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Volumn 21, Issue , 2005, Pages 247-269

Rho GTPases: Biochemistry and biology

Author keywords

Cell cycle; Cytoskeleton; Migration; Morphogenesis

Indexed keywords

ACTIN; RHO GUANINE NUCLEOTIDE BINDING PROTEIN;

EID: 27944479854     PISSN: 10810706     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.cellbio.21.020604.150721     Document Type: Review
Times cited : (2496)

References (151)
  • 1
    • 0037223605 scopus 로고    scopus 로고
    • Control of cell polarity and mitotic spindle positioning in animal cells
    • Ahringer J. 2003. Control of cell polarity and mitotic spindle positioning in animal cells. Curr. Opin. Cell Biol. 15:73-81
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 73-81
    • Ahringer, J.1
  • 3
    • 0034604710 scopus 로고    scopus 로고
    • Phosphorylation of collapsin response mediator protein-2 by Rho-kinase. Evidence for two separate signaling pathways for growth cone collapse
    • Arimura N, Inagaki N, Chihara K, Menager C, Nakamura N, et al. 2000. Phosphorylation of collapsin response mediator protein-2 by Rho-kinase. Evidence for two separate signaling pathways for growth cone collapse. J. Biol. Chem. 275:23973-80
    • (2000) J. Biol. Chem. , vol.275 , pp. 23973-23980
    • Arimura, N.1    Inagaki, N.2    Chihara, K.3    Menager, C.4    Nakamura, N.5
  • 4
    • 0942268723 scopus 로고    scopus 로고
    • Rho GTPases have diverse effects on the organization of the actin filament system
    • Aspenstrom P, Fransson A, Saras J. 2004. Rho GTPases have diverse effects on the organization of the actin filament system. Biochem. J. 377:327-37
    • (2004) Biochem. J. , vol.377 , pp. 327-337
    • Aspenstrom, P.1    Fransson, A.2    Saras, J.3
  • 5
    • 0030929148 scopus 로고    scopus 로고
    • IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links microfilaments
    • Bashour AM, Fullerton AT, Hart MJ, Bloom GS. 1997. IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links microfilaments. J. Cell Biol. 137:1555-66
    • (1997) J. Cell Biol. , vol.137 , pp. 1555-1566
    • Bashour, A.M.1    Fullerton, A.T.2    Hart, M.J.3    Bloom, G.S.4
  • 6
    • 0037451803 scopus 로고    scopus 로고
    • GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila
    • Bernards A. 2003. GAPs galore! A survey of putative Ras superfamily GTPase activating proteins in man and Drosophila. Biochim. Biophys. Acta 1603:47-82
    • (2003) Biochim. Biophys. Acta , vol.1603 , pp. 47-82
    • Bernards, A.1
  • 7
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop AL, Hall A. 2000. Rho GTPases and their effector proteins. Biochem. J. 348(Pt 2):241-55
    • (2000) Biochem. J. , vol.348 , Issue.PART 2 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 8
    • 0033730417 scopus 로고    scopus 로고
    • Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell-cell adhesion in normal human keratinocytes
    • Braga VM, Betson M, Li X, Lamarche-Vane N. 2000. Activation of the small GTPase Rac is sufficient to disrupt cadherin-dependent cell-cell adhesion in normal human keratinocytes. Mol. Biol. Cell 11:3703-21
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3703-3721
    • Braga, V.M.1    Betson, M.2    Li, X.3    Lamarche-Vane, N.4
  • 9
    • 0030968177 scopus 로고    scopus 로고
    • The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts
    • Braga VM, Machesky LM, Hall A, Hotchin NA. 1997. The small GTPases Rho and Rac are required for the establishment of cadherin-dependent cell-cell contacts. J. Cell Biol. 137:1421-31
    • (1997) J. Cell Biol. , vol.137 , pp. 1421-1431
    • Braga, V.M.1    Machesky, L.M.2    Hall, A.3    Hotchin, N.A.4
  • 10
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo PD, Drechsel D, Hall A. 1995. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270:29071-74
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 11
    • 21644460380 scopus 로고    scopus 로고
    • Cdc42 controls the polarity of the actin and microtubule cytoskeletons through two distinct signal transduction pathways
    • Cau J, Hall A. 2005. Cdc42 controls the polarity of the actin and microtubule cytoskeletons through two distinct signal transduction pathways. J. Cell Sci. 118(Pt. 12):2579-87
    • (2005) J. Cell Sci. , vol.118 , Issue.PART 12 , pp. 2579-2587
    • Cau, J.1    Hall, A.2
  • 12
    • 0036468982 scopus 로고    scopus 로고
    • The oncoprotein 18/stathmin family of microtubule destabilizers
    • Cassimeris L. 2002. The oncoprotein 18/stathmin family of microtubule destabilizers. Curr. Opin. Cell Biol. 14:18-24
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 18-24
    • Cassimeris, L.1
  • 13
    • 18544402891 scopus 로고    scopus 로고
    • 2-induced actin polymerization and early development but not for cell viability
    • 2-induced actin polymerization and early development but not for cell viability. Curr. Biol. 10:758-65
    • (2000) Curr. Biol. , vol.10 , pp. 758-765
    • Chen, F.1    Ma, L.2    Parrini, M.C.3    Mao, X.4    Lopez, M.5
  • 14
    • 0041315642 scopus 로고    scopus 로고
    • Cdc42 promotes G1 progression through p70 S6 kinase-mediated induction of cyclin e expression
    • Chou MM, Masuda-Robens JM, Gupta ML. 2003. Cdc42 promotes G1 progression through p70 S6 kinase-mediated induction of cyclin E expression. J. Biol. Chem. 278:35241-47
    • (2003) J. Biol. Chem. , vol.278 , pp. 35241-35247
    • Chou, M.M.1    Masuda-Robens, J.M.2    Gupta, M.L.3
  • 16
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway
    • Coso OA, Chiariello M, Yu JC, Teramoto H, Crespo P, et al. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell 81:1137-46
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5
  • 17
    • 0035910554 scopus 로고    scopus 로고
    • Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16
    • Daub H, Gevaert K, Vandekerckhove J, Sobel A, Hall A. 2001. Rac/Cdc42 and p65PAK regulate the microtubule-destabilizing protein stathmin through phosphorylation at serine 16. J. Biol. Chem. 276:1677-80
    • (2001) J. Biol. Chem. , vol.276 , pp. 1677-1680
    • Daub, H.1    Gevaert, K.2    Vandekerckhove, J.3    Sobel, A.4    Hall, A.5
  • 18
    • 12244303674 scopus 로고    scopus 로고
    • ADF/cofilin controls cell polarity during fibroblast migration
    • Dawe HR, Minamide LS, Bamburg JR, Cramer LP. 2003. ADF/cofilin controls cell polarity during fibroblast migration. Curr. Biol. 13:252-57
    • (2003) Curr. Biol. , vol.13 , pp. 252-257
    • Dawe, H.R.1    Minamide, L.S.2    Bamburg, J.R.3    Cramer, L.P.4
  • 20
    • 0033635236 scopus 로고    scopus 로고
    • Defective neurogenesis in citron kinase knockout mice by altered cytokinesis and massive apoptosis
    • Di Cunto F, Imarisio S, Hirsch E, Broccoli V, Bulfone A, et al. 2000. Defective neurogenesis in citron kinase knockout mice by altered cytokinesis and massive apoptosis. Neuron 28:115-27
