메뉴 건너뛰기




Volumn 186, Issue , 2008, Pages 431-460

Chemical inhibition through conformational stabilization of Rho GTPase effectors

Author keywords

[No Author keywords available]

Indexed keywords

CARBAZOLE DERIVATIVE; NEURAL WISKOTT ALDRICH SYNDROME PROTEIN; P21 ACTIVATED KINASE; PROPANOLAMINE DERIVATIVE; RHO GUANINE NUCLEOTIDE BINDING PROTEIN; SIGNAL TRANSDUCING ADAPTOR PROTEIN; WISKOSTATIN;

EID: 49049114363     PISSN: 01712004     EISSN: 18650325     Source Type: Book Series    
DOI: 10.1007/978-3-540-72843-6_18     Document Type: Article
Times cited : (7)

References (152)
  • 2
    • 0034697303 scopus 로고    scopus 로고
    • Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1
    • Adam L, Vadlamudi R, Mandal M, Chernoff J, Kumar R (2000) Regulation of microfilament reorganization and invasiveness of breast cancer cells by kinase dead p21-activated kinase-1. J Biol Chem 275:12041-12050
    • (2000) J Biol Chem , vol.275 , pp. 12041-12050
    • Adam, L.1    Vadlamudi, R.2    Mandal, M.3    Chernoff, J.4    Kumar, R.5
  • 3
    • 0035951824 scopus 로고    scopus 로고
    • Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain
    • Alberts AS (2001) Identification of a carboxyl-terminal diaphanous-related formin homology protein autoregulatory domain. J Biol Chem 276:2824-2830
    • (2001) J Biol Chem , vol.276 , pp. 2824-2830
    • Alberts, A.S.1
  • 4
    • 0032502680 scopus 로고    scopus 로고
    • Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7
    • Alberts AS, Bouquin N, Johnston LH, Treisman R (1998) Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7. J Biol Chem 273:8616-8622
    • (1998) J Biol Chem , vol.273 , pp. 8616-8622
    • Alberts, A.S.1    Bouquin, N.2    Johnston, L.H.3    Treisman, R.4
  • 8
    • 0037162288 scopus 로고    scopus 로고
    • Pak1 phosphorylation on t212 affects microtubules in cells undergoing mitosis
    • Banerjee M, Worth D, Prowse DM, Nikolic M (2002) Pak1 phosphorylation on t212 affects microtubules in cells undergoing mitosis. Curr Biol 12:1233-1239
    • (2002) Curr Biol , vol.12 , pp. 1233-1239
    • Banerjee, M.1    Worth, D.2    Prowse, D.M.3    Nikolic, M.4
  • 9
    • 33845730371 scopus 로고    scopus 로고
    • The Dbs PH domain contributes independently to membrane targeting and regulation of guanine nucleotide-exchange activity
    • Baumeister MA, Rossman KL, Sondek J, Lemmon MA (2006) The Dbs PH domain contributes independently to membrane targeting and regulation of guanine nucleotide-exchange activity. Biochem J 400:563-572
    • (2006) Biochem J , vol.400 , pp. 563-572
    • Baumeister, M.A.1    Rossman, K.L.2    Sondek, J.3    Lemmon, M.A.4
  • 10
    • 27744437045 scopus 로고    scopus 로고
    • Production and use of a cell permeable inhibitor of group A Paks (TAT-PID) to analyze signal transduction
    • Beeser A, Chernoff J (2005) Production and use of a cell permeable inhibitor of group A Paks (TAT-PID) to analyze signal transduction. Methods 37:203-207
    • (2005) Methods , vol.37 , pp. 203-207
    • Beeser, A.1    Chernoff, J.2
  • 11
    • 17344369363 scopus 로고    scopus 로고
    • A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: Evidence for conserved function in oogenesis and implications for human sterility
    • Bione S, Sala C, Manzini C, Arrigo G, Zuffardi O, Banfi S, Borsani G, Jonveaux P, Philippe C, Zuccotti M, Ballabio A, Toniolo D (1998) A human homologue of the Drosophila melanogaster diaphanous gene is disrupted in a patient with premature ovarian failure: evidence for conserved function in oogenesis and implications for human sterility. Am J Hum Genet 62:533-541
    • (1998) Am J Hum Genet , vol.62 , pp. 533-541
    • Bione, S.1    Sala, C.2    Manzini, C.3    Arrigo, G.4    Zuffardi, O.5    Banfi, S.6    Borsani, G.7    Jonveaux, P.8    Philippe, C.9    Zuccotti, M.10    Ballabio, A.11    Toniolo, D.12
  • 12
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch GM (2003) Biology of the p21-activated kinases. Annu Rev Biochem 72:743-781
    • (2003) Annu Rev Biochem , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 14
    • 34249018367 scopus 로고    scopus 로고
    • GEFs and GAPs: Critical elements in the control of small G proteins
    • Bos JL, Rehmann H, Wittinghofer A (2007) GEFs and GAPs: critical elements in the control of small G proteins. Cell 129:865-877
    • (2007) Cell , vol.129 , pp. 865-877
    • Bos, J.L.1    Rehmann, H.2    Wittinghofer, A.3
  • 15
    • 33845868501 scopus 로고    scopus 로고
    • Evolution of the Rho family of ras-like GTPases in eukaryotes
    • Boureux A, Vignal E, Faure S, Fort P (2007) Evolution of the Rho family of ras-like GTPases in eukaryotes. Mol Biol Evol 24:203-216
    • (2007) Mol Biol Evol , vol.24 , pp. 203-216
    • Boureux, A.1    Vignal, E.2    Faure, S.3    Fort, P.4
  • 17
    • 2642553258 scopus 로고    scopus 로고
    • Target identification in chemical genetics: The (often) missing link
    • Burdine L, Kodadek T (2004) Target identification in chemical genetics: the (often) missing link. Chem Biol 11:593-597
    • (2004) Chem Biol , vol.11 , pp. 593-597
    • Burdine, L.1    Kodadek, T.2
  • 21
    • 33745502220 scopus 로고    scopus 로고
    • In vitro study of nuclear assembly and nuclear import using Xenopus egg extracts
    • Chan RC, Forbes DI (2006) In vitro study of nuclear assembly and nuclear import using Xenopus egg extracts. Methods Mol Biol 322:289-300
    • (2006) Methods Mol Biol , vol.322 , pp. 289-300
    • Chan, R.C.1    Forbes, D.I.2
  • 23
    • 0030806901 scopus 로고    scopus 로고
    • Characterization of spindle assembly checkpoint in Xenopus egg extracts
    • Chen RH, Murray A (1997) Characterization of spindle assembly checkpoint in Xenopus egg extracts. Methods Enzymol 283:572-584
    • (1997) Methods Enzymol , vol.283 , pp. 572-584
