Li, E.; Stupack, D.; Bokoch, G.M.; Nemerow, G. R. Adenovirus endocytosis requires actin cytoskeleton reorganization mediated by Rho family GTPases. J. Virol. 1998, 72, 8806-8812.
    • (1998) J. Virol. , vol.72 , pp. 8806-8812
    • Li, E.1    Stupack, D.2    Bokoch, G.M.3    Nemerow, G.R.4
  • 89
    • 0033799367 scopus 로고    scopus 로고
    • Endocytosis and nuclear trafficking of adeno-associated virus type 2 are controlled by Rac1 and phosphatidylinositol-3 kinase activation
    • Sanlioglu, S.; Benson, P.K.; Yang, J.; Atkinson, E.M.; Reynolds, T.; Engelhardt, J.F. Endocytosis and nuclear trafficking of adeno-associated virus type 2 are controlled by Rac1 and phosphatidylinositol-3 kinase activation. J. Virol. 2000, 74, 9184-9196.
    • (2000) J. Virol. , vol.74 , pp. 9184-9196
    • Sanlioglu, S.1    Benson, P.K.2    Yang, J.3    Atkinson, E.M.4    Reynolds, T.5    Engelhardt, J.F.6
  • 90
    • 83655164541 scopus 로고    scopus 로고
    • Adeno-associated virus 2 infection requires endocytosis through the CLIC/GEEC pathway
    • Nonnenmacher, M.; Weber, T. Adeno-associated virus 2 infection requires endocytosis through the CLIC/GEEC pathway. Cell Host Microbe 2011, 10, 563-576.
    • (2011) Cell Host Microbe , vol.10 , pp. 563-576
    • Nonnenmacher, M.1    Weber, T.2
  • 91
    • 84871972407 scopus 로고    scopus 로고
    • Japanese encephalitis virus infects neuronal cells through a clathrin-independent endocytic mechanism
    • Kalia, M.; Khasa, R.; Sharma, M.; Nain, M.; Vrati, S. Japanese encephalitis virus infects neuronal cells through a clathrin-independent endocytic mechanism. J. Virol. 2013, 87, 148-162.
    • (2013) J. Virol. , vol.87 , pp. 148-162
    • Kalia, M.1    Khasa, R.2    Sharma, M.3    Nain, M.4    Vrati, S.5
  • 92
    • 33751414583 scopus 로고    scopus 로고
    • Early herpes simplex virus type 1 infection is dependent on regulated Rac1/Cdc42 signalling in epithelial MDCKII cells
    • Hoppe, S.; Schelhaas, M.; Jaeger, V.; Liebig, T.; Petermann, P.; Knebel-Mörsdorf, D. Early herpes simplex virus type 1 infection is dependent on regulated Rac1/Cdc42 signalling in epithelial MDCKII cells. J. Gen. Virol. 2006, 87, 3483-3494.
    • (2006) J. Gen. Virol. , vol.87 , pp. 3483-3494
    • Hoppe, S.1    Schelhaas, M.2    Jaeger, V.3    Liebig, T.4    Petermann, P.5    Knebel-Mörsdorf, D.6
  • 93
    • 11144224272 scopus 로고    scopus 로고
    • Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus
    • Naranatt, P.P.; Krishnan, H.H.; Smith, M.S.; Chandran, B. Kaposi's sarcoma-associated herpesvirus modulates microtubule dynamics via RhoA-GTP-diaphanous 2 signaling and utilizes the dynein motors to deliver its DNA to the nucleus. J. Virol. 2005, 79, 1191-1206.
    • (2005) J. Virol. , vol.79 , pp. 1191-1206
    • Naranatt, P.P.1    Krishnan, H.H.2    Smith, M.S.3    Chandran, B.4
  • 94
    • 34547096966 scopus 로고    scopus 로고
    • Lipid rafts of primary endothelial cells are essential for Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8-induced phosphatidylinositol 3-kinase and RhoA-GTPases critical for microtubule dynamics and nuclear delivery of viral DNA but dispensable for binding and entry
    • Raghu, H.; Sharma-Walia, N.; Veettil, M.V.; Sadagopan, S.; Caballero, A.; Sivakumar, R.; Varga, L.; Bottero, V.; Chandran, B. Lipid rafts of primary endothelial cells are essential for Kaposi's sarcoma-associated herpesvirus/human herpesvirus 8-induced phosphatidylinositol 3-kinase and RhoA-GTPases critical for microtubule dynamics and nuclear delivery of viral DNA but dispensable for binding and entry. J. Virol. 2007, 81, 7941-7959.