    • (2000) Neuron , vol.28 , pp. 115-127
    • Di Cunto, F.1    Imarisio, S.2    Hirsch, E.3    Broccoli, V.4    Bulfone, A.5
  • 21
    • 0028169005 scopus 로고
    • Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity
    • Diekmann D, Abo A, Johnston C, Segal AW, Hall A. 1994. Interaction of Rac with p67phox and regulation of phagocytic NADPH oxidase activity. Science 265:531-33
    • (1994) Science , vol.265 , pp. 531-533
    • Diekmann, D.1    Abo, A.2    Johnston, C.3    Segal, A.W.4    Hall, A.5
  • 22
    • 0037102301 scopus 로고    scopus 로고
    • Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck
    • Eden S, Rohatgi R, Podtelejnikov AV, Mann M, Kirschner MW. 2002. Mechanism of regulation of WAVE1-induced actin nucleation by Rac1 and Nck. Nature 418:790-93
    • (2002) Nature , vol.418 , pp. 790-793
    • Eden, S.1    Rohatgi, R.2    Podtelejnikov, A.V.3    Mann, M.4    Kirschner, M.W.5
  • 23
    • 0036696823 scopus 로고    scopus 로고
    • Spatio-temporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion
    • Ehrlich JS, Hansen MD, Nelson WJ. 2002. Spatio-temporal regulation of Rac1 localization and lamellipodia dynamics during epithelial cell-cell adhesion. Dev. Cell 3:259-70
    • (2002) Dev. Cell , vol.3 , pp. 259-270
    • Ehrlich, J.S.1    Hansen, M.D.2    Nelson, W.J.3
  • 24
    • 0035943401 scopus 로고    scopus 로고
    • Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta
    • Etienne-Manneville S, Hall A. 2001. Integrin-mediated activation of Cdc42 controls cell polarity in migrating astrocytes through PKCzeta. Cell 106:489-98
    • (2001) Cell , vol.106 , pp. 489-498
    • Etienne-Manneville, S.1    Hall, A.2
  • 25
    • 0037069690 scopus 로고    scopus 로고
    • Rho GTPases in cell biology
    • Etienne-Manneville S, Hall A. 2002. Rho GTPases in cell biology. Nature 420:629-35
    • (2002) Nature , vol.420 , pp. 629-635
    • Etienne-Manneville, S.1    Hall, A.2
  • 26
    • 0037434790 scopus 로고    scopus 로고
    • Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity
    • Etienne-Manneville S, Hall A. 2003. Cdc42 regulates GSK-3beta and adenomatous polyposis coli to control cell polarity. Nature 421:753-56
    • (2003) Nature , vol.421 , pp. 753-756
    • Etienne-Manneville, S.1    Hall, A.2
  • 27
    • 1242351972 scopus 로고    scopus 로고
    • Planar polarity from flies to vertebrates
    • Fanto M, McNeill H. 2004. Planar polarity from flies to vertebrates. J. Cell Sci. 117:527-33
    • (2004) J. Cell Sci. , vol.117 , pp. 527-533
    • Fanto, M.1    McNeill, H.2
  • 28
    • 18444369936 scopus 로고    scopus 로고
    • Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170
    • Fukata M, Watanabe T, Noritake J, Nakagawa M, Yamaga M, et al. 2002. Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170. Cell 109:873-85
    • (2002) Cell , vol.109 , pp. 873-885
    • Fukata, M.1    Watanabe, T.2    Noritake, J.3    Nakagawa, M.4    Yamaga, M.5
  • 29
  • 30
    • 3543063555 scopus 로고    scopus 로고
    • Activation of Cdc42 by trans interactions of the cell adhesion molecules nectins through c-Src and Cdc42-GEF FRG
    • Fukuhara T, Shimizu K, Kawakatsu T, Fukuyama T, Minami Y, et al. 2004. Activation of Cdc42 by trans interactions of the cell adhesion molecules nectins through c-Src and Cdc42-GEF FRG. J. Cell Biol. 166:393-405
    • (2004) J. Cell Biol. , vol.166 , pp. 393-405
    • Fukuhara, T.1    Shimizu, K.2    Kawakatsu, T.3    Fukuyama, T.4    Minami, Y.5
  • 31
    • 0345826110 scopus 로고    scopus 로고
    • Rho a binds to the amino terminus of MEKK1 and regulates its kinase activity
    • Gallagher ED, Gutowski S, Sternweis PC, Cobb MH. 2004. Rho A binds to the amino terminus of MEKK1 and regulates its kinase activity. J. Biol. Chem. 279:1872-77
    • (2004) J. Biol. Chem. , vol.279 , pp. 1872-1877
    • Gallagher, E.D.1    Gutowski, S.2    Sternweis, P.C.3    Cobb, M.H.4
  • 32
    • 0037022122 scopus 로고    scopus 로고
    • Assembly of epithelial tight junctions is negatively regulated by Par6
    • Gao L, Joberty G, Macara IG. 2002. Assembly of epithelial tight junctions is negatively regulated by Par6. Curr. Biol. 12:221-25
    • (2002) Curr. Biol. , vol.12 , pp. 221-225
    • Gao, L.1    Joberty, G.2    Macara, I.G.3
  • 34
  • 35
    • 0344413422 scopus 로고    scopus 로고
    • Apicobasal polarization: Epithelial form and function
    • Gibson MC, Perrimon N. 2003. Apicobasal polarization: epithelial form and function. Curr. Opin. Cell Biol. 15:747-52
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 747-752
    • Gibson, M.C.1    Perrimon, N.2
  • 36
    • 0030793160 scopus 로고    scopus 로고
    • Coupling of Jun amino-terminal kinase and Decapentaplegic signaling pathways in Drosophila morphogenesis
    • Glise B, Noselli S. 1997. Coupling of Jun amino-terminal kinase and Decapentaplegic signaling pathways in Drosophila morphogenesis. Genes Dev. 11:1738-47
    • (1997) Genes Dev. , vol.11 , pp. 1738-1747
    • Glise, B.1    Noselli, S.2
  • 38
    • 0035799292 scopus 로고    scopus 로고
    • CDC-42 controls early cell polarity and spindle orientation in C. elegans
    • Gotta M, Abraham MC, Ahringer J. 2001. CDC-42 controls early cell polarity and spindle orientation in C. elegans. Curr. Biol. 11:482-88
    • (2001) Curr. Biol. , vol.11 , pp. 482-488
    • Gotta, M.1    Abraham, M.C.2    Ahringer, J.3
  • 39
    • 0031019308 scopus 로고    scopus 로고
    • Role of Rho family proteins in phospholipase D activation by growth factors
    • Hess JA, Ross AH, Qiu RG, Symons M, Exton JH. 1997. Role of Rho family proteins in phospholipase D activation by growth factors. J. Biol. Chem. 272:1615-20
    • (1997) J. Biol. Chem. , vol.272 , pp. 1615-1620
    • Hess, J.A.1    Ross, A.H.2    Qiu, R.G.3    Symons, M.4    Exton, J.H.5
  • 40
    • 0037096161 scopus 로고    scopus 로고
    • Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation
    • Hirose T, Izumi Y, Nagashima Y, Tamai-Nagai Y, Kurihara H, et al. 2002. Involvement of ASIP/PAR-3 in the promotion of epithelial tight junction formation. J. Cell Sci. 115:2485-95
    • (2002) J. Cell Sci. , vol.115 , pp. 2485-2495
    • Hirose, T.1    Izumi, Y.2    Nagashima, Y.3    Tamai-Nagai, Y.4    Kurihara, H.5
  • 41
    • 3242671847 scopus 로고    scopus 로고
    • Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex
    • Ho HY, Rohatgi R, Lebensohn AM, Le M, Li J, et al. 2004. Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 118:203-16
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.1    Rohatgi, R.2    Lebensohn, A.M.3    Le, M.4    Li, J.5
  • 42
    • 0035949469 scopus 로고    scopus 로고
    • CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family