    • Chen, R.H.1    Murray, A.2
  • 24
    • 0034644473 scopus 로고    scopus 로고
    • Signaling to chromatin through histone modifications
    • Cheung P, Allis CD, Sassone-Corsi P (2000) Signaling to chromatin through histone modifications. Cell 103:263-271
    • (2000) Cell , vol.103 , pp. 263-271
    • Cheung, P.1    Allis, C.D.2    Sassone-Corsi, P.3
  • 25
    • 0035907296 scopus 로고    scopus 로고
    • The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity
    • Chong C, Tan L, Lim L, Manser E (2001) The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity. J Biol Chem 276:17347-17353
    • (2001) J Biol Chem , vol.276 , pp. 17347-17353
    • Chong, C.1    Tan, L.2    Lim, L.3    Manser, E.4
  • 26
    • 0020533805 scopus 로고
    • Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization
    • Cooper JA, Walker SB, Pollard TD (1983) Pyrene actin: documentation of the validity of a sensitive assay for actin polymerization. J Muscle Res Cell Motil 4:253-262
    • (1983) J Muscle Res Cell Motil , vol.4 , pp. 253-262
    • Cooper, J.A.1    Walker, S.B.2    Pollard, T.D.3
  • 27
    • 0036854328 scopus 로고    scopus 로고
    • The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization
    • Copeland JW, Treisman R (2002) The diaphanous-related formin mDia1 controls serum response factor activity through its effects on actin polymerization. Mol Biol Cell 13:4088-4099
    • (2002) Mol Biol Cell , vol.13 , pp. 4088-4099
    • Copeland, J.W.1    Treisman, R.2
  • 28
    • 0041631073 scopus 로고    scopus 로고
    • P21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD
    • Cotteret S, Jaffer ZM, Beeser A, Chernoff J (2003) p21-Activated kinase 5 (Pak5) localizes to mitochondria and inhibits apoptosis by phosphorylating BAD. Mol Cell Biol 23:5526-5539
    • (2003) Mol Cell Biol , vol.23 , pp. 5526-5539
    • Cotteret, S.1    Jaffer, Z.M.2    Beeser, A.3    Chernoff, J.4
  • 29
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies SP, Reddy H, Caivano M, Cohen P (2000) Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem J 351:95-105
    • (2000) Biochem J , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 31
    • 33745480959 scopus 로고    scopus 로고
    • Study of apoptosis in vitro using the Xenopus egg extract reconstitution system
    • Deming P, Kornbluth S (2006) Study of apoptosis in vitro using the Xenopus egg extract reconstitution system. Methods Mol Biol 322:379-393
    • (2006) Methods Mol Biol , vol.322 , pp. 379-393
    • Deming, P.1    Kornbluth, S.2
  • 32
    • 0036333485 scopus 로고    scopus 로고
    • Rac-PAK signaling stimulates extracellular signal-regulated kinase (ERK) activation by regulating formation of MEK1-ERK complexes
    • Eblen ST, Slack JK, Weber MJ, Catling AD (2002) Rac-PAK signaling stimulates extracellular signal-regulated kinase (ERK) activation by regulating formation of MEK1-ERK complexes. Mol Cell Biol 22:6023-6033
    • (2002) Mol Cell Biol , vol.22 , pp. 6023-6033
    • Eblen, S.T.1    Slack, J.K.2    Weber, M.J.3    Catling, A.D.4
  • 33
    • 0033194037 scopus 로고    scopus 로고
    • Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics
    • Edwards DC, Sanders LC, Bokoch GM, Gill GN (1999) Activation of LIM-kinase by Pak1 couples Rac/Cdc42 GTPase signalling to actin cytoskeletal dynamics. Nat Cell Biol 1:253-259
    • (1999) Nat Cell Biol , vol.1 , pp. 253-259
    • Edwards, D.C.1    Sanders, L.C.2    Bokoch, G.M.3    Gill, G.N.4
  • 35
    • 33646864565 scopus 로고    scopus 로고
    • Staying in shape with formins
    • Faix J, Grosse R (2006) Staying in shape with formins. Dev Cell 10:693-706
    • (2006) Dev Cell , vol.10 , pp. 693-706
    • Faix, J.1    Grosse, R.2
  • 36
    • 0030830220 scopus 로고    scopus 로고
    • Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins
    • Frost JA, Steen H, Shapiro P, Lewis T, Ahn N, Shaw PE, Cobb MH (1997) Cross-cascade activation of ERKs and ternary complex factors by Rho family proteins. Embo J 16:6426-6438
    • (1997) Embo J , vol.16 , pp. 6426-6438
    • Frost, J.A.1    Steen, H.2    Shapiro, P.3    Lewis, T.4    Ahn, N.5    Shaw, P.E.6    Cobb, M.H.7
  • 37
    • 0029830139 scopus 로고    scopus 로고
    • The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1
    • Galisteo ML, Chernoff J, Su YC, Skolnik EY, Schlessinger J (1996) The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1. J Biol Chem 271:20997-21000
    • (1996) J Biol Chem , vol.271 , pp. 20997-21000
    • Galisteo, M.L.1    Chernoff, J.2    Su, Y.C.3    Skolnik, E.Y.4    Schlessinger, J.5
  • 39
    • 0037341806 scopus 로고    scopus 로고
    • RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase
    • Gasman S, Kalaidzidis Y, Zerial M (2003) RhoD regulates endosome dynamics through Diaphanous-related Formin and Src tyrosine kinase. Nat Cell Biol 5:195-204
    • (2003) Nat Cell Biol , vol.5 , pp. 195-204
    • Gasman, S.1    Kalaidzidis, Y.2    Zerial, M.3
  • 40
    • 33845313646 scopus 로고    scopus 로고
    • PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane
    • Heo WD, Inoue T, Park WS, Kim ML, Park BO, Wandless TJ, Meyer T (2006) PI(3,4,5)P3 and PI(4,5)P2 lipids target proteins with polybasic clusters to the plasma membrane. Science 314:1458-1461
    • (2006) Science , vol.314 , pp. 1458-1461
    • Heo, W.D.1    Inoue, T.2    Park, W.S.3    Kim, M.L.4    Park, B.O.5    Wandless, T.J.6    Meyer, T.7
  • 42
    • 18844438774 scopus 로고    scopus 로고
    • Formin proteins: A domain-based approach
    • Higgs HN (2005) Formin proteins: a domain-based approach. Trends Biochem Sci 30:342-353
    • (2005) Trends Biochem Sci , vol.30 , pp. 342-353
    • Higgs, H.N.1
  • 43
    • 11144281883 scopus 로고    scopus 로고
    • Phylogenetic analysis of the formin homology 2 domain