    • (2007) J. Virol. , vol.81 , pp. 7941-7959
    • Raghu, H.1    Sharma-Walia, N.2    Veettil, M.V.3    Sadagopan, S.4    Caballero, A.5    Sivakumar, R.6    Varga, L.7    Bottero, V.8    Chandran, B.9
  • 95
    • 33751001055 scopus 로고    scopus 로고
    • Citron kinase, a RhoA effector, enhances HIV-1 virion production by modulating exocytosis
    • Loomis, R.J.; Holmes, D.A.; Elms, A.; Solski, P.A.; Der, C.J.; Su, L. Citron kinase, a RhoA effector, enhances HIV-1 virion production by modulating exocytosis. Traffic 2006, 7, 1643-1653.
    • (2006) Traffic , vol.7 , pp. 1643-1653
    • Loomis, R.J.1    Holmes, D.A.2    Elms, A.3    Solski, P.A.4    Der, C.J.5    Su, L.6
  • 97
    • 70049116403 scopus 로고    scopus 로고
    • Actin dynamics regulate multiple endosomal steps during Kaposi's sarcoma-associated herpesvirus entry and trafficking in endothelial cells
    • Greene, W.; Gao, S.J. Actin dynamics regulate multiple endosomal steps during Kaposi's sarcoma-associated herpesvirus entry and trafficking in endothelial cells. PLoS Pathog. 2009, 5, e1000512.
    • (2009) PLoS Pathog. , vol.5
    • Greene, W.1    Gao, S.J.2
  • 98
    • 84857097606 scopus 로고    scopus 로고
    • Small Rho GTPases and cholesterol biosynthetic pathway intermediates in African swine fever virus infection
    • Quetglas, J.I.; Hernáez, B.; Galindo, I.; Muñoz-Moreno, R.; Cuesta-Geijo, M.A.; Alonso, C. Small Rho GTPases and cholesterol biosynthetic pathway intermediates in African swine fever virus infection. J. Virol. 2012, 86, 1758-1767.
    • (2012) J. Virol. , vol.86 , pp. 1758-1767
    • Quetglas, J.I.1    Hernáez, B.2    Galindo, I.3    Muñoz-Moreno, R.4    Cuesta-Geijo, M.A.5    Alonso, C.6
  • 99
    • 0034907213 scopus 로고    scopus 로고
    • mDia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo, A.F.; Cook, T.A.; Alberts, A.S.; Gundersen, G.G. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 2001, 3, 723-729.
    • (2001) Nat. Cell Biol. , vol.3 , pp. 723-729
    • Palazzo, A.F.1    Cook, T.A.2    Alberts, A.S.3    Gundersen, G.G.4
  • 100
    • 34248190773 scopus 로고    scopus 로고
    • F11L-mediated inhibition of RhoA-mDia signaling stimulates microtubule dynamics during vaccinia virus infection
    • Arakawa, Y.; Cordeiro, J.V.; Way, M. F11L-mediated inhibition of RhoA-mDia signaling stimulates microtubule dynamics during vaccinia virus infection. Cell Host Microbe 2007, 1, 213-226.
    • (2007) Cell Host Microbe , vol.1 , pp. 213-226
    • Arakawa, Y.1    Cordeiro, J.V.2    Way, M.3
  • 101
    • 34248208646 scopus 로고    scopus 로고
    • The release of vaccinia virus from infected cells requires RhoA-mDia modulation of cortical actin
    • Arakawa, Y.; Cordeiro, J.V.; Schleich, S.; Newsome, T.P.; Way, M. The release of vaccinia virus from infected cells requires RhoA-mDia modulation of cortical actin. Cell Host Microbe 2007, 1, 227-240.
    • (2007) Cell Host Microbe , vol.1 , pp. 227-240
    • Arakawa, Y.1    Cordeiro, J.V.2    Schleich, S.3    Newsome, T.P.4    Way, M.5
  • 102
    • 31144458118 scopus 로고    scopus 로고
    • Vaccinia virus-induced cell motility requires F11L-mediated inhibition of RhoA signaling
    • Valderrama, F.; Cordeiro, J.V.; Schleich, S.; Frischknecht, F.; Way, M. Vaccinia virus-induced cell motility requires F11L-mediated inhibition of RhoA signaling. Science 2006, 311, 377-381.