    • Ho HY, Rohatgi R, Ma L, Kirschner MW. 2001. CR16 forms a complex with N-WASP in brain and is a novel member of a conserved proline-rich actin-binding protein family. Proc. Natl. Acad. Sci. USA 98:11306-11
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 11306-11311
    • Ho, H.Y.1    Rohatgi, R.2    Ma, L.3    Kirschner, M.W.4
  • 44
    • 0030742943 scopus 로고    scopus 로고
    • Drosophila Jun relays the Jun amino-terminal kinase signal transduction pathway to the Decapentaplegic signal transduction pathway in regulating epithelial cell sheet movement
    • Hou XS, Goldstein ES, Perrimon N. 1997. Drosophila Jun relays the Jun amino-terminal kinase signal transduction pathway to the Decapentaplegic signal transduction pathway in regulating epithelial cell sheet movement. Genes Dev. 11:1728-37
    • (1997) Genes Dev. , vol.11 , pp. 1728-1737
    • Hou, X.S.1    Goldstein, E.S.2    Perrimon, N.3
  • 46
    • 0033525188 scopus 로고    scopus 로고
    • RhoA stimulates p27(Kip) degradation through its regulation of cyclin E/CDK2 activity
    • Hu W, Bellone CJ, Baldassare JJ. 1999. RhoA stimulates p27(Kip) degradation through its regulation of cyclin E/CDK2 activity. J. Biol. Chem. 274:3396-401
    • (1999) J. Biol. Chem. , vol.274 , pp. 3396-3401
    • Hu, W.1    Bellone, C.J.2    Baldassare, J.J.3
  • 48
    • 0032476733 scopus 로고    scopus 로고
    • Stimulation of phospholipase C-beta2 by the Rho GTPases Cdc42Hs and Rac1
    • Illenberger D, Schwald F, Pimmer D, Binder W, Maier G, et al. 1998. Stimulation of phospholipase C-beta2 by the Rho GTPases Cdc42Hs and Rac1. EMBO J. 17:6241-49
    • (1998) EMBO J. , vol.17 , pp. 6241-6249
    • Illenberger, D.1    Schwald, F.2    Pimmer, D.3    Binder, W.4    Maier, G.5
  • 49
    • 2342483041 scopus 로고    scopus 로고
    • Abi1 is essential for the formation and activation of a WAVE2 signalling complex
    • Innocenti M, Zucconi A, Disanza A, Frittoli E, Areces LB, et al. 2004. Abi1 is essential for the formation and activation of a WAVE2 signalling complex. Nat. Cell Biol. 6:319-27
    • (2004) Nat. Cell Biol. , vol.6 , pp. 319-327
    • Innocenti, M.1    Zucconi, A.2    Disanza, A.3    Frittoli, E.4    Areces, L.B.5
  • 51
    • 0035817623 scopus 로고    scopus 로고
    • Junctional adhesion molecule (JAM) binds to PAR-3: A possible mechanism for the recruitment of PAR-3 to tight junctions
    • Itoh M, Sasaki H, Furuse M, Ozaki H, Kita T, Tsukita S. 2001. Junctional adhesion molecule (JAM) binds to PAR-3: a possible mechanism for the recruitment of PAR-3 to tight junctions. J. Cell Biol. 154:491-97
    • (2001) J. Cell Biol. , vol.154 , pp. 491-497
    • Itoh, M.1    Sasaki, H.2    Furuse, M.3    Ozaki, H.4    Kita, T.5    Tsukita, S.6
  • 52
    • 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 RE, Kurokawa K, Ohba Y, Yoshizaki H, Mochizuki N, Matsuda M. 2002. 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. 22:6582-91
    • (2002) Mol. Cell Biol. , vol.22 , pp. 6582-6591
    • Itoh, R.E.1    Kurokawa, K.2    Ohba, Y.3    Yoshizaki, H.4    Mochizuki, N.5    Matsuda, M.6
  • 53
    • 0032487494 scopus 로고    scopus 로고
    • An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3
    • Izumi Y, Hirose T, Tamai Y, Hirai S, Nagashima Y, et al. 1998. An atypical PKC directly associates and colocalizes at the epithelial tight junction with ASIP, a mammalian homologue of Caenorhabditis elegans polarity protein PAR-3. J. Cell Biol. 143:95-106
    • (1998) J. Cell Biol. , vol.143 , pp. 95-106
    • Izumi, Y.1    Hirose, T.2    Tamai, Y.3    Hirai, S.4    Nagashima, Y.5
  • 54
    • 0034676297 scopus 로고    scopus 로고
    • Dynamic actin-based epithelial adhesion and cell matching during Drosophila dorsal closure
    • Jacinto A, Wood W, Balayo T, Turmaine M, Martinez-Arias A, Martin P. 2000. Dynamic actin-based epithelial adhesion and cell matching during Drosophila dorsal closure. Curr. Biol. 10:1420-26
    • (2000) Curr. Biol. , vol.10 , pp. 1420-1426
    • Jacinto, A.1    Wood, W.2    Balayo, T.3    Turmaine, M.4    Martinez-Arias, A.5    Martin, P.6
  • 55
    • 0036191304 scopus 로고    scopus 로고
    • Rho GTPases in transformation and metastasis
    • Jaffe AB, Hall A. 2002. Rho GTPases in transformation and metastasis. Adv. Cancer Res. 84:57-80
    • (2002) Adv. Cancer Res. , vol.84 , pp. 57-80
    • Jaffe, A.B.1    Hall, A.2
  • 56
    • 14744276941 scopus 로고    scopus 로고
    • Association of CNK1 with Rho guanine nucleotide exchange factors controls signaling specificity downstream of Rho
    • Jaffe AB, Hall A, Schmidt A. 2005. Association of CNK1 with Rho guanine nucleotide exchange factors controls signaling specificity downstream of Rho. Curr. Biol. 15:405-12
    • (2005) Curr. Biol. , vol.15 , pp. 405-412
    • Jaffe, A.B.1    Hall, A.2    Schmidt, A.3
  • 57
    • 11844260672 scopus 로고    scopus 로고
    • Both the establishment and the maintenance of neuronal polarity require active mechanisms: Critical roles of GSK-3 beta and its upstream regulators
    • Jiang H, Guo W, Liang X, Rao Y. 2005. Both the establishment and the maintenance of neuronal polarity require active mechanisms: critical roles of GSK-3 beta and its upstream regulators. Cell 120:123-35
    • (2005) Cell , vol.120 , pp. 123-135
    • Jiang, H.1    Guo, W.2    Liang, X.3    Rao, Y.4
  • 58
    • 0032541085 scopus 로고    scopus 로고
    • A Rac1 effector site controlling mitogenesis through superoxide production
    • Joneson T, Bar-Sagi D. 1998. A Rac1 effector site controlling mitogenesis through superoxide production. J. Biol. Chem. 273:17991-94
    • (1998) J. Biol. Chem. , vol.273 , pp. 17991-17994
    • Joneson, T.1    Bar-Sagi, D.2
  • 59
    • 0033520458 scopus 로고    scopus 로고
    • Integration of Rac-dependent regulation of cyclin D1 transcription through a nuclear factor-kappaB-dependent pathway
    • Joyce D, Bouzahzah B, Fu M, Albanese C, D'Amico M, et al. 1999. Integration of Rac-dependent regulation of cyclin D1 transcription through a nuclear factor-kappaB-dependent pathway. J. Biol. Chem. 274:25245-49
    • (1999) J. Biol. Chem. , vol.274 , pp. 25245-25249
    • Joyce, D.1    Bouzahzah, B.2    Fu, M.3    Albanese, C.4    D'Amico, M.5
  • 60
    • 0035081810 scopus 로고    scopus 로고
    • Localization of a mammalian homolog of diaphanous, mDial, to the mitotic spindle in HeLa cells
    • Kato T, Watanabe N, Morishima Y, Fujita A, Ishizaki T, Narumiya S. 2001. Localization of a mammalian homolog of diaphanous, mDial, to the mitotic spindle in HeLa cells. J. Cell Sci. 114:775-84
    • (2001) J. Cell Sci. , vol.114 , pp. 775-784
    • Kato, T.1    Watanabe, N.2    Morishima, Y.3    Fujita, A.4    Ishizaki, T.5    Narumiya, S.6
  • 61
    • 0037184967 scopus 로고    scopus 로고
    • Trans-interactions of nectins induce formation of filopodia and lamellipodia through the respective activation of Cdc42 and Rac small G proteins