    • Higgs HN, Peterson KJ (2005) Phylogenetic analysis of the formin homology 2 domain. Mol Biol Cell 16:1-13
    • (2005) Mol Biol Cell , vol.16 , pp. 1-13
    • Higgs, H.N.1    Peterson, K.J.2
  • 44
    • 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, Gygi SP, Kirschner MW (2004) Toca-1 mediates Cdc42-dependent actin nucleation by activating the N-WASP-WIP complex. Cell 118:203-216
    • (2004) Cell , vol.118 , pp. 203-216
    • Ho, H.Y.1    Rohatgi, R.2    Lebensohn, A.M.3    Le Li, M.J.4    Gygi, S.P.5    Kirschner, M.W.6
  • 45
    • 32144458888 scopus 로고    scopus 로고
    • In vitro reconstitution of cdc42-mediated actin assembly using purified components
    • Ho HY, Rohatgi R, Lebensohn AM, Kirschner MW (2006) In vitro reconstitution of cdc42-mediated actin assembly using purified components. Methods Enzymol 406:174-190
    • (2006) Methods Enzymol , vol.406 , pp. 174-190
    • Ho, H.Y.1    Rohatgi, R.2    Lebensohn, A.M.3    Kirschner, M.W.4
  • 47
    • 27944479854 scopus 로고    scopus 로고
    • Rho GTPases: Biochemistry and biology
    • Jaffe AB, Hall A (2005) Rho GTPases: biochemistry and biology. Annu Rev Cell Dev Biol 21:247-269
    • (2005) Annu Rev Cell Dev Biol , vol.21 , pp. 247-269
    • Jaffe, A.B.1    Hall, A.2
  • 48
    • 0036223236 scopus 로고    scopus 로고
    • P21-activated kinases: Three more join the Pak
    • Jaffer ZM, Chernoff J (2002) p21-activated kinases: three more join the Pak. Int J Biochem Cell Biol 34:713-717
    • (2002) Int J Biochem Cell Biol , vol.34 , pp. 713-717
    • Jaffer, Z.M.1    Chernoff, J.2
  • 50
    • 0035081810 scopus 로고    scopus 로고
    • Localization of a mammalian homolog of diaphanous, mDia1, 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, mDia1, to the mitotic spindle in HeLa cells. J Cell Sci 114:775-784
    • (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
  • 51
    • 0034624753 scopus 로고    scopus 로고
    • Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein
    • Kim AS, Kakalis LT, Abdul-Manan N, Liu GA, Rosen MK (2000) Autoinhibition and activation mechanisms of the Wiskott-Aldrich syndrome protein. Nature 404:151-158
    • (2000) Nature , vol.404 , pp. 151-158
    • Kim, A.S.1    Kakalis, L.T.2    Abdul-Manan, N.3    Liu, G.A.4    Rosen, M.K.5
  • 52
    • 0032511882 scopus 로고    scopus 로고
    • The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338
    • King AJ, Sun H, Diaz B, Barnard D, Miao W, Bagrodia S, Marshall MS (1998) The protein kinase Pak3 positively regulates Raf-1 activity through phosphorylation of serine 338. Nature 396:180-183
    • (1998) Nature , vol.396 , pp. 180-183
    • King, A.J.1    Sun, H.2    Diaz, B.3    Barnard, D.4    Miao, W.5    Bagrodia, S.6    Marshall, M.S.7
  • 53
    • 0037155916 scopus 로고    scopus 로고
    • Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization
    • Kissil JL, Johnson KC, Eckman MS, Jacks T (2002) Merlin phosphorylation by p21-activated kinase 2 and effects of phosphorylation on merlin localization. J Biol Chem 277:10394-10399
    • (2002) J Biol Chem , vol.277 , pp. 10394-10399
    • Kissil, J.L.1    Johnson, K.C.2    Eckman, M.S.3    Jacks, T.4
  • 54
    • 0242298576 scopus 로고    scopus 로고
    • Merlin, the product of the Nf2 tumor suppressor gene, is an inhibitor of the p21-activated kinase, Pak1
    • Kissil JL, Wilker EW, Johnson KC, Eckman MS, Yaffe MB, Jacks T (2003) Merlin, the product of the Nf2 tumor suppressor gene, is an inhibitor of the p21-activated kinase, Pak1. Mol Cell 12:841-849
    • (2003) Mol Cell , vol.12 , pp. 841-849
    • Kissil, J.L.1    Wilker, E.W.2    Johnson, K.C.3    Eckman, M.S.4    Yaffe, M.B.5    Jacks, T.6
  • 55
    • 24944497371 scopus 로고    scopus 로고
    • Features of selective kinase inhibitors
    • Knight ZA, Shokat KM (2005) Features of selective kinase inhibitors. Chem Biol 12:621-637
    • (2005) Chem Biol , vol.12 , pp. 621-637
    • Knight, Z.A.1    Shokat, K.M.2
  • 56
    • 33846676987 scopus 로고    scopus 로고
    • Chemical genetics: Where genetics and pharmacology meet
    • Knight ZA, Shokat KM (2007) Chemical genetics: where genetics and pharmacology meet. Cell 128:425-430
    • (2007) Cell , vol.128 , pp. 425-430
    • Knight, Z.A.1    Shokat, K.M.2
  • 57
    • 0037133041 scopus 로고    scopus 로고
    • The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family
    • Koh CG, Tan EJ, Manser E, Lim L (2002) The p21-activated kinase PAK is negatively regulated by POPX1 and POPX2, a pair of serine/threonine phosphatases of the PP2C family. Curr Biol 12:317-321
    • (2002) Curr Biol , vol.12 , pp. 317-321
    • Koh, C.G.1    Tan, E.J.2    Manser, E.3    Lim, L.4
  • 58
    • 0019427215 scopus 로고
    • Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin
    • Kouyama T, Mihashi K (1981) Fluorimetry study of N-(1-pyrenyl)iodoacetamide-labelled F-actin. Local structural change of actin protomer both on polymerization and on binding of heavy meromyosin. Eur J Biochem 114:33-38
    • (1981) Eur J Biochem , vol.114 , pp. 33-38
    • Kouyama, T.1    Mihashi, K.2
  • 59
    • 0036836941 scopus 로고    scopus 로고
    • Emerging functions of p21-activated kinases in human cancer cells
    • Kumar R, Vadlamudi RK (2002) Emerging functions of p21-activated kinases in human cancer cells. J Cell Physiol 193:133-144
    • (2002) J Cell Physiol , vol.193 , pp. 133-144
    • Kumar, R.1    Vadlamudi, R.K.2
  • 61
    • 28644442126 scopus 로고    scopus 로고
    • The regulation of mDia1 by autoinhibition and its release by Rho*GTP
    • Lammers M, Rose R, Scrima A, Wittinghofer A (2005) The regulation of mDia1 by autoinhibition and its release by Rho*GTP. Embo J 24:4176-4187
    • (2005) Embo J , vol.24 , pp. 4176-4187
    • Lammers, M.1    Rose, R.2    Scrima, A.3    Wittinghofer, A.4
  • 62
    • 32144433330 scopus 로고    scopus 로고