    • (2006) Science , vol.311 , pp. 377-381
    • Valderrama, F.1    Cordeiro, J.V.2    Schleich, S.3    Frischknecht, F.4    Way, M.5
  • 103
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • Bos, J.L.; Rehmann, H.; Wittinghofer, A. GEFs and GAPs: Critical elements in the control of small G proteins. Cell 2007, 129, 865-877.
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 104
    • 79958772180 scopus 로고    scopus 로고
    • Cdc42 in oncogenic transformation, invasion, and tumorigenesis
    • Stengel, K.; Zheng, Y. Cdc42 in oncogenic transformation, invasion, and tumorigenesis. Cell. Signal. 2011, 23, 1415-1423.
    • (2011) Cell. Signal. , vol.23 , pp. 1415-1423
    • Stengel, K.1    Zheng, Y.2
  • 105
    • 0033551698 scopus 로고    scopus 로고
    • Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation
    • Lin, R.; Cerione, R.A.; Manor, D. Specific contributions of the small GTPases Rho, Rac, and Cdc42 to Dbl transformation. J. Biol. Chem. 1999, 274, 23633-23641.
    • (1999) J. Biol. Chem. , vol.274 , pp. 23633-23641
    • Lin, R.1    Cerione, R.A.2    Manor, D.3
  • 106
    • 33846969965 scopus 로고    scopus 로고
    • Current knowledge of the large RhoGAP family of proteins
    • Tcherkezian, J.; Lamarche-Vane, N. Current knowledge of the large RhoGAP family of proteins. Biol. Cell 2007, 99, 67-86.
    • (2007) Biol. Cell , vol.99 , pp. 67-86
    • Tcherkezian, J.1    Lamarche-Vane, N.2
  • 107
    • 40149083557 scopus 로고    scopus 로고
    • Deleted in liver cancer-1 (DLC-1): A tumor suppressor not just for liver
    • Liao, Y.C.; Lo, S.H. Deleted in liver cancer-1 (DLC-1): A tumor suppressor not just for liver. Int. J. Biochem. Cell Biol. 2008, 40, 843-847.
    • (2008) Int. J. Biochem. Cell Biol. , vol.40 , pp. 843-847
    • Liao, Y.C.1    Lo, S.H.2
  • 108
    • 79953057231 scopus 로고    scopus 로고
    • ARAP3 inhibits peritoneal dissemination of scirrhous gastric carcinoma cells by regulating cell adhesion and invasion
    • Yagi, R.; Tanaka, M.; Sasaki, K.; Kamata, R.; Nakanishi, Y.; Kanai, Y.; Sakai, R. ARAP3 inhibits peritoneal dissemination of scirrhous gastric carcinoma cells by regulating cell adhesion and invasion. Oncogene 2010, 30, 1413-1421.
    • (2010) Oncogene , vol.30 , pp. 1413-1421
    • Yagi, R.1    Tanaka, M.2    Sasaki, K.3    Kamata, R.4    Nakanishi, Y.5    Kanai, Y.6    Sakai, R.7
  • 109
    • 70350218798 scopus 로고    scopus 로고
    • TrkBT1 induces liver metastasis of pancreatic cancer cells by sequestering Rho GDP dissociation inhibitor and promoting RhoA activation
    • Li, Z.; Chang, Z.; Chiao, L.J.; Kang, Y.A.; Xia, Q.; Zhu, C.; Fleming, J.B.; Evans, D.B.; Chiao, P.J. TrkBT1 induces liver metastasis of pancreatic cancer cells by sequestering Rho GDP dissociation inhibitor and promoting RhoA activation. Cancer Res. 2009, 69, 7851-7859.
    • (2009) Cancer Res. , vol.69 , pp. 7851-7859
    • Li, Z.1    Chang, Z.2    Chiao, L.J.3    Kang, Y.A.4    Xia, Q.5    Zhu, C.6    Fleming, J.B.7    Evans, D.B.8    Chiao, P.J.9
  • 110
    • 2542606977 scopus 로고    scopus 로고
    • Reduced expression of metastasis suppressor RhoGDI2 is associated with decreased survival for patients with bladder cancer
    • Theodorescu, D.; Sapinoso, L.; Conaway, M.; Oxford, G.; Hampton, G.; Frierson, H. Reduced expression of metastasis suppressor RhoGDI2 is associated with decreased survival for patients with bladder cancer. Clin. Cancer. Res. 2004, 10, 3800-3806.