    • Kawakatsu T, Shimizu K, Honda T, Fukuhara T, Hoshino T, Takai Y. 2002. Trans-interactions of nectins induce formation of filopodia and lamellipodia through the respective activation of Cdc42 and Rac small G proteins. J. Biol. Chem. 277:50749-55
    • (2002) J. Biol. Chem. , vol.277 , pp. 50749-50755
    • Kawakatsu, T.1    Shimizu, K.2    Honda, T.3    Fukuhara, T.4    Hoshino, T.5    Takai, Y.6
  • 62
    • 0032496326 scopus 로고    scopus 로고
    • Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change
    • Kheradmand F, Werner E, Tremble P, Symons M, Werb Z. 1998. Role of Rac1 and oxygen radicals in collagenase-1 expression induced by cell shape change. Science 280:898-902
    • (1998) Science , vol.280 , pp. 898-902
    • Kheradmand, F.1    Werner, E.2    Tremble, P.3    Symons, M.4    Werb, Z.5
  • 63
    • 0034602428 scopus 로고    scopus 로고
    • Effects of the regulatory light chain phosphorylation of myosin II on mitosis and cytokinesis of mammalian cells
    • Komatsu S, Yano T, Shibata M, Tuft RA, Ikebe M. 2000. Effects of the regulatory light chain phosphorylation of myosin II on mitosis and cytokinesis of mammalian cells. J. Biol. Chem. 275:34512-20
    • (2000) J. Biol. Chem. , vol.275 , pp. 34512-34520
    • Komatsu, S.1    Yano, T.2    Shibata, M.3    Tuft, R.A.4    Ikebe, M.5
  • 64
    • 0034619765 scopus 로고    scopus 로고
    • Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow
    • Kosako H, Yoshida T, Matsumura F, Ishizaki T, Narumiya S, Inagaki M. 2000. Rho-kinase/ROCK is involved in cytokinesis through the phosphorylation of myosin light chain and not ezrin/radixin/moesin proteins at the cleavage furrow. Oncogene 19:6059-64
    • (2000) Oncogene , vol.19 , pp. 6059-6064
    • Kosako, H.1    Yoshida, T.2    Matsumura, F.3    Ishizaki, T.4    Narumiya, S.5    Inagaki, M.6
  • 66
    • 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. 1999. Cdc42 controls secretory and endocytic transport to the basolateral plasma membrane of MDCK cells. Nat. Cell Biol. 1:8-13
    • (1999) Nat. Cell Biol. , vol.1 , pp. 8-13
    • Kroschewski, R.1    Hall, A.2    Mellman, I.3
  • 67
    • 0033584471 scopus 로고    scopus 로고
    • Cdc42, Rac1, and their effector IQ-GAP1 as molecular switches for cadherin-mediated cell-cell adhesion
    • Kuroda S, Fukata M, Nakagawa M, Kaibuchi K. 1999. Cdc42, Rac1, and their effector IQ-GAP1 as molecular switches for cadherin-mediated cell-cell adhesion. Biochem. Biophys. Res. Commun. 262:1-6
    • (1999) Biochem. Biophys. Res. Commun. , vol.262 , pp. 1-6
    • Kuroda, S.1    Fukata, M.2    Nakagawa, M.3    Kaibuchi, K.4
  • 68
    • 0036837872 scopus 로고    scopus 로고
    • Cytosolic retention of phosphorylated extracellular signal-regulated kinase and a Rho-associated kinase-mediated signal impair expression of p21(Cip1/Waf1) in phorbol 12-myristate-13-acetate-induced apoptotic cells
    • Lai JM, Wu S, Huang DY, Chang ZF. 2002. Cytosolic retention of phosphorylated extracellular signal-regulated kinase and a Rho-associated kinase-mediated signal impair expression of p21(Cip1/Waf1) in phorbol 12-myristate-13-acetate-induced apoptotic cells. Mol. Cell Biol. 22:7581-92
    • (2002) Mol. Cell Biol. , vol.22 , pp. 7581-7592
    • Lai, J.M.1    Wu, S.2    Huang, D.Y.3    Chang, Z.F.4
  • 69
    • 0036134932 scopus 로고    scopus 로고
    • Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases
    • Lambeth JD. 2002. Nox/Duox family of nicotinamide adenine dinucleotide (phosphate) oxidases. Curr. Opin. Hematol. 9:11-17
    • (2002) Curr. Opin. Hematol. , vol.9 , pp. 11-17
    • Lambeth, J.D.1
  • 70
    • 0030040750 scopus 로고    scopus 로고
    • Protein kinase a phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes
    • Lang P, Gesbert F, Delespine-Carmagnat M, Stancou R, Pouchelet M, Bertoglio J. 1996. Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes. EMBO J. 15:510-19
    • (1996) EMBO J. , vol.15 , pp. 510-519
    • Lang, P.1    Gesbert, F.2    Delespine-Carmagnat, M.3    Stancou, R.4    Pouchelet, M.5    Bertoglio, J.6
  • 71
    • 0346461418 scopus 로고    scopus 로고
    • MgcRacGAP regulates cortical activity through RhoA during cytokinesis
    • Lee JS, Kamijo K, Ohara N, Kitamura T, Miki T. 2004. MgcRacGAP regulates cortical activity through RhoA during cytokinesis. Exp. Cell Res. 293:275-82
    • (2004) Exp. Cell Res. , vol.293 , pp. 275-282
    • Lee, J.S.1    Kamijo, K.2    Ohara, N.3    Kitamura, T.4    Miki, T.5
  • 72
    • 0041352963 scopus 로고    scopus 로고
    • Directional sensing requires G beta gamma-mediated PAK1 and PIX alpha-dependent activation of Cdc42
    • Li Z, Hannigan M, Mo Z, Liu B, Lu W, et al. 2003. Directional sensing requires G beta gamma-mediated PAK1 and PIX alpha-dependent activation of Cdc42. Cell 114:215-27
    • (2003) Cell , vol.114 , pp. 215-227
    • Li, Z.1    Hannigan, M.2    Mo, Z.3    Liu, B.4    Lu, W.5
  • 73
    • 0000202186 scopus 로고    scopus 로고
    • A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity
    • Lin D, Edwards AS, Fawcett JP, Mbamalu G, Scott JD, Pawson T. 2000. A mammalian PAR-3-PAR-6 complex implicated in Cdc42/Rac1 and aPKC signalling and cell polarity. Nat. Cell Biol. 2:540-47
    • (2000) Nat. Cell Biol. , vol.2 , pp. 540-547
    • Lin, D.1    Edwards, A.S.2    Fawcett, J.P.3    Mbamalu, G.4    Scott, J.D.5    Pawson, T.6
  • 74
    • 0032581530 scopus 로고    scopus 로고
    • Role of citron kinase as a target of the small GTPase Rho in cytokinesis
    • Madaule P, Eda M, Watanabe N, Fujisawa K, Matsuoka T, et al. 1998. Role of citron kinase as a target of the small GTPase Rho in cytokinesis. Nature 394:491-4
    • (1998) Nature , vol.394 , pp. 491-494
    • Madaule, P.1    Eda, M.2    Watanabe, N.3    Fujisawa, K.4    Matsuoka, T.5
  • 75
    • 0036667233 scopus 로고    scopus 로고
    • Rho1 interacts with p120ctn and alpha-catenin, and regulates cadherin-based adherens junction components in Drosophila
    • Magie CR, Pinto-Santini D, Parkhurst SM. 2002. Rho1 interacts with p120ctn and alpha-catenin, and regulates cadherin-based adherens junction components in Drosophila. Development 129:3771-82
    • (2002) Development , vol.129 , pp. 3771-3782
    • Magie, C.R.1    Pinto-Santini, D.2    Parkhurst, S.M.3
  • 76
    • 3142674246 scopus 로고    scopus 로고
    • The Rac exchange factor Tiam1 is required for the establishment and maintenance of cadherin-based adhesions
    • Malliri A, van Es S, Huveneers S, Collard JG. 2004. The Rac exchange factor Tiam1 is required for the establishment and maintenance of cadherin-based adhesions. J. Biol. Chem. 279:30092-98
    • (2004) J. Biol. Chem. , vol.279 , pp. 30092-30098
    • Malliri, A.1    Van Es, S.2    Huveneers, S.3    Collard, J.G.4
  • 78
    • 0031917782 scopus 로고    scopus 로고
    • Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells
    • Matsumura F, Ono S, Yamakita Y, Totsukawa G, Yamashiro S. 1998. Specific localization of serine 19 phosphorylated myosin II during cell locomotion and mitosis of cultured cells. J. Cell Biol. 140:119-29
    • (1998) J. Cell Biol. , vol.140 , pp. 119-129
    • Matsumura, F.1    Ono, S.2    Yamakita, Y.3    Totsukawa, G.4    Yamashiro, S.5
  • 79
    • 0041327718 scopus 로고    scopus 로고
    • Leading the way: Directional sensing through phosphatidylinositol 3-kinase and other signaling pathways
    • Merlot S, Firtel RA. 2003. Leading the way: directional sensing through phosphatidylinositol 3-kinase and other signaling pathways. J. Cell Sci. 116:3471-18
    • (2003) J. Cell Sci. , vol.116 , pp. 3471-3518
    • Merlot, S.1    Firtel, R.A.2
  • 81
    • 2642579936 scopus 로고    scopus 로고
    • Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex
    • Millard TH, Sharp SJ, Machesky LM. 2004. Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex. Biochem. J. 380:1-17
    • (2004) Biochem. J. , vol.380 , pp. 1-17
    • Millard, T.H.1    Sharp, S.J.2    Machesky, L.M.3
  • 82
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden A, Lin A, Claret FX, Abo A, Karin M. 1995. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147-57
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.X.3    Abo, A.4    Karin, M.5
  • 83
    • 0038737042 scopus 로고    scopus 로고
    • Actin dynamics control SRF activity by regulation of its coactivator MAL
    • Miralles F, Posern G, Zaromytidou AI, Treisman R. 2003. Actin dynamics control SRF activity by regulation of its coactivator MAL. Cell 113:329-42
    • (2003) Cell , vol.113 , pp. 329-342
    • Miralles, F.1    Posern, G.2    Zaromytidou, A.I.3    Treisman, R.4
  • 84
    • 0344393408 scopus 로고    scopus 로고
    • Regulation of MAP kinase signaling modules by scaffold proteins in mammals
    • Morrison DK, Davis RJ. 2003. Regulation of MAP kinase signaling modules by scaffold proteins in mammals. Annu. Rev. Cell Dev. Biol. 19:91-118
    • (2003) Annu. Rev. Cell Dev. Biol. , vol.19 , pp. 91-118
    • Morrison, D.K.1    Davis, R.J.2
  • 85
    • 0742289586 scopus 로고    scopus 로고
    • Microtubule organization and function in epithelial cells
    • Musch A. 2004. Microtubule organization and function in epithelial cells. Traffic 5:1-9
    • (2004) Traffic , vol.5 , pp. 1-9
    • Musch, A.1
  • 86
    • 13144258753 scopus 로고    scopus 로고
    • A new look at Rho GTPases in cell cycle: Role in kinetochore-microtubule attachment
    • Narumiya S, Oceguera-Yanez F, Yasuda S. 2004. A new look at Rho GTPases in cell cycle: role in kinetochore-microtubule attachment. Cell Cycle 3:855-57
    • (2004) Cell Cycle , vol.3 , pp. 855-857
    • Narumiya, S.1    Oceguera-Yanez, F.2    Yasuda, S.3
  • 87
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes CD, Hall A. 1999. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144:1235-44
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 88
    • 1542286233 scopus 로고    scopus 로고
    • Positive role of IQGAP1, an effector of Rac1, in actin-meshwork formation at sites of cell-cell contact
    • Noritake J, Fukata M, Sato K, Nakagawa M, Watanabe T, et al. 2004. Positive role of IQGAP1, an effector of Rac1, in actin-meshwork formation at sites of cell-cell contact. Mol. Biol. Cell 15:1065-76
    • (2004) Mol. Biol. Cell , vol.15 , pp. 1065-1076
    • Noritake, J.1    Fukata, M.2    Sato, K.3    Nakagawa, M.4    Watanabe, T.5
  • 90
    • 0034602959 scopus 로고    scopus 로고
    • Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop
    • Ohashi K, Nagata K, Maekawa M, Ishizaki T, Narumiya S, Mizuno K. 2000. Rho-associated kinase ROCK activates LIM-kinase 1 by phosphorylation at threonine 508 within the activation loop. J. Biol. Chem. 275:3577-82
    • (2000) J. Biol. Chem. , vol.275 , pp. 3577-3582
    • Ohashi, K.1    Nagata, K.2    Maekawa, M.3    Ishizaki, T.4    Narumiya, S.5    Mizuno, K.6
  • 91
    • 0033058184 scopus 로고    scopus 로고
    • Rho guanine dissociation inhibitors: Pivotal molecules in cellular signalling
    • Olofsson B. 1999. Rho guanine dissociation inhibitors: pivotal molecules in cellular signalling. Cell Signal 11:545-54
    • (1999) Cell Signal , vol.11 , pp. 545-554
    • Olofsson, B.1
  • 92
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson MF, Ashworth A, Hall A. 1995. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 269:1270-72
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 93
    • 0032537819 scopus 로고    scopus 로고
    • Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1
    • Olson MF, Paterson HF, Marshall CJ. 1998. Signals from Ras and Rho GTPases interact to regulate expression of p21Waf1/Cip1. Nature 394:295-99
    • (1998) Nature , vol.394 , pp. 295-299
    • Olson, M.F.1    Paterson, H.F.2    Marshall, C.J.3
  • 94
    • 0034907213 scopus 로고    scopus 로고
    • Dia mediates Rho-regulated formation and orientation of stable microtubules
    • Palazzo AF, Cook TA, Alberts AS, Gundersen GG. 2001. mDia mediates Rho-regulated formation and orientation of stable microtubules. Nat. Cell Biol. 3:723-29
    • (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
  • 96
    • 1642276423 scopus 로고    scopus 로고
    • Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition
    • Peterson FC, Penkert RR, Volkman BF, Prehoda KE. 2004. Cdc42 regulates the Par-6 PDZ domain through an allosteric CRIB-PDZ transition. Mol. Cell 13:665-76
    • (2004) Mol. Cell , vol.13 , pp. 665-676
    • Peterson, F.C.1    Penkert, R.R.2    Volkman, B.F.3    Prehoda, K.E.4
  • 97
    • 0037385561 scopus 로고    scopus 로고
    • A polarity complex of mPar6 and atypical PKC binds, phosphorylates and regulates mammalian Lg1
    • Plant PJ, Fawcett JP, Lin DC, Holdorf AD, Binns K, et al. 2003. A polarity complex of mPar6 and atypical PKC binds, phosphorylates and regulates mammalian Lg1. Nat. Cell Biol. 5:301-8
    • (2003) Nat. Cell Biol. , vol.5 , pp. 301-308
    • Plant, P.J.1    Fawcett, J.P.2    Lin, D.C.3    Holdorf, A.D.4    Binns, K.5
  • 98
    • 0037459075 scopus 로고    scopus 로고
    • Cellular motility driven by assembly and disassembly of actin filaments
    • Pollard TD, Borisy GG. 2003. Cellular motility driven by assembly and disassembly of actin filaments. Cell 112:453-65
    • (2003) Cell , vol.112 , pp. 453-465
    • Pollard, T.D.1    Borisy, G.G.2
  • 99
    • 0033200353 scopus 로고    scopus 로고
    • A putative exchange factor for Rho1 GTPase is required for initiation of cytokinesis in Drosophila
    • Prokopenko SN, Brumby A, O'Keefe L, Prior L, He Y, et al. 1999. A putative exchange factor for Rho1 GTPase is required for initiation of cytokinesis in Drosophila. Genes Dev. 13:2301-14
    • (1999) Genes Dev. , vol.13 , pp. 2301-2314
    • Prokopenko, S.N.1    Brumby, A.2    O'Keefe, L.3    Prior, L.4    He, Y.5
  • 100