    • Cdc42 and PI(4,5)P2-induced actin assembly in Xenopus egg extracts
    • Lebensohn AM, Ma L, Ho HY, Kirschner MW (2006) Cdc42 and PI(4,5)P2-induced actin assembly in Xenopus egg extracts. Methods Enzymol 406:156-173
    • (2006) Methods Enzymol , vol.406 , pp. 156-173
    • Lebensohn, A.M.1    Ma, L.2    Ho, H.Y.3    Kirschner, M.W.4
  • 63
    • 0035889090 scopus 로고    scopus 로고
    • A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast
    • Lechler T, Jonsdottir GA, Klee SK, Pellman D, Li R (2001) A two-tiered mechanism by which Cdc42 controls the localization and activation of an Arp2/3-activating motor complex in yeast. J Cell Biol 155:261-270
    • (2001) J Cell Biol , vol.155 , pp. 261-270
    • Lechler, T.1    Jonsdottir, G.A.2    Klee, S.K.3    Pellman, D.4    Li, R.5
  • 64
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei M, Lu W, Meng W, Parrini MC, Eck MJ, Mayer BJ, Harrison SC (2000) Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102:387-397
    • (2000) Cell , vol.102 , pp. 387-397
    • Lei, M.1    Lu, W.2    Meng, W.3    Parrini, M.C.4    Eck, M.J.5    Mayer, B.J.6    Harrison, S.C.7
  • 65
    • 23744432051 scopus 로고    scopus 로고
    • Essential role of CIB1 in regulating PAK1 activation and cell migration
    • Leisner TM, Liu M, Jaffer ZM, Chernoff J, Parise LV (2005) Essential role of CIB1 in regulating PAK1 activation and cell migration. J Cell Biol 170:465-476
    • (2005) J Cell Biol , vol.170 , pp. 465-476
    • Leisner, T.M.1    Liu, M.2    Jaffer, Z.M.3    Chernoff, J.4    Parise, L.V.5
  • 66
    • 0043202969 scopus 로고    scopus 로고
    • The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition
    • Li F, Higgs HN (2003) The mouse Formin mDia1 is a potent actin nucleation factor regulated by autoinhibition. Curr Biol 13:1335-1340
    • (2003) Curr Biol , vol.13 , pp. 1335-1340
    • Li, F.1    Higgs, H.N.2
  • 67
    • 14844288286 scopus 로고    scopus 로고
    • Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1
    • Li F, Higgs HN (2005) Dissecting requirements for auto-inhibition of actin nucleation by the formin, mDia1. J Biol Chem 280:6986-6992
    • (2005) J Biol Chem , vol.280 , pp. 6986-6992
    • Li, F.1    Higgs, H.N.2
  • 68
  • 69
    • 0031080595 scopus 로고    scopus 로고
    • Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck
    • Lu W, Katz S, Gupta R, Mayer BJ (1997) Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nck. Curr Biol 7:85-94
    • (1997) Curr Biol , vol.7 , pp. 85-94
    • Lu, W.1    Katz, S.2    Gupta, R.3    Mayer, B.J.4
  • 70
    • 0030707797 scopus 로고    scopus 로고
    • Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous
    • Lynch ED, Lee MK, Morrow JE, Welcsh PL, Leon PE, King MC (1997) Nonsyndromic deafness DFNA1 associated with mutation of a human homolog of the Drosophila gene diaphanous. Science 278:1315-1318
    • (1997) Science , vol.278 , pp. 1315-1318
    • Lynch, E.D.1    Lee, M.K.2    Morrow, J.E.3    Welcsh, P.L.4    Leon, P.E.5    King, M.C.6
  • 71
    • 0032498854 scopus 로고    scopus 로고
    • Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 in inducing actin assembly in Xenopus egg extracts
    • Ma L, Cantley LC, Janmey PA, Kirschner MW (1998a) Corequirement of specific phosphoinositides and small GTP-binding protein Cdc42 in inducing actin assembly in Xenopus egg extracts. J Cell Biol 140:1125-1136
    • (1998) J Cell Biol , vol.140 , pp. 1125-1136
    • Ma, L.1    Cantley, L.C.2    Janmey, P.A.3    Kirschner, M.W.4
  • 72
    • 0032430263 scopus 로고    scopus 로고
    • The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42
    • Ma L, Rohatgi R, Kirschner MW (1998b) The Arp2/3 complex mediates actin polymerization induced by the small GTP-binding protein Cdc42. Proc Natl Acad Sci USA 95:15362-15367
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 15362-15367
    • Ma, L.1    Rohatgi, R.2    Kirschner, M.W.3
  • 73
    • 0028136434 scopus 로고
    • Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose
    • Machesky LM, Atkinson SJ, Ampe C, Vandekerckhove J, Pollard TD (1994) Purification of a cortical complex containing two unconventional actins from Acanthamoeba by affinity chromatography on profilin-agarose. J Cell Biol 127:107-115
    • (1994) J Cell Biol , vol.127 , pp. 107-115
    • Machesky, L.M.1    Atkinson, S.J.2    Ampe, C.3    Vandekerckhove, J.4    Pollard, T.D.5
  • 74
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser E, Leung T, Salihuddin H, Zhao ZS, Lim L (1994) A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature 367:40-46
    • (1994) Nature , vol.367 , pp. 40-46
    • Manser, E.1    Leung, T.2    Salihuddin, H.3    Zhao, Z.S.4    Lim, L.5
  • 75
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes
    • Manser E, Huang HY, Loo TH, Chen XQ, Dong JM, Leung T, Lim L (1997) Expression of constitutively active alpha-PAK reveals effects of the kinase on actin and focal complexes. Mol Cell Biol 17:1129-1143
    • (1997) Mol Cell Biol , vol.17 , pp. 1129-1143
    • Manser, E.1    Huang, H.Y.2    Loo, T.H.3    Chen, X.Q.4    Dong, J.M.5    Leung, T.6    Lim, L.7
  • 78
    • 33846270032 scopus 로고    scopus 로고
    • PTENmediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42
    • Martin-Belmonte F, Gassama A, Datta A, Yu W, Rescher U, Gerke V, Mostov K (2007) PTENmediated apical segregation of phosphoinositides controls epithelial morphogenesis through Cdc42. Cell 128:383-397
    • (2007) Cell , vol.128 , pp. 383-397
    • Martin-Belmonte, F.1    Gassama, A.2    Datta, A.3    Yu, W.4    Rescher, U.5    Gerke, V.6    Mostov, K.7
  • 79
    • 27944445790 scopus 로고    scopus 로고
    • CZH proteins: A new family of Rho-GEFs
    • Meller N, Merlot S, Guda C (2005) CZH proteins: a new family of Rho-GEFs. J Cell Sci 118:4937-4946.
