메뉴 건너뛰기




Volumn 11, Issue 10, 2010, Pages 1272-1279

Cdc42 and Vesicle Trafficking in Polarized Cells

Author keywords

Adherens junctions; APKC; Arp2 3; Cdc42; Cell polarity; Drosophila; Par3; Par6; Vesicle trafficking; Yeast

Indexed keywords

ACTIN; COATOMER PROTEIN; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PHOSPHATIDYLINOSITOL 3,4,5 TRISPHOSPHATE 3 PHOSPHATASE; PROTEIN CDC42; PROTEIN KINASE C; RHO KINASE;

EID: 77956454496     PISSN: 13989219     EISSN: 16000854     Source Type: Journal    
DOI: 10.1111/j.1600-0854.2010.01102.x     Document Type: Review
Times cited : (151)

References (72)
  • 1
  • 2
    • 54549102285 scopus 로고    scopus 로고
    • Coordinated protein sorting, targeting and distribution in polarized cells.
    • Mellman I, Nelson WJ. Coordinated protein sorting, targeting and distribution in polarized cells. Nat Rev Mol Cell Biol 2008, 9:833-845..
    • (2008) Nat Rev Mol Cell Biol , vol.9
    • Mellman, I.1    Nelson, W.J.2
  • 3
    • 62849097694 scopus 로고    scopus 로고
    • New roles for endosomes: from vesicular carriers to multi-purpose platforms.
    • Gould GW, Lippincott-Schwartz J. New roles for endosomes: from vesicular carriers to multi-purpose platforms. Nat Rev Mol Cell Biol 2009, 10:287-292..
    • (2009) Nat Rev Mol Cell Biol , vol.10
    • Gould, G.W.1    Lippincott-Schwartz, J.2
  • 4
    • 69249137477 scopus 로고    scopus 로고
    • Endocytosis and signalling: intertwining molecular networks.
    • Sorkin A, von Zastrow M. Endocytosis and signalling: intertwining molecular networks. Nat Rev Mol Cell Biol 2009, 10:609-622..
    • (2009) Nat Rev Mol Cell Biol , vol.10
    • Sorkin, A.1    von Zastrow, M.2
  • 5
    • 70450128390 scopus 로고    scopus 로고
    • Apical trafficking in epithelial cells: signals, clusters and motors.
    • Weisz OA, Rodriguez-Boulan E. Apical trafficking in epithelial cells: signals, clusters and motors. J Cell Sci 2009, 122:4253-4266..
    • (2009) J Cell Sci , vol.122
    • Weisz, O.A.1    Rodriguez-Boulan, E.2
  • 6
    • 70450176317 scopus 로고    scopus 로고
    • Polarized traffic towards the cell surface: how to find the route.
    • Carmosino M, Valenti G, Caplan M, Svelto M. Polarized traffic towards the cell surface: how to find the route. Biol Cell 2009, 102:75-91..
    • (2009) Biol Cell , vol.102
    • Carmosino, M.1    Valenti, G.2    Caplan, M.3    Svelto, M.4
  • 8
    • 35549001736 scopus 로고    scopus 로고
    • The PAR proteins: fundamental players in animal cell polarization.
    • Goldstein B, Macara IG. The PAR proteins: fundamental players in animal cell polarization. Dev Cell 2007, 13:609-622..
    • (2007) Dev Cell , vol.13
    • Goldstein, B.1    Macara, I.G.2
  • 9
    • 0037032804 scopus 로고    scopus 로고
    • Composition and formation of intercellular junctions in epithelial cells.
    • Knust E, Bossinger O. Composition and formation of intercellular junctions in epithelial cells. Science 2002, 298:1955-1959..
    • (2002) Science , vol.298
    • Knust, E.1    Bossinger, O.2
  • 10
    • 0037452071 scopus 로고    scopus 로고
    • Adaptation of core mechanisms to generate cell polarity.
    • Nelson WJ. Adaptation of core mechanisms to generate cell polarity. Nature 2003, 422:766-774..
