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Volumn 18, Issue 4, 1998, Pages 2153-2163

A conserved negative regulatory region in αPAK: Inhibition of PAK kinases reveals their morphological roles downstream of Cdc42 and Rac1

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; CDC 42 PROTEIN; CELL CYCLE PROTEIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE 5' O (3 THIOTRIPHOSPHATE); MUTANT PROTEIN; PHOSPHOTRANSFERASE; PROTEIN KINASE; PROTEIN P21; RAC1 PROTEIN; UNCLASSIFIED DRUG;

EID: 0031948850     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.18.4.2153     Document Type: Article
Times cited : (285)

References (62)
  • 1
    • 0029680639 scopus 로고
    • Two GTPases, Cdc42 and Rac. bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome
    • Aspenstrom, P., U. Lindberg, and A. Hall. 1995. Two GTPases, Cdc42 and Rac. bind directly to a protein implicated in the immunodeficiency disorder Wiskott-Aldrich syndrome. Curr. Biol. 6:70-75.
    • (1995) Curr. Biol. , vol.6 , pp. 70-75
    • Aspenstrom, P.1    Lindberg, U.2    Hall, A.3
  • 2
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signalling leads to JNK and p38 mitogen-activated protein kinase activation
    • Bagrodia, S., B. Derijard, R. J. Davis, and R. A. Cerione. 1995. Cdc42 and PAK-mediated signalling leads to JNK and p38 mitogen-activated protein kinase activation. J. Biol. Chem. 270:27995-27998.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27995-27998
    • Bagrodia, S.1    Derijard, B.2    Davis, R.J.3    Cerione, R.A.4
  • 4
    • 0029134875 scopus 로고
    • Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation
    • Benner, G. E., P. B. Dennis, and R. A. Masaracchia. 1995. Activation of an S6/H4 kinase (PAK 65) from human placenta by intramolecular and intermolecular autophosphorylation. J. Biol. Chem. 270:21121-21128.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21121-21128
    • Benner, G.E.1    Dennis, P.B.2    Masaracchia, R.A.3
  • 6
    • 0030134625 scopus 로고    scopus 로고
    • Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway
    • Brown, J. L., L. Stowers, M. Baer, J. A. Trejo, S. Coughlin, and J. Chant. 1996. Human Ste20 homologue hPAK1 links GTPases to the JNK MAP kinase pathway. Curr. Biol. 6:598-605.
    • (1996) Curr. Biol. , vol.6 , pp. 598-605
    • Brown, J.L.1    Stowers, L.2    Baer, M.3    Trejo, J.A.4    Coughlin, S.5    Chant, J.6
  • 7
    • 0028786020 scopus 로고
    • A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases
    • Burbelo, P. D., D. Drechsel, and A. Hall. 1995. A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases. J. Biol. Chem. 270:29071-29074.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29071-29074
    • Burbelo, P.D.1    Drechsel, D.2    Hall, A.3
  • 8
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signalling pathway
    • Coso, O. A., M. Chiariello, J. C. Yu, H. Teramoto, P. Crespo, N. Xu, T. Miki, and J. S. Gutkind. 1995. The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signalling pathway. Cell 81:1137-1146.
    • (1995) Cell , vol.81 , pp. 1137-1146
    • Coso, O.A.1    Chiariello, M.2    Yu, J.C.3    Teramoto, H.4    Crespo, P.5    Xu, N.6    Miki, T.7    Gutkind, J.S.8
  • 9
    • 0022504365 scopus 로고
    • Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signalling pathways
    • Coussens, L., P. J. Parker, L. Rhee, T. L. Yang-Feng, E. Chen, M. D. Waterfield, U. Francke, and A. Ullrich. 1986. Multiple, distinct forms of bovine and human protein kinase C suggest diversity in cellular signalling pathways. Science 233:859-866.