    • (2005) J Cell Sci , vol.118 , pp. 4937-4946
    • Meller, N.1    Merlot, S.2    Guda, C.3
  • 80
    • 0029815611 scopus 로고    scopus 로고
    • N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases
    • Miki H, Miura K, Takenawa T (1996) N-WASP, a novel actin-depolymerizing protein, regulates the cortical cytoskeletal rearrangement in a PIP2-dependent manner downstream of tyrosine kinases. EMBO J 15:5326-5335
    • (1996) EMBO J , vol.15 , pp. 5326-5335
    • Miki, H.1    Miura, K.2    Takenawa, T.3
  • 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
    • 33745493305 scopus 로고    scopus 로고
    • Pre-mRNA splicing in the nuclei of Xenopus oocytes
    • Moon KH, Zhao X, Yu YT (2006) Pre-mRNA splicing in the nuclei of Xenopus oocytes. Methods Mol Biol 322:149-163
    • (2006) Methods Mol Biol , vol.322 , pp. 149-163
    • Moon, K.H.1    Zhao, X.2    Yu, Y.T.3
  • 84
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes CD, Hall A (1995) Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53-62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 85
    • 20844439387 scopus 로고    scopus 로고
    • Structural basis of Rho GTPase-mediated activation of the formin mDia1
    • Otomo T, Otomo C, Tomchick DR, Machius M, Rosen MK (2005) Structural basis of Rho GTPase-mediated activation of the formin mDia1. Mol Cell 18:273-281
    • (2005) Mol Cell , vol.18 , pp. 273-281
    • Otomo, T.1    Otomo, C.2    Tomchick, D.R.3    Machius, M.4    Rosen, M.K.5
  • 86
    • 0033773937 scopus 로고    scopus 로고
    • Fluorescence polarization and anisotropy in high throughput screening: Perspectives and primer
    • Owicki JC (2000) Fluorescence polarization and anisotropy in high throughput screening: perspectives and primer. J Biomol Screen 5:297-306
    • (2000) J Biomol Screen , vol.5 , pp. 297-306
    • Owicki, J.C.1
  • 88
    • 0036158988 scopus 로고    scopus 로고
    • Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1
    • Parrini MC, Lei M, Harrison SC, Mayer BJ (2002) Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1. Mol Cell 9:73-83
    • (2002) Mol Cell , vol.9 , pp. 73-83
    • Parrini, M.C.1    Lei, M.2    Harrison, S.C.3    Mayer, B.J.4
  • 89
    • 0034809353 scopus 로고    scopus 로고
    • Use of biomimetic diversityoriented synthesis to discover galanthamine-like molecules with biological properties beyond those of the natural product
    • Pelish HE, Westwood NJ, Feng Y, Kirchhausen T, Shair MD (2001) Use of biomimetic diversityoriented synthesis to discover galanthamine-like molecules with biological properties beyond those of the natural product. J Am Chem Soc 123:6740-6741
    • (2001) J Am Chem Soc , vol.123 , pp. 6740-6741
    • Pelish, H.E.1    Westwood, N.J.2    Feng, Y.3    Kirchhausen, T.4    Shair, M.D.5
  • 91
    • 0037382160 scopus 로고    scopus 로고
    • Disruption of the Diaphanousrelated formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42
    • Peng J, Wallar BJ, Flanders A, Swiatek PJ, Alberts AS (2003) Disruption of the Diaphanousrelated formin Drf1 gene encoding mDia1 reveals a role for Drf3 as an effector for Cdc42. Curr Biol 13:534-545
    • (2003) Curr Biol , vol.13 , pp. 534-545
    • Peng, J.1    Wallar, B.J.2    Flanders, A.3    Swiatek, P.J.4    Alberts, A.S.5
  • 92
    • 0032101410 scopus 로고    scopus 로고
    • FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation
    • Petersen J, Nielsen O, Egel R, Hagan IM (1998) FH3, a domain found in formins, targets the fission yeast formin Fus1 to the projection tip during conjugation. J Cell Biol 141:1217-1228
    • (1998) J Cell Biol , vol.141 , pp. 1217-1228
    • Petersen, J.1    Nielsen, O.2    Egel, R.3    Hagan, I.M.4
  • 93
    • 34247179024 scopus 로고    scopus 로고
    • Multiple WASP-interacting protein recognition motifs are required for a functional interaction with N-WASP
    • Peterson FC, Deng Q, Zettl M, Prehoda KE, Lim WA, Way M, Volkman BF (2007) Multiple WASP-interacting protein recognition motifs are required for a functional interaction with N-WASP. J Biol Chem 282:8446-8453
    • (2007) J Biol Chem , vol.282 , pp. 8446-8453
    • Peterson, F.C.1    Deng, Q.2    Zettl, M.3    Prehoda, K.E.4    Lim, W.A.5    Way, M.6    Volkman, B.F.7
  • 94
    • 16644399583 scopus 로고    scopus 로고
    • Autoinhibited proteins as promising drug targets
    • Peterson JR, Golemis EA (2004) Autoinhibited proteins as promising drug targets. J Cell Biochem 93:68-73
    • (2004) J Cell Biochem , vol.93 , pp. 68-73
    • Peterson, J.R.1    Golemis, E.A.2
  • 95
    • 0036909567 scopus 로고    scopus 로고
    • Small molecules, big impact: A history of chemical inhibitors and the cytoskeleton
    • Peterson JR, Mitchison TJ (2002) Small molecules, big impact: a history of chemical inhibitors and the cytoskeleton. Chem Biol 9:1275-1285
    • (2002) Chem Biol , vol.9 , pp. 1275-1285
    • Peterson, J.R.1    Mitchison, T.J.2
  • 96
    • 0035845540 scopus 로고    scopus 로고
    • A chemical inhibitor of N-WASP reveals a new mechanism for targeting protein interactions
    • Peterson JR, Lokey RS, Mitchison TJ, Kirschner MW (2001) A chemical inhibitor of N-WASP reveals a new mechanism for targeting protein interactions. Proc Natl Acad Sci USA 98:10624-10629
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 10624-10629
    • Peterson, J.R.1    Lokey, R.S.2    Mitchison, T.J.3    Kirschner, M.W.4
  • 98
    • 33646073413 scopus 로고    scopus 로고
    • Biochemical suppression of small-molecule inhibitors: A strategy to identify inhibitor targets and signaling pathway components