    • (2003) Nature , vol.422
    • Nelson, W.J.1
  • 11
    • 2342432240 scopus 로고    scopus 로고
    • Cdc42-the centre of polarity.
    • Etienne-Manneville S. Cdc42-the centre of polarity. J Cell Sci 2004, 117:1291-1300..
    • (2004) J Cell Sci , vol.117
    • Etienne-Manneville, S.1
  • 12
    • 1442274703 scopus 로고    scopus 로고
    • Cdc42: new roads to travel.
    • Cerione RA. Cdc42: new roads to travel. Trends Cell Biol 2004, 14:127-132..
    • (2004) Trends Cell Biol , vol.14
    • Cerione, R.A.1
  • 13
    • 33645746316 scopus 로고    scopus 로고
    • The PAR-aPKC system: lessons in polarity.
    • Suzuki A, Ohno S. The PAR-aPKC system: lessons in polarity. J Cell Sci 2006, 119:979-987..
    • (2006) J Cell Sci , vol.119
    • Suzuki, A.1    Ohno, S.2
  • 14
    • 24644499168 scopus 로고    scopus 로고
    • Molecular control of cell polarity and asymmetric cell division in Drosophila neuroblasts.
    • Wodarz A. Molecular control of cell polarity and asymmetric cell division in Drosophila neuroblasts. Curr Opin Cell Biol 2005, 17:475-481..
    • (2005) Curr Opin Cell Biol , vol.17
    • Wodarz, A.1
  • 15
    • 77953283628 scopus 로고    scopus 로고
    • Cell polarity in eggs and epithelia: parallels and diversity.
    • St Johnston D, Ahringer J. Cell polarity in eggs and epithelia: parallels and diversity. Cell 2010, 141:757-774..
    • (2010) Cell , vol.141
    • St Johnston, D.1    Ahringer, J.2
  • 16
    • 0025294640 scopus 로고
    • CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae.
    • Adams AE, Johnson DI, Longnecker RM, Sloat BF, Pringle JR. CDC42 and CDC43, two additional genes involved in budding and the establishment of cell polarity in the yeast Saccharomyces cerevisiae. J Cell Biol 1990, 111:131-142..
    • (1990) J Cell Biol , vol.111
    • Adams, A.E.1    Johnson, D.I.2    Longnecker, R.M.3    Sloat, B.F.4    Pringle, J.R.5
  • 19
    • 33947398366 scopus 로고    scopus 로고
    • Central roles of small GTPases in the development of cell polarity in yeast and beyond.
    • Park HO, Bi E. Central roles of small GTPases in the development of cell polarity in yeast and beyond. Microbiol Mol Biol Rev 2007, 71:48-96..
    • (2007) Microbiol Mol Biol Rev , vol.71
    • Park, H.O.1    Bi, E.2
  • 20
    • 0037815488 scopus 로고    scopus 로고
    • Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast.
    • Dong Y, Pruyne D, Bretscher A. Formin-dependent actin assembly is regulated by distinct modes of Rho signaling in yeast. J Cell Biol 2003, 161:1081-1092..
    • (2003) J Cell Biol , vol.161
    • Dong, Y.1    Pruyne, D.2    Bretscher, A.3
  • 21
    • 0026484397 scopus 로고
    • Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth, and their defect is suppressed by a high dose of bud formation genes CDC42 and BEM1.
    • Matsui Y, Toh-E A. Yeast RHO3 and RHO4 ras superfamily genes are necessary for bud growth, and their defect is suppressed by a high dose of bud formation genes CDC42 and BEM1. Mol Cell Biol 1992, 12:5690-5699..
    • (1992) Mol Cell Biol , vol.12
    • Matsui, Y.1    Toh-E, A.2
  • 23
    • 38349030651 scopus 로고    scopus 로고
    • Membrane association and functional regulation of Sec3 by phospholipids and Cdc42.
    • Zhang X, Orlando K, He B, Xi F, Zhang J, Zajac A, Guo W. Membrane association and functional regulation of Sec3 by phospholipids and Cdc42. J Cell Biol 2008, 180:145-158..