    • (1986) Science , vol.233 , pp. 859-866
    • Coussens, L.1    Parker, P.J.2    Rhee, L.3    Yang-Feng, T.L.4    Chen, E.5    Waterfield, M.D.6    Francke, U.7    Ullrich, A.8
  • 10
    • 0022182550 scopus 로고
    • Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase
    • Edelman, A. M., K. Takio, D. K. Blumenthal, R. S. Hansen, K. A. Walsh, K. Titani, and E. G. Krebs. 1985. Characterization of the calmodulin-binding and catalytic domains in skeletal muscle myosin light chain kinase. J. Biol. Chem. 260:11275-11285.
    • (1985) J. Biol. Chem. , vol.260 , pp. 11275-11285
    • Edelman, A.M.1    Takio, K.2    Blumenthal, D.K.3    Hansen, R.S.4    Walsh, K.A.5    Titani, K.6    Krebs, E.G.7
  • 11
    • 0029830139 scopus 로고    scopus 로고
    • The adaptor protein Nek links receptor tyrosine kinases with the serine-threonine kinase Pak1
    • Galisteo, M. L., J. Chernoff, Y.-C. Su, E. Y. Skolnik, and J. Schlessinger. 1996. The adaptor protein Nek 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
  • 12
    • 0023555557 scopus 로고
    • Protein kinase C contains a pseudosubslrate prototype in its regulatory domain
    • House, C., and B. E. Kemp. 1987. Protein kinase C contains a pseudosubslrate prototype in its regulatory domain. Science 238:1726-1728.
    • (1987) Science , vol.238 , pp. 1726-1728
    • House, C.1    Kemp, B.E.2
  • 14
    • 0025819344 scopus 로고
    • Definition of the inhibitory domain of smooth muscle myosin light chain kinase by site-directed mutagenesis
    • Ito, M., V. Guerriero, Jr., X. M. Chen, and D. J. Hartshorne. 1991. Definition of the inhibitory domain of smooth muscle myosin light chain kinase by site-directed mutagenesis. Biochemistry 30:3498-3503.
    • (1991) Biochemistry , vol.30 , pp. 3498-3503
    • Ito, M.1    Guerriero Jr., V.2    Chen, X.M.3    Hartshorne, D.J.4
  • 15
    • 0029802561 scopus 로고    scopus 로고
    • RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase
    • Joneson, T., M. McDonough, D. Bar-Sagi, and L. Van Aelst. 1996. RAC regulation of actin polymerization and proliferation by a pathway distinct from Jun kinase. Science 274:1374-1376.
    • (1996) Science , vol.274 , pp. 1374-1376
    • Joneson, T.1    McDonough, M.2    Bar-Sagi, D.3    Van Aelst, L.4
  • 16
    • 0028251408 scopus 로고
    • Substrate and pseudosubstrate interactions with protein kinases: Determinants of specificity
    • Kemp, B. E., M. W. Parker, S. Hu, T. Tiganis, and C. House. 1994. Substrate and pseudosubstrate interactions with protein kinases: determinants of specificity. Trends Biochem. Sci. 19:440-444.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 440-444
    • Kemp, B.E.1    Parker, M.W.2    Hu, S.3    Tiganis, T.4    House, C.5
  • 17
    • 0023645552 scopus 로고
    • Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain
    • Kennelly, P. J., A. M. Edelman, D. K. Blumenthal, and E. G. Krebs. 1987. Rabbit skeletal muscle myosin light chain kinase. The calmodulin binding domain as a potential active site-directed inhibitory domain. J. Biol. Chem. 262:11958-11963.