    • Peterson JR, Lebensohn AM, Pelish HE, Kirschner MW (2006) Biochemical suppression of small-molecule inhibitors: a strategy to identify inhibitor targets and signaling pathway components. Chem Biol 13:443-452
    • (2006) Chem Biol , vol.13 , pp. 443-452
    • Peterson, J.R.1    Lebensohn, A.M.2    Pelish, H.E.3    Kirschner, M.W.4
  • 99
    • 0034721696 scopus 로고    scopus 로고
    • Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex
    • Prehoda KE, Scott JA, Mullins RD, Lim WA (2000) Integration of multiple signals through cooperative regulation of the N-WASP-Arp2/3 complex. Science 290:801-806
    • (2000) Science , vol.290 , pp. 801-806
    • Prehoda, K.E.1    Scott, J.A.2    Mullins, R.D.3    Lim, W.A.4
  • 102
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • Ridley AJ, Hall A (1992) The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell 70:389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 103
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley AJ, Paterson HF, Johnston CL, Diekmann D, Hall A (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell 70:401-410
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 104
    • 20444381052 scopus 로고    scopus 로고
    • A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa
    • Rivero F, Muramoto T, Meyer AK, Urushihara H, Uyeda TQ, Kitayama C (2005) A comparative sequence analysis reveals a common GBD/FH3-FH1-FH2-DAD architecture in formins from Dictyostelium, fungi and metazoa. BMC Genomics 6:28
    • (2005) BMC Genomics , vol.6 , pp. 28
    • Rivero, F.1    Muramoto, T.2    Meyer, A.K.3    Urushihara, H.4    Uyeda, T.Q.5    Kitayama, C.6
  • 105
    • 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 MW (1999) The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly. Cell 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
  • 106
    • 0034683746 scopus 로고    scopus 로고
    • Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate
    • Rohatgi R, Ho HY, Kirschner MW (2000) Mechanism of N-WASP activation by CDC42 and phosphatidylinositol 4, 5-bisphosphate. J Cell Biol 150:1299-1310
    • (2000) J Cell Biol , vol.150 , pp. 1299-1310
    • Rohatgi, R.1    Ho, H.Y.2    Kirschner, M.W.3
  • 107
    • 0035854732 scopus 로고    scopus 로고
    • Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway
    • Rohatgi R, Nollau P, Ho HY, Kirschner MW, Mayer BJ (2001) Nck and phosphatidylinositol 4,5-bisphosphate synergistically activate actin polymerization through the N-WASP-Arp2/3 pathway. J Biol Chem 276:26448-26452
    • (2001) J Biol Chem , vol.276 , pp. 26448-26452
    • Rohatgi, R.1    Nollau, P.2    Ho, H.Y.3    Kirschner, M.W.4    Mayer, B.J.5
  • 108
    • 19544386803 scopus 로고    scopus 로고
    • Structural and mechanistic insights into the interaction between Rho and mammalian Dia
    • Rose R, Weyand M, Lammers M, Ishizaki T, Ahmadian MR, Wittinghofer A (2005) Structural and mechanistic insights into the interaction between Rho and mammalian Dia. Nature 435:513-518
    • (2005) Nature , vol.435 , pp. 513-518
    • Rose, R.1    Weyand, M.2    Lammers, M.3    Ishizaki, T.4    Ahmadian, M.R.5    Wittinghofer, A.6
  • 109
    • 13444252631 scopus 로고    scopus 로고
    • GEF means go: Turning on RHO GTPases with guanine nucleotide-exchange factors
    • Rossman KL, Der CJ, Sondek J (2005) GEF means go: turning on RHO GTPases with guanine nucleotide-exchange factors. Nat Rev Mol Cell Biol 6:167-180
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 167-180
    • Rossman, K.L.1    Der Sondek, C.J.J.2
  • 110
    • 3142707455 scopus 로고    scopus 로고
    • PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: Role of mDia1 in PKD2 localization to mitotic spindles
    • Rundle DR, Gorbsky G, Tsiokas L (2004) PKD2 interacts and co-localizes with mDia1 to mitotic spindles of dividing cells: role of mDia1 IN PKD2 localization to mitotic spindles. J Biol Chem 279:29728-29739
    • (2004) J Biol Chem , vol.279 , pp. 29728-29739
    • Rundle, D.R.1    Gorbsky, G.2    Tsiokas, L.3
  • 112
    • 0033714885 scopus 로고    scopus 로고
    • Control of beta-catenin stability: Reconstitution of the cytoplasmic steps of the wnt pathway in Xenopus egg extracts
    • Salic A, Lee E, Mayer L, Kirschner MW (2000) Control of beta-catenin stability: reconstitution of the cytoplasmic steps of the wnt pathway in Xenopus egg extracts. Mol Cell 5:523-532
    • (2000) Mol Cell , vol.5 , pp. 523-532
    • Salic, A.1    Lee, E.2    Mayer, L.3    Kirschner, M.W.4
  • 113
    • 0029795850 scopus 로고    scopus 로고
    • Dynamics of capping protein and actin assembly in vitro: Uncapping barbed ends by polyphosphoinositides
    • Schafer DA, Jennings PB, Cooper JA (1996) Dynamics of capping protein and actin assembly in vitro: uncapping barbed ends by polyphosphoinositides. J Cell Biol 135:169-179
    • (1996) J Cell Biol , vol.135 , pp. 169-179
    • Schafer, D.A.1    Jennings, P.B.2    Cooper, J.A.3
  • 114
    • 0041423391 scopus 로고    scopus 로고
    • Combined array comparative genomic hybridization and tissue microarray analysis suggest PAK1 at 11q13.5-q14 as a critical oncogene target in ovarian carcinoma
    • Schraml P, Schwerdtfeger G, Burkhalter F, Raggi A, Schmidt D, Ruffalo T, King W, Wilber K, Mihatsch MJ, Moch H (2003) Combined array comparative genomic hybridization and tissue microarray analysis suggest PAK1 at 11q13.5-q14 as a critical oncogene target in ovarian carcinoma. Am J Pathol 163:985-992
    • (2003) Am J Pathol , vol.163 , pp. 985-992