    • 0032841725 scopus 로고    scopus 로고
    • Activation of the small GTPaseCdc42 by the inflammatory cytokines TNF-α and IL-1, and by the Epstein-Barr virus transforming protein LMP1
    • Puls A, Eliopoulos AG, Nobes CD, Bridges T, Young LS, Hall A. 1999. Activation of the small GTPaseCdc42 by the inflammatory cytokines TNF-α and IL-1, and by the Epstein-Barr virus transforming protein LMP1. J. Cell Sci. 112:2983-92
    • (1999) J. Cell Sci. , vol.112 , pp. 2983-2992
    • Puls, A.1    Eliopoulos, A.G.2    Nobes, C.D.3    Bridges, T.4    Young, L.S.5    Hall, A.6
  • 101
    • 0032891511 scopus 로고    scopus 로고
    • Dcdc42 acts in TGF-beta signaling during Drosophila morphogenesis: Distinct roles for the Drac1/JNK and Dcdc42/TGF-beta cascades in cytoskeletal regulation
    • Ricos MG, Harden N, Sem KP, Lim L, Chia W. 1999. Dcdc42 acts in TGF-beta signaling during Drosophila morphogenesis: distinct roles for the Drac1/JNK and Dcdc42/TGF-beta cascades in cytoskeletal regulation. J. Cell Sci. 112(Pt 8):1225-35
    • (1999) J. Cell Sci. , vol.112 , Issue.PART 8 , pp. 1225-1235
    • Ricos, M.G.1    Harden, N.2    Sem, K.P.3    Lim, L.4    Chia, W.5
  • 103
    • 0038024241 scopus 로고    scopus 로고
    • Rocks: Multifunctional kinases in cell behaviour
    • Riento K, Ridley AJ. 2003. Rocks: multifunctional kinases in cell behaviour. Nat. Rev. Mol. Cell Biol. 4:446-56
    • (2003) Nat. Rev. Mol. Cell Biol. , vol.4 , pp. 446-456
    • Riento, K.1    Ridley, A.J.2
  • 105
    • 0041440180 scopus 로고    scopus 로고
    • Nuclear translocation of LIM kinase mediates Rho-Rho kinase regulation of cyclin D1 expression
    • Roovers K, Klein EA, Castagnino P, Assoian RK. 2003. Nuclear translocation of LIM kinase mediates Rho-Rho kinase regulation of cyclin D1 expression. Dev. Cell 5:273-84
    • (2003) Dev. Cell , vol.5 , pp. 273-284
    • Roovers, K.1    Klein, E.A.2    Castagnino, P.3    Assoian, R.K.4
  • 106
    • 2042544799 scopus 로고    scopus 로고
    • Myosin II-dependent cortical movement is required for centrosome separation and positioning during mitotic spindle assembly
    • Rosenblatt J, Cramer LP, Baum B, McGee KM. 2004. Myosin II-dependent cortical movement is required for centrosome separation and positioning during mitotic spindle assembly. Cell 117:361-72
    • (2004) Cell , vol.117 , pp. 361-372
    • Rosenblatt, J.1    Cramer, L.P.2    Baum, B.3    McGee, K.M.4
  • 107
    • 0042354574 scopus 로고    scopus 로고
    • Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis
    • Sahai E, Marshall CJ. 2003. Differing modes of tumour cell invasion have distinct requirements for Rho/ROCK signalling and extracellular proteolysis. Nat. Cell Biol. 5:711-19
    • (2003) Nat. Cell Biol. , vol.5 , pp. 711-719
    • Sahai, E.1    Marshall, C.J.2
  • 108
    • 0035865137 scopus 로고    scopus 로고
    • Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility
    • Sahai E, Olson MF, Marshall CJ. 2001. Cross-talk between Ras and Rho signalling pathways in transformation favours proliferation and increased motility. EMBO J. 20:755-66
    • (2001) EMBO J. , vol.20 , pp. 755-766
    • Sahai, E.1    Olson, M.F.2    Marshall, C.J.3
  • 109
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • Sander EE, van Delft S, ten Klooster JP, Reid T, van der Kammen RA, et al. 1998. Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J. Cell Biol. 143:1385-98
    • (1998) J. Cell Biol. , vol.143 , pp. 1385-1398
    • Sander, E.E.1    Van Delft, S.2    Ten Klooster, J.P.3    Reid, T.4    Van Der Kammen, R.A.5
  • 110
    • 0036644975 scopus 로고    scopus 로고
    • Guanine nucleotide exchange factors for Rho GTPases: Turning on the switch
    • Schmidt A, Hall A. 2002. Guanine nucleotide exchange factors for Rho GTPases: turning on the switch. Genes Dev. 16:1587-609
    • (2002) Genes Dev. , vol.16 , pp. 1587-1609
    • Schmidt, A.1    Hall, A.2
  • 111
    • 4344594485 scopus 로고    scopus 로고
    • The sequential activity of the GTPases Rap1B and Cdc42 determines neuronal polarity
    • Schwamborn JC, Puschel AW. 2004. The sequential activity of the GTPases Rap1B and Cdc42 determines neuronal polarity. Nat. Neurosci. 7:923-29
    • (2004) Nat. Neurosci. , vol.7 , pp. 923-929
    • Schwamborn, J.C.1    Puschel, A.W.2
  • 112
    • 9244249219 scopus 로고    scopus 로고
    • APC and GSK-3beta are involved in mPar3 targeting to the nascent axon and establishment of neuronal polarity
    • Shi SH, Cheng T, Jan LY, Jan YN. 2004. APC and GSK-3beta are involved in mPar3 targeting to the nascent axon and establishment of neuronal polarity. Curr. Biol. 14:2025-32
    • (2004) Curr. Biol. , vol.14 , pp. 2025-2032
    • Shi, S.H.1    Cheng, T.2    Jan, L.Y.3    Jan, Y.N.4
  • 113
    • 0037428076 scopus 로고    scopus 로고
    • Hippocampal neuronal polarity specified by spatially localized mPar3/mPar6 and PI 3-kinase activity
    • Shi SH, Jan LY, Jan YN. 2003. Hippocampal neuronal polarity specified by spatially localized mPar3/mPar6 and PI 3-kinase activity. Cell 112:63-75
    • (2003) Cell , vol.112 , pp. 63-75
    • Shi, S.H.1    Jan, L.Y.2    Jan, Y.N.3
  • 114
    • 0029157469 scopus 로고
    • Role for the Rho-family GTPase Cdc42 in yeast mating-pheromone signal pathway
    • Simon MN, De Virgilio C, Souza B, Pringle JR, Abo A, Reed SI. 1995. Role for the Rho-family GTPase Cdc42 in yeast mating-pheromone signal pathway. Nature 376:702-5
    • (1995) Nature , vol.376 , pp. 702-705
    • Simon, M.N.1    De Virgilio, C.2    Souza, B.3    Pringle, J.R.4    Abo, A.5    Reed, S.I.6
  • 116
    • 0035911955 scopus 로고    scopus 로고
    • Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures
    • Suzuki A, Yamanaka T, Hirose T, Manabe N, Mizuno K, et al. 2001. Atypical protein kinase C is involved in the evolutionarily conserved par protein complex and plays a critical role in establishing epithelia-specific junctional structures. J. Cell Biol. 152:1183-96
    • (2001) J. Cell Biol. , vol.152 , pp. 1183-1196
    • Suzuki, A.1    Yamanaka, T.2    Hirose, T.3    Manabe, N.4    Mizuno, K.5
  • 117
    • 0033620689 scopus 로고    scopus 로고
    • Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia
    • Svitkina TM, Borisy GG. 1999. Arp2/3 complex and actin depolymerizing factor/cofilin in dendritic organization and treadmilling of actin filament array in lamellipodia. J. Cell Biol. 145:1009-26
    • (1999) J. Cell Biol. , vol.145 , pp. 1009-1026
    • Svitkina, T.M.1    Borisy, G.G.2
  • 119
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells
    • Takaishi K, Sasaki T, Kotani H, Nishioka H, Takai Y. 1997. Regulation of cell-cell adhesion by rac and rho small G proteins in MDCK cells. J. Cell Biol. 139:1047-59
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 120
    • 1442307630 scopus 로고    scopus 로고