    • (1987) J. Biol. Chem. , vol.262 , pp. 11958-11963
    • Kennelly, P.J.1    Edelman, A.M.2    Blumenthal, D.K.3    Krebs, E.G.4
  • 19
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma, R., S. Ahmed, A. Best, and L. Lim. 1995. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15:1942-1952.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 20
    • 0031027205 scopus 로고    scopus 로고
    • Rho family GTPases and neuronal growth cone remodelling: Relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid
    • Kozma, R., S. Sarner, S. Ahmed, and L. Lim. 1997. Rho family GTPases and neuronal growth cone remodelling: relationship between increased complexity induced by Cdc42Hs, Rac1, and acetylcholine and collapse induced by RhoA and lysophosphatidic acid. Mol. Cell. Biol. 17:1201-1211.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1201-1211
    • Kozma, R.1    Sarner, S.2    Ahmed, S.3    Lim, L.4
  • 22
    • 0027048684 scopus 로고
    • The protein kinase homologue Steo20p is required to link the yeast pheromone response G-protein βγ subunits to downstream signalling components
    • Leberer, E., D. Dignard, D. Harcus, D. Y. Thomas, and M. Whiteway. 1992. The protein kinase homologue Steo20p is required to link the yeast pheromone response G-protein βγ subunits to downstream signalling components. EMBO J. 11:4815-4824.
    • (1992) EMBO J. , vol.11 , pp. 4815-4824
    • Leberer, E.1    Dignard, D.2    Harcus, D.3    Thomas, D.Y.4    Whiteway, M.5
  • 23
    • 0031015562 scopus 로고    scopus 로고
    • Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase
    • Leberer, E., C. Wu, T. Leeuw, A. Fourest-Lieuvin, J. E. Segall, and D. Y. Thomas. 1997. Functional characterization of the Cdc42p binding domain of yeast Ste20p protein kinase. EMBO J. 16:83-97.
    • (1997) EMBO J. , vol.16 , pp. 83-97
    • Leberer, E.1    Wu, C.2    Leeuw, T.3    Fourest-Lieuvin, A.4    Segall, J.E.5    Thomas, D.Y.6
  • 24
    • 0028863142 scopus 로고
    • A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes
    • Leung, T., E. Manser, L. Tan, and L. Lim. 1995. A novel serine/threonine kinase binding the Ras-related RhoA GTPase which translocates the kinase to peripheral membranes. J. Biol. Chem. 270:29051-29054.
    • (1995) J. Biol. Chem. , vol.270 , pp. 29051-29054
    • Leung, T.1    Manser, E.2    Tan, L.3    Lim, L.4
  • 25
    • 0029789678 scopus 로고    scopus 로고
    • The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton
    • Leung, T., X.-Q. Chen, E. Manser, and L. Lim. 1996. The p160 RhoA-binding kinase ROKα is a member of a kinase family and is involved in the reorganization of the cytoskeleton. Mol. Cell. Biol. 16:5313-5327.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5313-5327
    • Leung, T.1    Chen, X.-Q.2    Manser, E.3    Lim, L.4
  • 26
    • 0031962372 scopus 로고    scopus 로고
    • Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization
    • Leung, T., X.-Q. Chen, I. Tan, E. Manser, and L. Lim. 1998. Myotonic dystrophy kinase-related Cdc42-binding kinase acts as a Cdc42 effector in promoting cytoskeletal reorganization. Mol. Cell. Biol. 18:130-140.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 130-140
    • Leung, T.1    Chen, X.-Q.2    Tan, I.3    Manser, E.4    Lim, L.5
  • 27
    • 0029805324 scopus 로고    scopus 로고
    • Regulation of phosphorylation pathways by p21 GTPases
    • Lim, L., E. Manser, T. Leung, and C. Hall. 1996. Regulation of phosphorylation pathways by p21 GTPases. Eur. J. Biochem. 242:171-185.
    • (1996) Eur. J. Biochem. , vol.242 , pp. 171-185
    • Lim, L.1    Manser, E.2    Leung, T.3    Hall, C.4
  • 28
    • 0027759277 scopus 로고
    • Elements of the yeast pheromone response pathway required for filamentous growth of diploids
    • Liu, H., C. Styles, and G. R. Fink. 1993. Elements of the yeast pheromone response pathway required for filamentous growth of diploids. Science 262: 1741-1744.