    • (2008) J Cell Biol , vol.180
    • Zhang, X.1    Orlando, K.2    He, B.3    Xi, F.4    Zhang, J.5    Zajac, A.6    Guo, W.7
  • 24
    • 0025814609 scopus 로고
    • Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway.
    • Chant J, Herskowitz I. Genetic control of bud site selection in yeast by a set of gene products that constitute a morphogenetic pathway. Cell 1991, 65:1203-1212..
    • (1991) Cell , vol.65
    • Chant, J.1    Herskowitz, I.2
  • 25
    • 4544295912 scopus 로고    scopus 로고
    • Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling.
    • Wedlich-Soldner R, Wai SC, Schmidt T, Li R. Robust cell polarity is a dynamic state established by coupling transport and GTPase signaling. J Cell Biol 2004, 166:889-900..
    • (2004) J Cell Biol , vol.166
    • Wedlich-Soldner, R.1    Wai, S.C.2    Schmidt, T.3    Li, R.4
  • 28
    • 0037458909 scopus 로고    scopus 로고
    • Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase.
    • Wedlich-Soldner R, Altschuler S, Wu L, Li R. Spontaneous cell polarization through actomyosin-based delivery of the Cdc42 GTPase. Science 2003, 299:1231-1235..
    • (2003) Science , vol.299
    • Wedlich-Soldner, R.1    Altschuler, S.2    Wu, L.3    Li, R.4
  • 29
    • 34147175165 scopus 로고    scopus 로고
    • Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity.
    • Marco E, Wedlich-Soldner R, Li R, Altschuler SJ, Wu LF. Endocytosis optimizes the dynamic localization of membrane proteins that regulate cortical polarity. Cell 2007, 129:411-422..
    • (2007) Cell , vol.129
    • Marco, E.1    Wedlich-Soldner, R.2    Li, R.3    Altschuler, S.J.4    Wu, L.F.5
  • 31
    • 60749122102 scopus 로고    scopus 로고
    • Actin nucleation and elongation factors: mechanisms and interplay.
    • Chesarone MA, Goode BL. Actin nucleation and elongation factors: mechanisms and interplay. Curr Opin Cell Biol 2009, 21:28-37..
    • (2009) Curr Opin Cell Biol , vol.21
    • Chesarone, M.A.1    Goode, B.L.2
  • 32
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: connecting the membrane to the cytoskeleton.
    • Takenawa T, Suetsugu S. The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat Rev Mol Cell Biol 2007, 8:37-48..
    • (2007) Nat Rev Mol Cell Biol , vol.8
    • Takenawa, T.1    Suetsugu, S.2
  • 33
    • 48249134102 scopus 로고    scopus 로고
    • Mediation, modulation, and consequences of membrane-cytoskeleton interactions.
    • Doherty GJ, McMahon HT. Mediation, modulation, and consequences of membrane-cytoskeleton interactions. Annu Rev Biophys 2008, 37:65-95..
    • (2008) Annu Rev Biophys , vol.37
    • Doherty, G.J.1    McMahon, H.T.2
  • 34
    • 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
    • Lanzetti, L.1
  • 35
    • 33845699085 scopus 로고    scopus 로고
    • Actin regulation in endocytosis.
    • Smythe E, Ayscough KR. Actin regulation in endocytosis. J Cell Sci 2006, 119:4589-4598..
    • (2006) J Cell Sci , vol.119
    • Smythe, E.1    Ayscough, K.R.2
  • 36
    • 38549147387 scopus 로고    scopus 로고
    • Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells.
    • Trifaró JM, Gasman S, Gutiérrez LM. Cytoskeletal control of vesicle transport and exocytosis in chromaffin cells. Acta Physiol (Oxf) 2008, 192:165-172..
    • (2008) Acta Physiol (Oxf) , vol.192
    • Trifaró, J.M.1    Gasman, S.2    Gutiérrez, L.M.3
  • 37
    • 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 RG, 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
    • Sabharanjak, S.1    Sharma, P.2    Parton, R.G.3    Mayor, S.4
  • 38
    • 34249090252 scopus 로고    scopus 로고
    • Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway.