    • Molecular mechanism for activation of superoxide-producing NADPH oxidases
    • Takeya R, Sumimoto H. 2003. Molecular mechanism for activation of superoxide-producing NADPH oxidases. Mol. Cell. 16:271-77
    • (2003) Mol. Cell , vol.16 , pp. 271-277
    • Takeya, R.1    Sumimoto, H.2
  • 121
    • 0042991381 scopus 로고    scopus 로고
    • Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases
    • Takeya R, Ueno N, Kami K, Taura M, Kohjima M, et al. 2003. Novel human homologues of p47phox and p67phox participate in activation of superoxide-producing NADPH oxidases. J. Biol. Chem. 278:25234-46
    • (2003) J. Biol. Chem. , vol.278 , pp. 25234-25246
    • Takeya, R.1    Ueno, N.2    Kami, K.3    Taura, M.4    Kohjima, M.5
  • 122
    • 0032473569 scopus 로고    scopus 로고
    • A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways
    • Tapon N, Nagata K, Lamarche N, Hall A. 1998. A new rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways. EMBO J. 17:1395-404
    • (1998) EMBO J. , vol.17 , pp. 1395-1404
    • Tapon, N.1    Nagata, K.2    Lamarche, N.3    Hall, A.4
  • 123
    • 0033615978 scopus 로고    scopus 로고
    • Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis
    • Tatsumoto T, Xie X, Blumenthal R, Okamoto I, Miki T. 1999. Human ECT2 is an exchange factor for Rho GTPases, phosphorylated in G2/M phases, and involved in cytokinesis. J. Cell Biol. 147:921-28
    • (1999) J. Cell Biol. , vol.147 , pp. 921-928
    • Tatsumoto, T.1    Xie, X.2    Blumenthal, R.3    Okamoto, I.4    Miki, T.5
  • 124
    • 0029913510 scopus 로고    scopus 로고
    • Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. A role for mixed lineage kinase 3/protein-tyrosine kinase 1, a novel member of the mixed lineage kinase family
    • Teramoto H, Coso OA, Miyata H, Igishi T, Miki T, Gutkind JS. 1996. Signaling from the small GTP-binding proteins Rac1 and Cdc42 to the c-Jun N-terminal kinase/stress-activated protein kinase pathway. A role for mixed lineage kinase 3/protein-tyrosine kinase 1, a novel member of the mixed lineage kinase family. J. Biol. Chem. 271:27225-28
    • (1996) J. Biol. Chem. , vol.271 , pp. 27225-27228
    • Teramoto, H.1    Coso, O.A.2    Miyata, H.3    Igishi, T.4    Miki, T.5    Gutkind, J.S.6
  • 126
    • 0036746704 scopus 로고    scopus 로고
    • Actin cable dynamics and Rho/Rock orchestrate a polarized cytoskeletal architecture in the early steps of assembling a stratified epithelium
    • Vaezi A, Bauer C, Vasioukhin V, Fuchs E. 2002. Actin cable dynamics and Rho/Rock orchestrate a polarized cytoskeletal architecture in the early steps of assembling a stratified epithelium. Dev. Cell 3:367-81
    • (2002) Dev. Cell , vol.3 , pp. 367-381
    • Vaezi, A.1    Bauer, C.2    Vasioukhin, V.3    Fuchs, E.4
  • 127
    • 0034695656 scopus 로고    scopus 로고
    • Directed actin polymerization is the driving force for epithelial cell-cell adhesion
    • Vasioukhin V, Bauer C, Yin M, Fuchs E. 2000. Directed actin polymerization is the driving force for epithelial cell-cell adhesion. Cell 100:209-19
    • (2000) Cell , vol.100 , pp. 209-219
    • Vasioukhin, V.1    Bauer, C.2    Yin, M.3    Fuchs, E.4
  • 128
    • 0037053407 scopus 로고    scopus 로고
    • Rho activity can alter the translation of p27 mRNA and is important for RasV12-induced transformation in a manner dependent on p27 status
    • Vidal A, Millard SS, Miller JP, Koff A. 2002. Rho activity can alter the translation of p27 mRNA and is important for RasV12-induced transformation in a manner dependent on p27 status. J. Biol. Chem. 277:16433-40
    • (2002) J. Biol. Chem. , vol.277 , pp. 16433-16440
    • Vidal, A.1    Millard, S.S.2    Miller, J.P.3    Koff, A.4
  • 131
    • 0344758986 scopus 로고    scopus 로고
    • Regulation of cell polarity and protrusion formation by targeting RhoA for degradation
    • Wang HR, Zhang Y, Ozdamar B, Ogunjimi AA, Alexandrova E, et al. 2003. Regulation of cell polarity and protrusion formation by targeting RhoA for degradation. Science 302:1775-79
    • (2003) Science , vol.302 , pp. 1775-1779
    • Wang, H.R.1    Zhang, Y.2    Ozdamar, B.3    Ogunjimi, A.A.4    Alexandrova, E.5
  • 132
    • 10644281068 scopus 로고    scopus 로고
    • Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration
    • Watanabe T, Wang S, Noritake J, Sato K, Fukata M, et al. 2004. Interaction with IQGAP1 links APC to Rac1, Cdc42, and actin filaments during cell polarization and migration. Dev. Cell 7:871-83
    • (2004) Dev. Cell , vol.7 , pp. 871-883
    • Watanabe, T.1    Wang, S.2    Noritake, J.3    Sato, K.4    Fukata, M.5
  • 133
    • 0031453368 scopus 로고    scopus 로고
    • Ras-stimulated extracellular signal-related kinase 1 and RhoA activities coordinate platelet-derived growth factor-induced G1 progression through the independent regulation of cyclin D1 and p27
    • Weber JD, Hu W, Jefcoat SC Jr, Raben DM, Baldassare JJ. 1997. Ras-stimulated extracellular signal-related kinase 1 and RhoA activities coordinate platelet-derived growth factor-induced G1 progression through the independent regulation of cyclin D1 and p27. J. Biol. Chem. 272:32966-71
    • (1997) J. Biol. Chem. , vol.272 , pp. 32966-32971
    • Weber, J.D.1    Hu, W.2    Jefcoat Jr., S.C.3    Raben, D.M.4    Baldassare, J.J.5
  • 134
    • 1542319943 scopus 로고    scopus 로고
    • Activation of type I phosphatidylinositol 4-phosphate 5-kinase isoforms by the Rho GTPases, RhoA, Rac1, and Cdc42
    • Weernink PA, Meletiadis K, Hommeltenberg S, Hinz M, Ishihara H, et al. 2004. Activation of type I phosphatidylinositol 4-phosphate 5-kinase isoforms by the Rho GTPases, RhoA, Rac1, and Cdc42. J. Biol. Chem. 279:7840-49
    • (2004) J. Biol. Chem. , vol.279 , pp. 7840-7849
    • Weernink, P.A.1    Meletiadis, K.2    Hommeltenberg, S.3    Hinz, M.4    Ishihara, H.5
  • 136
    • 4444360489 scopus 로고    scopus 로고
    • EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration
    • Wen Y, Eng CH, Schmoranzer J, Cabrera-Poch N, Morris EJ, et al. 2004. EB1 and APC bind to mDia to stabilize microtubules downstream of Rho and promote cell migration. Nat. Cell Biol. 6:820-30
    • (2004) Nat. Cell Biol. , vol.6 , pp. 820-830
    • Wen, Y.1    Eng, C.H.2    Schmoranzer, J.3    Cabrera-Poch, N.4    Morris, E.J.5
  • 137
    • 0031026132 scopus 로고    scopus 로고
    • Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways
    • Westwick JK, Lambert QT, Clark GJ, Symons M, Van Aelst L, et al. 1997. Rac regulation of transformation, gene expression, and actin organization by multiple, PAK-independent pathways. Mol. Cell Biol. 17:1324-35
    • (1997) Mol. Cell Biol. , vol.17 , pp. 1324-1335
    • Westwick, J.K.1    Lambert, Q.T.2    Clark, G.J.3    Symons, M.4    Van Aelst, L.5
  • 138
    • 0035178210 scopus 로고    scopus 로고
    • Cell motility: Can Rho GTPases and microtubules point the way?