    • (1993) Science , vol.262 , pp. 1741-1744
    • Liu, H.1    Styles, C.2    Fink, G.R.3
  • 29
    • 0031080595 scopus 로고    scopus 로고
    • Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nek
    • Lu, W., S. Katz, R. Gupta, and B. J. Mayer. 1997. Activation of Pak by membrane localization mediated by an SH3 domain from the adaptor protein Nek. 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
  • 30
    • 0026768682 scopus 로고
    • Diversity and versatility of GTPase activating proteins for the p21rho subfamily of ras G proteins detected by a novel overlay assay
    • Manser, E., T. Leung, C. Monfries, M. Teo, C. Hall, and L. Lim. 1992. Diversity and versatility of GTPase activating proteins for the p21rho subfamily of ras G proteins detected by a novel overlay assay. J. Biol. Chem. 267:16025-16028.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16025-16028
    • Manser, E.1    Leung, T.2    Monfries, C.3    Teo, M.4    Hall, C.5    Lim, L.6
  • 32
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser, E., T. Leung, H. Salihuddin, Z.-S. Zhao, and L. Lim. 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
  • 33
    • 0028862297 scopus 로고
    • Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family
    • Manser, E., C. Chong, Z.-S. Zhao, T. Leung, G. Michael, C. Hall, and L. Lim. 1995. Molecular cloning of a new member of the p21-Cdc42/Rac-activated kinase (PAK) family. J. Biol. Chem. 270:25070-25078.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25070-25078
    • Manser, E.1    Chong, C.2    Zhao, Z.-S.3    Leung, T.4    Michael, G.5    Hall, C.6    Lim, L.7
  • 34
    • 0031036626 scopus 로고    scopus 로고
    • Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes
    • Manser, E., H.-Y. Huang, T.-H. Loo, X.-Q. Chen, J.-M. Dong, T. Leung, and L. Lim. 1997. Expression of constitutively active α-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
  • 35
    • 0031610579 scopus 로고    scopus 로고
    • A family of guanine nucleotide exchange factors (PIXs) is directly coupled to the p21(Cdc42 and Rac)-activated kinase αPAK
    • Manser, E., T.-H. Loo, C.-G. Koh, Z.-S. Zhao, I. Tan, T. Leung, and L. Lim. 1998. A family of guanine nucleotide exchange factors (PIXs) is directly coupled to the p21(Cdc42 and Rac)-activated kinase αPAK. Mol. Cell 1:183-192.
    • (1998) Mol. Cell , vol.1 , pp. 183-192
    • Manser, E.1    Loo, T.-H.2    Koh, C.-G.3    Zhao, Z.-S.4    Tan, I.5    Leung, T.6    Lim, L.7
  • 36
    • 0029056399 scopus 로고
    • A novel serine kinase activated by rac/Cdc42Hs-dependent autophosphorylation is related to PAK65 and Ste20
    • Martin, G. A., G. Bollag, F. A. McCormick, and A. Abo. 1995. A novel serine kinase activated by rac/Cdc42Hs-dependent autophosphorylation is related to PAK65 and Ste20. EMBO J. 14:1970-1978.
    • (1995) EMBO J. , vol.14 , pp. 1970-1978
    • Martin, G.A.1    Bollag, G.2    McCormick, F.A.3    Abo, A.4
  • 38
    • 0029070887 scopus 로고
    • Selective activation of the JNK signalling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., A. Lin, F.-X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signalling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147-1157.
    • (1995) Cell , vol.81 , pp. 1147-1157
    • Minden, A.1    Lin, A.2    Claret, F.-X.3    Abo, A.4    Karin, M.5
  • 39
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolccular local complexes associated with actin stress fibres, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolccular local complexes associated with actin stress fibres, lamellipodia, and filopodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 40
    • 0028829555 scopus 로고
    • A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae
    • Nonaka, H., K. Tanaka, H. Hirano, T. Fujiwara, H. Kohno, M. Umikawa, A. Mino, and Y. Takai. 1995. A downstream target of RHO1 small GTP-binding protein is PKC1, a homolog of protein kinase C, which leads to activation of the MAP kinase cascade in Saccharomyces cerevisiae. EMBO J. 14:5931-5938.