    • Schraml, P.1    Schwerdtfeger, G.2    Burkhalter, F.3    Raggi, A.4    Schmidt, D.5    Ruffalo, T.6    King, W.7    Wilber, K.8    Mihatsch, M.J.9    Moch, H.10
  • 116
    • 33745511274 scopus 로고    scopus 로고
    • Xenopus egg extracts: A model system to study proprotein convertases
    • Shennan KI (2006) Xenopus egg extracts: a model system to study proprotein convertases. Methods Mol Biol 322:199-212
    • (2006) Methods Mol Biol , vol.322 , pp. 199-212
    • Shennan, K.I.1
  • 118
    • 0041989574 scopus 로고    scopus 로고
    • Cdc42-dependent actin polymerization during compensatory endocytosis in Xenopus eggs
    • Sokac AM, Co C, Taunton J, Bement W (2003) Cdc42-dependent actin polymerization during compensatory endocytosis in Xenopus eggs. Nat Cell Biol 5:727-732
    • (2003) Nat Cell Biol , vol.5 , pp. 727-732
    • Sokac, A.M.1    Co, C.2    Taunton, J.3    Bement, W.4
  • 119
    • 0034331004 scopus 로고    scopus 로고
    • Chemical genetics: Ligand-based discovery of gene function
    • Stockwell BR (2000) Chemical genetics: ligand-based discovery of gene function. Nat Rev Genet 1:116-125
    • (2000) Nat Rev Genet , vol.1 , pp. 116-125
    • Stockwell, B.R.1
  • 120
    • 30844466190 scopus 로고    scopus 로고
    • Protein complexes regulating Arp2/3-mediated actin assembly
    • Stradal TE, Scita G (2006) Protein complexes regulating Arp2/3-mediated actin assembly. Curr Opin Cell Biol 18:4-10
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 4-10
    • Stradal, T.E.1    Scita, G.2
  • 121
    • 33845729059 scopus 로고    scopus 로고
    • The WASP-WAVE protein network: Connecting the membrane to the cytoskeleton
    • Takenawa T, Suetsugu S (2007) The WASP-WAVE protein network: connecting the membrane to the cytoskeleton. Nat Rev Mol Cell Biol 8:37-48
    • (2007) Nat Rev Mol Cell Biol , vol.8 , pp. 37-48
    • Takenawa, T.1    Suetsugu, S.2
  • 122
    • 33644774386 scopus 로고    scopus 로고
    • CRIPak, a novel endogenous Pak1 inhibitor
    • Talukder AH, Meng Q, Kumar R (2006) CRIPak, a novel endogenous Pak1 inhibitor. Oncogene 25:1311-1319
    • (2006) Oncogene , vol.25 , pp. 1311-1319
    • Talukder, A.H.1    Meng, Q.2    Kumar, R.3
  • 125
    • 21744440559 scopus 로고    scopus 로고
    • Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine
    • Tang DD, Bai Y, Gunst SJ (2005) Silencing of p21-activated kinase attenuates vimentin phosphorylation on Ser-56 and reorientation of the vimentin network during stimulation of smooth muscle cells by 5-hydroxytryptamine. Biochem J 388:773-783
    • (2005) Biochem J , vol.388 , pp. 773-783
    • Tang, D.D.1    Bai, Y.2    Gunst, S.J.3
  • 129
    • 0037500256 scopus 로고    scopus 로고
    • Phosphorylation of Raf-1 by p21-activated kinase 1 and Src regulates Raf-1 autoinhibition
    • Tran NH, Frost JA (2003) Phosphorylation of Raf-1 by p21-activated kinase 1 and Src regulates Raf-1 autoinhibition. J Biol Chem 278:11221-11226
    • (2003) J Biol Chem , vol.278 , pp. 11221-11226
    • Tran, N.H.1    Frost, J.A.2
  • 130
    • 0032907949 scopus 로고    scopus 로고
    • Genetic evidence for Pak1 autoinhibition and its release by Cdc42
    • Tu H, Wigler M (1999) Genetic evidence for Pak1 autoinhibition and its release by Cdc42. Mol Cell Biol 19:602-611
    • (1999) Mol Cell Biol , vol.19 , pp. 602-611
    • Tu, H.1    Wigler, M.2
  • 131
    • 33745513871 scopus 로고    scopus 로고
    • Chromosomal DNA replication in a soluble cell-free system derived from Xenopus eggs
    • Tutter AV, Walter JC (2006) Chromosomal DNA replication in a soluble cell-free system derived from Xenopus eggs. Methods Mol Biol 322:121-137
    • (2006) Methods Mol Biol , vol.322 , pp. 121-137
    • Tutter, A.V.1    Walter, J.C.2
  • 132
    • 0034680834 scopus 로고    scopus 로고
    • Regulatable expression of p21-activated kinase-1 promotes anchorage-independent growth and abnormal organization of mitotic spindles in human epithelial breast cancer cells
    • Vadlamudi RK, Adam L, Wang RA, Mandal M, Nguyen D, Sahin A, Chernoff J, Hung MC, Kumar R (2000) Regulatable expression of p21-activated kinase-1 promotes anchorage-independent growth and abnormal organization of mitotic spindles in human epithelial breast cancer cells. J Biol Chem 275:36238-36244
    • (2000) J Biol Chem , vol.275 , pp. 36238-36244
    • Vadlamudi, R.K.1    Adam, L.2    Wang, R.A.3    Mandal, M.4    Nguyen, D.5    Sahin, A.6    Chernoff, J.7    Hung, M.C.8    Kumar, R.9
  • 134
    • 0037112347 scopus 로고    scopus 로고
    • Structure of the N-WASP EVH1 domain-WIP complex: Insight into the molecular basis of Wiskott-Aldrich Syndrome
    • Volkman BF, Prehoda KE, Scott JA, Peterson FC, Lim WA (2002) Structure of the N-WASP EVH1 domain-WIP complex: insight into the molecular basis of Wiskott-Aldrich Syndrome. Cell 111:565-576
    • (2002) Cell , vol.111 , pp. 565-576
    • Volkman, B.F.1    Prehoda, K.E.2    Scott, J.A.3    Peterson, F.C.4    Lim, W.A.5
  • 135
    • 33645235850 scopus 로고    scopus 로고
    • The basic region of the diaphanous-autoregulatory domain (DAD) is required for autoregulatory interactions with the diaphanous-related formin inhibitory domain
    • Wallar BJ, Stropich BN, Schoenherr JA, Holman HA, Kitchen SM, Alberts AS (2006) The basic region of the diaphanous-autoregulatory domain (DAD) is required for autoregulatory interactions with the diaphanous-related formin inhibitory domain. J Biol Chem 281:4300-4307
    • (2006) J Biol Chem , vol.281 , pp. 4300-4307