    • Chadda R, Howes MT, Plowman SJ, Hancock JF, Parton RG, Mayor S. Cholesterol-sensitive Cdc42 activation regulates actin polymerization for endocytosis via the GEEC pathway. Traffic 2007, 8:702-717..
    • (2007) Traffic , vol.8
    • Chadda, R.1    Howes, M.T.2    Plowman, S.J.3    Hancock, J.F.4    Parton, R.G.5    Mayor, S.6
  • 39
    • 34547114456 scopus 로고    scopus 로고
    • Pathways of clathrin-independent endocytosis.
    • Mayor S, Pagano RE. Pathways of clathrin-independent endocytosis. Nat Rev Mol Cell Biol 2007, 8:603-612..
    • (2007) Nat Rev Mol Cell Biol , vol.8
    • Mayor, S.1    Pagano, R.E.2
  • 40
    • 0029998595 scopus 로고    scopus 로고
    • Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus.
    • Erickson JW, Zhang C, Kahn RA, Evans T, Cerione RA. Mammalian Cdc42 is a brefeldin A-sensitive component of the Golgi apparatus. J Biol Chem 1996, 271:26850-26854..
    • (1996) J Biol Chem , vol.271
    • Erickson, J.W.1    Zhang, C.2    Kahn, R.A.3    Evans, T.4    Cerione, R.A.5
  • 41
    • 0001264854 scopus 로고    scopus 로고
    • The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation.
    • Wu WJ, Erickson JW, Lin R, Cerione RA. The gamma-subunit of the coatomer complex binds Cdc42 to mediate transformation. Nature 2000, 405:800-804..
    • (2000) Nature , vol.405
    • Wu, W.J.1    Erickson, J.W.2    Lin, R.3    Cerione, R.A.4
  • 42
    • 0036179523 scopus 로고    scopus 로고
    • Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1.
    • Fucini RV, Chen JL, Sharma C, Kessels MM, Stamnes M. Golgi vesicle proteins are linked to the assembly of an actin complex defined by mAbp1. Mol Biol Cell 2002, 13:621-631..
    • (2002) Mol Biol Cell , vol.13
    • Fucini, R.V.1    Chen, J.L.2    Sharma, C.3    Kessels, M.M.4    Stamnes, M.5
  • 43
    • 2442494215 scopus 로고    scopus 로고
    • Cytosol-derived proteins are sufficient for Arp2/3 recruitment and ARF/coatomer-dependent actin polymerization on Golgi membranes.
    • Chen JL, 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
    • Chen, J.L.1    Lacomis, L.2    Erdjument-Bromage, H.3    Tempst, P.4    Stamnes, M.5
  • 45
    • 7244238111 scopus 로고    scopus 로고
    • Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes.
    • Matas OB, Martínez-Menárguez JA, Egea G. Association of Cdc42/N-WASP/Arp2/3 signaling pathway with Golgi membranes. Traffic 2004, 5:838-846..
    • (2004) Traffic , vol.5
    • Matas, O.B.1    Martínez-Menárguez, J.A.2    Egea, G.3
  • 47
    • 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
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 48
    • 0034903162 scopus 로고    scopus 로고
    • Selective control of basolateral membrane protein polarity by cdc42.
    • Cohen D, Müsch A, Rodriguez-Boulan E. Selective control of basolateral membrane protein polarity by cdc42. Traffic 2001, 2:556-564..
    • (2001) Traffic , vol.2
    • Cohen, D.1    Müsch, A.2    Rodriguez-Boulan, E.3
  • 49
    • 0035341316 scopus 로고    scopus 로고
    • Cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network.
    • Müsch A, Cohen D, Kreitzer G, Rodriguez-Boulan E. cdc42 regulates the exit of apical and basolateral proteins from the trans-Golgi network. EMBO J 2001, 20:2171-2179..
    • (2001) EMBO J , vol.20
    • Müsch, A.1    Cohen, D.2    Kreitzer, G.3    Rodriguez-Boulan, E.4
  • 50
    • 0035159369 scopus 로고    scopus 로고
    • Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cells.