    • (2004) Clin. Cancer. Res. , vol.10 , pp. 3800-3806
    • Theodorescu, D.1    Sapinoso, L.2    Conaway, M.3    Oxford, G.4    Hampton, G.5    Frierson, H.6
  • 111
    • 0042761752 scopus 로고    scopus 로고
    • RhoGDI is required for Cdc42-mediated cellular transformation
    • Lin, Q.; Fuji, R.N.; Yang, W.; Cerione, R.A. RhoGDI is required for Cdc42-mediated cellular transformation. Curr. Biol. 2003, 13, 1469-1479.
    • (2003) Curr. Biol. , vol.13 , pp. 1469-1479
    • Lin, Q.1    Fuji, R.N.2    Yang, W.3    Cerione, R.A.4
  • 112
    • 0028903247 scopus 로고
    • An essential role for Rac in Ras transformation
    • Qiu, R.G.; Chen, J.; Kirn, D.; McCormick, F.; Symons, M. An essential role for Rac in Ras transformation. Nature 1995, 374, 457-459.
    • (1995) Nature , vol.374 , pp. 457-459
    • Qiu, R.G.1    Chen, J.2    Kirn, D.3    McCormick, F.4    Symons, M.5
  • 114
    • 0030992814 scopus 로고    scopus 로고
    • Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation
    • Qiu, R.G.; Abo, A.; McCormick, F.; Symons, M. Cdc42 regulates anchorage-independent growth and is necessary for Ras transformation. Mol. Cell. Biol. 1997, 17, 3449-3458.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 3449-3458
    • Qiu, R.G.1    Abo, A.2    McCormick, F.3    Symons, M.4
  • 115
    • 84862490151 scopus 로고    scopus 로고
    • Essential role of Cdc42 in Ras-induced transformation revealed by gene targeting
    • Stengel, K.R.; Zheng, Y. Essential role of Cdc42 in Ras-induced transformation revealed by gene targeting. PLoS One 2012, 7, e37317.
    • (2012) PLoS One , vol.7
    • Stengel, K.R.1    Zheng, Y.2
  • 117
    • 0033547363 scopus 로고    scopus 로고
    • Functional Rac-1 and Nck signaling networks are required for FGF-2-induced DNA synthesis in MCF-7 cells
    • Liu, J.F.; Chevet, E.; Kebache, S.; Lemaitre, G.; Barritault, D.; Larose, L.; Crepin, M. Functional Rac-1 and Nck signaling networks are required for FGF-2-induced DNA synthesis in MCF-7 cells. Oncogene 1999, 18, 6425-6433.
    • (1999) Oncogene , vol.18 , pp. 6425-6433
    • Liu, J.F.1    Chevet, E.2    Kebache, S.3    Lemaitre, G.4    Barritault, D.5    Larose, L.6    Crepin, M.7
  • 118
    • 79959322098 scopus 로고    scopus 로고
    • Rho GTPase effector functions in tumor cell invasion and metastasis
    • Baranwal, S.; K Alahari, S. Rho GTPase effector functions in tumor cell invasion and metastasis. Curr. Drug Targets 2011, 12, 1194-1201.
    • (2011) Curr. Drug Targets , vol.12 , pp. 1194-1201
    • Baranwal, S.1    Alahari, S.K.2
  • 119
    • 84876011758 scopus 로고    scopus 로고
    • PAK signaling in cancer
    • Ye, D.Z.; Field, J. PAK signaling in cancer. Cell Logist. 2012, 2, 105-116.
    • (2012) Cell Logist. , vol.2 , pp. 105-116
    • Ye, D.Z.1    Field, J.2
  • 120
    • 0141426629 scopus 로고    scopus 로고
    • Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation
    • Wu, W.J.; Tu, S.; Cerione, R.A. Activated Cdc42 sequesters c-Cbl and prevents EGF receptor degradation. Cell 2003, 114, 715-725.