    • (1995) EMBO J. , vol.14 , pp. 5931-5938
    • Nonaka, H.1    Tanaka, K.2    Hirano, H.3    Fujiwara, T.4    Kohno, H.5    Umikawa, M.6    Mino, A.7    Takai, Y.8
  • 41
    • 0029101360 scopus 로고
    • An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1
    • Olson, M. F., A. Ashworth, and A. Hall. 1995. An essential role for Rho, Rac, and Cdc42 GTPases in cell cycle progression through G1. Science 269:1270-1272.
    • (1995) Science , vol.269 , pp. 1270-1272
    • Olson, M.F.1    Ashworth, A.2    Hall, A.3
  • 44
    • 0030465534 scopus 로고    scopus 로고
    • Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast
    • Peter, M., A. M. Neiman, H.-O. Park, M. van Lohuizen, and I. Herskowitz. 1996. Functional analysis of the interaction between the small GTP binding protein Cdc42 and the Ste20 protein kinase in yeast. EMBO J. 15:7046-7059.
    • (1996) EMBO J. , vol.15 , pp. 7046-7059
    • Peter, M.1    Neiman, A.M.2    Park, H.-O.3    Van Lohuizen, M.4    Herskowitz, I.5
  • 45
    • 0028846513 scopus 로고
    • Activation of mitogen-activated protein kinase cascades by p21-activated protein kinases in cell-free extracts of Xenopus oocytes
    • Polverino, A., J. Frost, P. Yang, M. Hutchison, A. M. Neiman, M. H. Cobb, and S. Marcus. 1995. Activation of mitogen-activated protein kinase cascades by p21-activated protein kinases in cell-free extracts of Xenopus oocytes. J. Biol. Chem. 270:26067-26070.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26067-26070
    • Polverino, A.1    Frost, J.2    Yang, P.3    Hutchison, M.4    Neiman, A.M.5    Cobb, M.H.6    Marcus, S.7
  • 46
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibres in response to growth factors
    • Ridley, A. J., and A. Hall. 1992. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibres in response to growth factors. Cell 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 47
    • 0026654125 scopus 로고
    • The small GTP-binding protein Rac regulates growth factor-induced membrane ruffling
    • Ridley, A. J., H. F. Paterson, C. L. Johnston, D. Diekmann, and A. Hall. 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
  • 48
    • 0030918572 scopus 로고    scopus 로고
    • Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2
    • Rudel, T., and G. M. Bokoch. 1997. Membrane and morphological changes in apoptotic cells regulated by caspase-mediated activation of PAK2. Science 276:1571-1574.
    • (1997) Science , vol.276 , pp. 1571-1574
    • Rudel, T.1    Bokoch, G.M.2
  • 49
    • 0031127255 scopus 로고    scopus 로고
    • Emerging from the Pak: The p21-activated protein kinase family
    • Sells, M. A., and J. Chernoff. 1997. Emerging from the Pak: the p21-activated protein kinase family. Trends Cell Biol. 7:162-167.
    • (1997) Trends Cell Biol. , vol.7 , pp. 162-167
    • Sells, M.A.1    Chernoff, J.2
  • 50
  • 51
    • 0029157469 scopus 로고
    • Role for the Rho-family GTPase Cdc42 in yeast mating pheromone signal pathway
    • Simon, M. N., C. Devirgilio, B. Souza, J. R. Pringle, A. Abo, and S. I. Reed. 1995. Role for the Rho-family GTPase Cdc42 in yeast mating pheromone signal pathway. Nature 376:702-705.