    • Wallar, B.J.1    Stropich, B.N.2    Schoenherr, J.A.3    Holman, H.A.4    Kitchen, S.M.5    Alberts, A.S.6
  • 136
    • 33646682385 scopus 로고    scopus 로고
    • PAK1 hyperactivation is sufficient for mammary gland tumor formation
    • Wang RA, Zhang H, Balasenthil S, Medina D, Kumar R (2006) PAK1 hyperactivation is sufficient for mammary gland tumor formation. Oncogene 25:2931-2936
    • (2006) Oncogene , vol.25 , pp. 2931-2936
    • Wang, R.A.1    Zhang, H.2    Balasenthil, S.3    Medina, D.4    Kumar, R.5
  • 138
    • 0033160196 scopus 로고    scopus 로고
    • Cooperation between mDia1 and ROCK in Rho-induced actin reorganization
    • Watanabe N, Kato T, Fujita A, Ishizaki T, Narumiya S (1999) Cooperation between mDia1 and ROCK in Rho-induced actin reorganization. Nat Cell Biol 1:136-143
    • (1999) Nat Cell Biol , vol.1 , pp. 136-143
    • Watanabe, N.1    Kato, T.2    Fujita, A.3    Ishizaki, T.4    Narumiya, S.5
  • 140
    • 33750509850 scopus 로고    scopus 로고
    • Multiple Rho proteins regulate the subcellular targeting of PAK5
    • Wu X, Frost JA (2006) Multiple Rho proteins regulate the subcellular targeting of PAK5. Biochem Biophys Res Commun 351:328-335
    • (2006) Biochem Biophys Res Commun , vol.351 , pp. 328-335
    • Wu, X.1    Frost, J.A.2
  • 141
    • 0035932983 scopus 로고    scopus 로고
    • Regulation of the p21-activated kinase (PAK) by a human Gbeta-like WD-repeat protein, hPIP1
    • Xia C, Ma W, Stafford LJ, Marcus S, Xiong WC, Liu M (2001) Regulation of the p21-activated kinase (PAK) by a human Gbeta-like WD-repeat protein, hPIP1. Proc Natl Acad Sci USA 98:6174-6179
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 6174-6179
    • Xia, C.1    Ma, W.2    Stafford, L.J.3    Marcus, S.4    Xiong, W.C.5    Liu, M.6
  • 142
    • 0037059807 scopus 로고    scopus 로고
    • P21-activated kinase links Rac/Cdc42 signaling to merlin
    • Xiao GH, Beeser A, Chernoff J, Testa JR (2002) p21-activated kinase links Rac/Cdc42 signaling to merlin. J Biol Chem 277:883-886
    • (2002) J Biol Chem , vol.277 , pp. 883-886
    • Xiao, G.H.1    Beeser, A.2    Chernoff, J.3    Testa, J.R.4
  • 143
    • 14844355090 scopus 로고    scopus 로고
    • The NF2 tumor suppressor gene product, merlin, inhibits cell proliferation and cell cycle progression by repressing cyclin D1 expression
    • Xiao GH, Gallagher R, Shetler J, Skele K, Altomare DA, Pestell RG, Jhanwar S, Testa JR (2005) The NF2 tumor suppressor gene product, merlin, inhibits cell proliferation and cell cycle progression by repressing cyclin D1 expression. Mol Cell Biol 25:2384-2394
    • (2005) Mol Cell Biol , vol.25 , pp. 2384-2394
    • Xiao, G.H.1    Gallagher, R.2    Shetler, J.3    Skele, K.4    Altomare, D.A.5    Pestell, R.G.6    Jhanwar, S.7    Testa, J.R.8
  • 144
  • 147
    • 0037040291 scopus 로고    scopus 로고
    • Interaction between active Pak1 and Raf-1 is necessary for phosphorylation and activation of Raf-1
    • Zang M, Hayne C, Luo Z (2002) Interaction between active Pak1 and Raf-1 is necessary for phosphorylation and activation of Raf-1. J Biol Chem 277:4395-4405
    • (2002) J Biol Chem , vol.277 , pp. 4395-4405
    • Zang, M.1    Hayne, C.2    Luo, Z.3
  • 148
    • 0032748298 scopus 로고    scopus 로고
    • Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity
    • Zenke FT, King CC, Bohl BP, Bokoch GM (1999) Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity. J Biol Chem 274:32565-32573
    • (1999) J Biol Chem , vol.274 , pp. 32565-32573
    • Zenke, F.T.1    King, C.C.2    Bohl, B.P.3    Bokoch, G.M.4
  • 149
    • 0141920605 scopus 로고    scopus 로고
    • P21-activated kinase 2 in neutrophils can be regulated by phosphorylation at multiple sites and by a variety of protein phosphatases
    • Zhan Q, Ge Q, Ohira T, Van Dyke T, Badwey JA (2003) p21-activated kinase 2 in neutrophils can be regulated by phosphorylation at multiple sites and by a variety of protein phosphatases. J Immunol 171:3785-3793
    • (2003) J Immunol , vol.171 , pp. 3785-3793
    • Zhan, Q.1    Ge, Q.2    Ohira, T.3    Van Dyke, T.4    Badwey, J.A.5
  • 150
    • 0031948850 scopus 로고    scopus 로고
    • A conserved negative regulatory region in alphaPAK: Inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1
    • Zhao ZS, Manser E, Chen XQ, Chong C, Leung T, Lim L (1998) A conserved negative regulatory region in alphaPAK: inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1. Mol Cell Biol 18:2153-2163
    • (1998) Mol Cell Biol , vol.18 , pp. 2153-2163
    • Zhao, Z.S.1    Manser, E.2    Chen, X.Q.3    Chong, C.4    Leung, T.5    Lim, L.6
  • 151
    • 26944442735 scopus 로고    scopus 로고
    • The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A
    • Zhao ZS, Lim JP, Ng YW, Lim L, Manser E (2005) The GIT-associated kinase PAK targets to the centrosome and regulates Aurora-A. Mol Cell 20:237-249
    • (2005) Mol Cell , vol.20 , pp. 237-249
    • Zhao, Z.S.1    Lim, J.P.2    Ng, Y.W.3    Lim, L.4    Manser, E.5
  • 152
    • 0029835783 scopus 로고    scopus 로고
    • Phosphatidylinositol 4,5-bisphosphate provides an alternative to guanine nucleotide exchange factors by stimulating the dissociation of GDP from Cdc42Hs
    • Zheng Y, Glaven JA, Wu WJ, Cerione RA (1996) Phosphatidylinositol 4,5-bisphosphate provides an alternative to guanine nucleotide exchange factors by stimulating the dissociation of GDP from Cdc42Hs. J Biol Chem 271:23815-23819
    • (1996) J Biol Chem , vol.271 , pp. 23815-23819
    • Zheng, Y.1    Glaven, J.A.2    Wu, W.J.3    Cerione, R.A.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.