    • Rojas R, Ruiz WG, Leung SM, Jou TS, Apodaca G. Cdc42-dependent modulation of tight junctions and membrane protein traffic in polarized Madin-Darby canine kidney cells. Mol Biol Cell 2001, 12:2257-2274..
    • (2001) Mol Biol Cell , vol.12
    • Rojas, R.1    Ruiz, W.G.2    Leung, S.M.3    Jou, T.S.4    Apodaca, G.5
  • 51
    • 63249127139 scopus 로고    scopus 로고
    • Multifaceted role of Rho, Rac, Cdc42 and Ras in intercellular junctions, lessons from toxins.
    • Popoff MR, Geny B. Multifaceted role of Rho, Rac, Cdc42 and Ras in intercellular junctions, lessons from toxins. Biochim Biophys Acta 2009, 1788:797-812..
    • (2009) Biochim Biophys Acta , vol.1788
    • Popoff, M.R.1    Geny, B.2
  • 52
    • 3242705077 scopus 로고    scopus 로고
    • RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin.
    • Bruewer M, Hopkins AM, Hobert ME, Nusrat A, Madara JL. RhoA, Rac1, and Cdc42 exert distinct effects on epithelial barrier via selective structural and biochemical modulation of junctional proteins and F-actin. Am J Physiol Cell Physiol 2004, 287:C327-C335..
    • (2004) Am J Physiol Cell Physiol , vol.287
    • Bruewer, M.1    Hopkins, A.M.2    Hobert, M.E.3    Nusrat, A.4    Madara, J.L.5
  • 55
    • 41549086164 scopus 로고    scopus 로고
    • Regulation of cell polarity during epithelial morphogenesis.
    • Martin-Belmonte F, Mostov K. Regulation of cell polarity during epithelial morphogenesis. Curr Opin Cell Biol 2008, 20:227-234..
    • (2008) Curr Opin Cell Biol , vol.20
    • Martin-Belmonte, F.1    Mostov, K.2
  • 56
    • 33846270032 scopus 로고    scopus 로고
    • PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42.
    • Martin-Belmonte F, Gassama A, Datta A, Yu W, Rescher U, Gerke V, Mostov K. PTEN-mediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 2007, 128:383-397..
    • (2007) Cell , vol.128
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5    Gerke, V.6    Mostov, K.7
  • 58
    • 34548295310 scopus 로고    scopus 로고
    • Genome-wide analysis identifies a general requirement for polarity proteins in endocytic traffic.
    • Balklava Z, Pant S, Fares H, Grant BD. Genome-wide analysis identifies a general requirement for polarity proteins in endocytic traffic. Nat Cell Biol 2007, 9:1066-1073..
    • (2007) Nat Cell Biol , vol.9
    • Balklava, Z.1    Pant, S.2    Fares, H.3    Grant, B.D.4
  • 59
    • 58249094157 scopus 로고    scopus 로고
    • Cdc42 and Par proteins stabilize dynamic adherens junctions in the Drosophila neuroectoderm through regulation of apical endocytosis.
    • Harris KP, Tepass U. Cdc42 and Par proteins stabilize dynamic adherens junctions in the Drosophila neuroectoderm through regulation of apical endocytosis. J Cell Biol 2008, 183:1129-1143..
    • (2008) J Cell Biol , vol.183
    • Harris, K.P.1    Tepass, U.2
  • 60
    • 55249111248 scopus 로고    scopus 로고
    • Cdc42, Par6, and aPKC regulate Arp2/3-mediated endocytosis to control local adherens junction stability.
    • Georgiou M, Marinari E, Burden J, Baum B. Cdc42, Par6, and aPKC regulate Arp2/3-mediated endocytosis to control local adherens junction stability. Curr Biol 2008, 18:1631-1638..
    • (2008) Curr Biol , vol.18
    • Georgiou, M.1    Marinari, E.2    Burden, J.3    Baum, B.4
  • 61
    • 55249104474 scopus 로고    scopus 로고
    • Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-cadherin endocytosis.