    • (2003) Cell , vol.114 , pp. 715-725
    • Wu, W.J.1    Tu, S.2    Cerione, R.A.3
  • 122
    • 46549089054 scopus 로고    scopus 로고
    • Simulation of the regulation of EGFR endocytosis and EGFR-ERK signaling by endophilin-mediated RhoA-EGFR crosstalk
    • Ung, C.Y.; Li, H.; Ma, X.H.; Jia, J.; Li, B.W.; Low, B.C.; Chen, Y.Z. Simulation of the regulation of EGFR endocytosis and EGFR-ERK signaling by endophilin-mediated RhoA-EGFR crosstalk. FEBS Lett. 2008, 582, 2283-2290.
    • (2008) FEBS Lett. , vol.582 , pp. 2283-2290
    • Ung, C.Y.1    Li, H.2    Ma, X.H.3    Jia, J.4    Li, B.W.5    Low, B.C.6    Chen, Y.Z.7
  • 123
    • 68549122708 scopus 로고    scopus 로고
    • Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion
    • Narumiya, S.; Tanji, M.; Ishizaki, T. Rho signaling, ROCK and mDia1, in transformation, metastasis and invasion. Cancer Metast. Rev. 2009, 28, 65-76.
    • (2009) Cancer Metast. Rev. , vol.28 , pp. 65-76
    • Narumiya, S.1    Tanji, M.2    Ishizaki, T.3
  • 125
    • 70350418724 scopus 로고    scopus 로고
    • Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions
    • Albiges-Rizo, C.; Destaing, O.; Fourcade, B.; Planus, E.; Block, M.R. Actin machinery and mechanosensitivity in invadopodia, podosomes and focal adhesions. J. Cell Sci. 2009, 122, 3037-3049.
    • (2009) J. Cell Sci. , vol.122 , pp. 3037-3049
    • Albiges-Rizo, C.1    Destaing, O.2    Fourcade, B.3    Planus, E.4    Block, M.R.5
  • 127
    • 34247468876 scopus 로고    scopus 로고
    • Regulation of the actin cytoskeleton in cancer cell migration and invasion
    • Yamaguchi, H.; Condeelis, J. Regulation of the actin cytoskeleton in cancer cell migration and invasion. BBA-Mol. Cell Res. 2007, 1773, 642-652.
    • (2007) BBA-Mol. Cell Res. , vol.1773 , pp. 642-652
    • Yamaguchi, H.1    Condeelis, J.2
  • 128
    • 84862629472 scopus 로고    scopus 로고
    • Hic-5 promotes invadopodia formation and invasion during TGF-β-induced epithelial-mesenchymal transition
    • Pignatelli, J.; Tumbarello, D.A.; Schmidt, R.P.; Turner, C.E. Hic-5 promotes invadopodia formation and invasion during TGF-β-induced epithelial-mesenchymal transition. J. Cell Biol. 2012, 197, 421-437.
    • (2012) J. Cell Biol. , vol.197 , pp. 421-437
    • Pignatelli, J.1    Tumbarello, D.A.2    Schmidt, R.P.3    Turner, C.E.4
  • 129
    • 14844318496 scopus 로고    scopus 로고
    • Rac-WAVE2 signaling is involved in the invasive and metastatic phenotypes of murine melanoma cells
    • Kurisu, S.; Suetsugu, S.; Yamazaki, D.; Yamaguchi, H.; Takenawa, T. Rac-WAVE2 signaling is involved in the invasive and metastatic phenotypes of murine melanoma cells. Oncogene 2004, 24, 1309-1319.
    • (2004) Oncogene , vol.24 , pp. 1309-1319
    • Kurisu, S.1    Suetsugu, S.2    Yamazaki, D.3    Yamaguchi, H.4    Takenawa, T.5
  • 131
    • 35348997467 scopus 로고    scopus 로고
    • ROCK-II mediates colon cancer invasion via regulation of MMP-2 and MMP-13 at the site of invadopodia as revealed by multiphoton imaging
    • Vishnubhotla, R.; Sun, S.; Huq, J.; Bulic, M.; Ramesh, A.; Guzman, G.; Cho, M.; Glover, S.C. ROCK-II mediates colon cancer invasion via regulation of MMP-2 and MMP-13 at the site of invadopodia as revealed by multiphoton imaging. Lab. Invest. 2007, 87, 1149-1158.
    • (2007) Lab. Invest. , vol.87 , pp. 1149-1158
    • Vishnubhotla, R.1    Sun, S.2    Huq, J.3    Bulic, M.4    Ramesh, A.5    Guzman, G.6    Cho, M.7    Glover, S.C.8


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