    • Wittmann T, Waterman-Storer CM. 2001. Cell motility: Can Rho GTPases and microtubules point the way? J. Cell Sci. 114:3795-803
    • (2001) J. Cell Sci. , vol.114 , pp. 3795-3803
    • Wittmann, T.1    Waterman-Storer, C.M.2
  • 139
    • 0038037737 scopus 로고    scopus 로고
    • RhoA and ROCK promote migration by limiting membrane protrusions
    • Worthylake RA, Burridge K. 2003. RhoA and ROCK promote migration by limiting membrane protrusions. J. Biol. Chem. 278:13578-84
    • (2003) J. Biol. Chem. , vol.278 , pp. 13578-13584
    • Worthylake, R.A.1    Burridge, K.2
  • 140
    • 0037439170 scopus 로고    scopus 로고
    • POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis
    • Xu Z, Kukekov NV, Greene LA. 2003. POSH acts as a scaffold for a multiprotein complex that mediates JNK activation in apoptosis. EMBO J. 22:252-61
    • (2003) EMBO J. , vol.22 , pp. 252-261
    • Xu, Z.1    Kukekov, N.V.2    Greene, L.A.3
  • 141
    • 0027280575 scopus 로고
    • ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle
    • Yamamoto M, Marui N, Sakai T, Morii N, Kozaki S, et al. 1993. ADP-ribosylation of the rhoA gene product by botulinum C3 exoenzyme causes Swiss 3T3 cells to accumulate in the G1 phase of the cell cycle. Oncogene 8:1449-55
    • (1993) Oncogene , vol.8 , pp. 1449-1455
    • Yamamoto, M.1    Marui, N.2    Sakai, T.3    Morii, N.4    Kozaki, S.5
  • 142
    • 0038032917 scopus 로고    scopus 로고
    • Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity
    • Yamanaka T, Horikoshi Y, Sugiyama Y, Ishiyama C, Suzuki A, et al. 2003. Mammalian Lgl forms a protein complex with PAR-6 and aPKC independently of PAR-3 to regulate epithelial cell polarity. Curr. Biol. 13:734-43
    • (2003) Curr. Biol. , vol.13 , pp. 734-743
    • Yamanaka, T.1    Horikoshi, Y.2    Sugiyama, Y.3    Ishiyama, C.4    Suzuki, A.5
  • 143
    • 0034874862 scopus 로고    scopus 로고
    • PAR-6 regulates aPKC activity in a novel way and mediates cell-cell contact-induced formation of the epithelial junctional complex
    • Yamanaka T, Horikoshi Y, Suzuki A, Sugiyama Y, Kitamura K, et al. 2001. PAR-6 regulates aPKC activity in a novel way and mediates cell-cell contact-induced formation of the epithelial junctional complex. Genes Cells 6:721-31
    • (2001) Genes Cells , vol.6 , pp. 721-731
    • Yamanaka, T.1    Horikoshi, Y.2    Suzuki, A.3    Sugiyama, Y.4    Kitamura, K.5
  • 144
    • 0038247927 scopus 로고    scopus 로고
    • Citron kinase, a Rho-dependent kinase, induces di-phosphorylation of regulatory light chain of myosin II
    • Yamashiro S, Totsukawa G, Yamakita Y, Sasaki Y, Madaule P, et al. 2003. Citron kinase, a Rho-dependent kinase, induces di-phosphorylation of regulatory light chain of myosin II. Mol. Biol. Cell 14:1745-56
    • (2003) Mol. Biol. Cell , vol.14 , pp. 1745-1756
    • Yamashiro, S.1    Totsukawa, G.2    Yamakita, Y.3    Sasaki, Y.4    Madaule, P.5
  • 145
    • 1942455757 scopus 로고    scopus 로고
    • Cdc42 and mDia3 regulate microtubule attachment to kinetochores
    • Yasuda S, Oceguera-Yanez F, Kato T, Okamoto M, Yonemura S, et al. 2004. Cdc42 and mDia3 regulate microtubule attachment to kinetochores. Nature 428:767-71
    • (2004) Nature , vol.428 , pp. 767-771
    • Yasuda, S.1    Oceguera-Yanez, F.2    Kato, T.3    Okamoto, M.4    Yonemura, S.5
  • 147
    • 12844272106 scopus 로고    scopus 로고
    • β1-integrin orients epithelial polarity via Rac1 and laminin
    • Yu W, Datta A, Leroy P, O'Brien LE, Mak G, et al. 2005. β1-integrin orients epithelial polarity via Rac1 and laminin. Mol. Biol. Cell 16:433-45
    • (2005) Mol. Biol. Cell , vol.16 , pp. 433-445
    • Yu, W.1    Datta, A.2    Leroy, P.3    O'Brien, L.E.4    Mak, G.5
  • 149
    • 0035861749 scopus 로고    scopus 로고
    • Cdc42 interacts with the exocyst and regulates polarized secretion
    • Zhang X, Bi E, Novick P, Du L, Kozminski KG, et al. 2001. Cdc42 interacts with the exocyst and regulates polarized secretion. J. Biol. Chem. 276:46745-50
    • (2001) J. Biol. Chem. , vol.276 , pp. 46745-46750
    • Zhang, X.1    Bi, E.2    Novick, P.3    Du, L.4    Kozminski, K.G.5
  • 150
    • 0028338545 scopus 로고
    • Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85
    • Zheng Y, Bagrodia S, Cerione RA. 1994. Activation of phosphoinositide 3-kinase activity by Cdc42Hs binding to p85. J. Biol. Chem. 269:18727-30
    • (1994) J. Biol. Chem. , vol.269 , pp. 18727-18730
    • Zheng, Y.1    Bagrodia, S.2    Cerione, R.A.3
  • 151
    • 1642391823 scopus 로고    scopus 로고
    • Formin-induced nucleation of actin filaments
    • Zigmond SH. 2004. Formin-induced nucleation of actin filaments. Curr. Opin. Cell Biol. 16:99-105
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 99-105
    • Zigmond, S.H.1


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