    • Leibfried A, Fricke R, Morgan MJ, Bogdan S, Bellaiche Y. Drosophila Cip4 and WASp define a branch of the Cdc42-Par6-aPKC pathway regulating E-cadherin endocytosis. Curr Biol 2008, 18:1639-1648..
    • (2008) Curr Biol , vol.18
    • Leibfried, A.1    Fricke, R.2    Morgan, M.J.3    Bogdan, S.4    Bellaiche, Y.5
  • 63
    • 1842419430 scopus 로고    scopus 로고
    • Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts.
    • Merrifield CJ, Qualmann B, Kessels MM, Almers W. Neural Wiskott Aldrich Syndrome Protein (N-WASP) and the Arp2/3 complex are recruited to sites of clathrin-mediated endocytosis in cultured fibroblasts. Eur J Cell Biol 2004, 83:13-18..
    • (2004) Eur J Cell Biol , vol.83
    • Merrifield, C.J.1    Qualmann, B.2    Kessels, M.M.3    Almers, W.4
  • 64
    • 19344375254 scopus 로고    scopus 로고
    • Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells.
    • Merrifield CJ, Perrais D, Zenisek D. Coupling between clathrin-coated-pit invagination, cortactin recruitment, and membrane scission observed in live cells. Cell 2005, 121:593-606..
    • (2005) Cell , vol.121
    • Merrifield, C.J.1    Perrais, D.2    Zenisek, D.3
  • 65
    • 58049135823 scopus 로고    scopus 로고
    • Roles of F-BAR/PCH proteins in the regulation of membrane dynamics and actin reorganization.
    • Aspenström P. Roles of F-BAR/PCH proteins in the regulation of membrane dynamics and actin reorganization. Int Rev Cell Mol Biol 2009, 272:1-31..
    • (2009) Int Rev Cell Mol Biol , vol.272
    • Aspenström, P.1
  • 67
    • 52949115363 scopus 로고    scopus 로고
    • Linking cell cycle to asymmetric division: Aurora-A phosphorylates the Par complex to regulate Numb localization.
    • Wirtz-Peitz F, Nishimura T, Knoblich JA. Linking cell cycle to asymmetric division: Aurora-A phosphorylates the Par complex to regulate Numb localization. Cell 2008, 135:161-173..
    • (2008) Cell , vol.135
    • Wirtz-Peitz, F.1    Nishimura, T.2    Knoblich, J.A.3
  • 69
    • 67449161807 scopus 로고    scopus 로고
    • Distinct functions for Rho1 in maintaining adherens junctions and apical tension in remodeling epithelia.
    • Warner SJ, Longmore GD. Distinct functions for Rho1 in maintaining adherens junctions and apical tension in remodeling epithelia. J Cell Biol 2009, 185:1111-1125..
    • (2009) J Cell Biol , vol.185
    • Warner, S.J.1    Longmore, G.D.2
  • 70
    • 70449573317 scopus 로고    scopus 로고
    • Cdc42 antagonizes Rho1 activity at adherens junctions to limit epithelial cell apical tension.
    • Warner SJ, Longmore GD. Cdc42 antagonizes Rho1 activity at adherens junctions to limit epithelial cell apical tension. J Cell Biol 2009, 187:119-133..
    • (2009) J Cell Biol , vol.187
    • Warner, S.J.1    Longmore, G.D.2
  • 71
    • 0842281652 scopus 로고    scopus 로고
    • Rho and Rac take center stage.
    • Burridge K, Wennerberg K. Rho and Rac take center stage. Cell 2004, 116:167-179..
    • (2004) Cell , vol.116
    • Burridge, K.1    Wennerberg, K.2
  • 72
    • 52149106669 scopus 로고    scopus 로고
    • Cellular signaling for activation of Rho GTPase Cdc42.
    • Sinha S, Yang W. Cellular signaling for activation of Rho GTPase Cdc42. Cell Signal 2008, 20:1927-1934..
    • (2008) Cell Signal , vol.20
    • Sinha, S.1    Yang, W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.