    • (1995) Nature , vol.376 , pp. 702-705
    • Simon, M.N.1    Devirgilio, C.2    Souza, B.3    Pringle, J.R.4    Abo, A.5    Reed, S.I.6
  • 52
    • 0025145585 scopus 로고
    • Protein kinases. Regulation by autoinhibitory domains
    • Soderling, T. R. 1990. Protein kinases. Regulation by autoinhibitory domains. J. Biol. Chem. 265:1823-1826.
    • (1990) J. Biol. Chem. , vol.265 , pp. 1823-1826
    • Soderling, T.R.1
  • 53
    • 0030006284 scopus 로고    scopus 로고
    • Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization
    • Symons, M., J. M. J. Derry, B. Karlak, S. Jiang, V. Lemahieu, F. McCormick, U. Francke, and A. Abo. 1996. Wiskott-Aldrich syndrome protein, a novel effector for the GTPase Cdc42Hs, is implicated in actin polymerization. Cell 84:723-734.
    • (1996) Cell , vol.84 , pp. 723-734
    • Symons, M.1    Derry, J.M.J.2    Karlak, B.3    Jiang, S.4    Lemahieu, V.5    McCormick, F.6    Francke, U.7    Abo, A.8
  • 54
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N., and A. Hall. 1997. Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9:86-92.
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 55
    • 0028842508 scopus 로고
    • cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets
    • cdc42/rac1-activated serine/threonine kinase that is rapidly activated by thrombin in platelets. J. Biol. Chem. 270:26690-26697.
    • (1995) J. Biol. Chem. , vol.270 , pp. 26690-26697
    • Teo, M.1    Manser, E.2    Lim, L.3
  • 56
    • 0029757748 scopus 로고    scopus 로고
    • Identification of a novel Rac1-interacting protein involved in membrane ruffling
    • Van Aelst, L., T. Juneson, and D. Bar-Sagi. 1996. Identification of a novel Rac1-interacting protein involved in membrane ruffling. EMBO J. 15:3778-3786.
    • (1996) EMBO J. , vol.15 , pp. 3778-3786
    • Van Aelst, L.1    Juneson, T.2    Bar-Sagi, D.3
  • 59
    • 0031026132 scopus 로고    scopus 로고
    • Rac regulation of transformation, gene expression, and actin organization by multiple. PAK-independent pathways
    • Westwick, J. K., Q. T. Lambert, G. J. Clarke, M. Symons, L. Van Aelst, R. G. Pestell, and C. J. Der. 1997. Rac regulation of transformation, gene expression, and actin organization by multiple. PAK-independent pathways. Mol. Cell. Biol. 17:1324-1335.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1324-1335
    • Westwick, J.K.1    Lambert, Q.T.2    Clarke, G.J.3    Symons, M.4    Van Aelst, L.5    Pestell, R.G.6    Der, C.J.7
  • 60
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang, S., J. Han, M. A. Sells, J. Chernoff, U. G. Knaus, R. J. Ulevitch, and G. M. Bokoch. 1995. Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J. Biol. Chem. 270: 23934-23936.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23934-23936
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 61
    • 0029118202 scopus 로고
    • Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24
    • Zhan, Z.-S., T. Leung, E. Manser, and L. Lim. 1995. Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24. Mol. Cell. Biol. 15:5246-5257.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 5246-5257
    • Zhan, Z.-S.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 62
    • 0025847665 scopus 로고
    • Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity
    • Ziman, M., J. M. O'Brien, L. A. Ouellette, W. R. Church, and D. I. Johnson. 1991. Mutational analysis of CDC42Sc, a Saccharomyces cerevisiae gene that encodes a putative GTP-binding protein involved in the control of cell polarity. Mol. Cell. Biol. 11:3537-3544.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3537-3544
    • Ziman, M.1    O'Brien, J.M.2    Ouellette, L.A.3    Church, W.R.4    Johnson, D.I.5


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