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Volumn 17, Issue 3, 1997, Pages 1129-1143

Expression of constitutively active α-PAK reveals effects of the kinase on actin and focal complexes

Author keywords

[No Author keywords available]

Indexed keywords

ACTIN; GUANOSINE TRIPHOSPHATASE; MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE; PROTEIN P21;

EID: 0031036626     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/mcb.17.3.1129     Document Type: Article
Times cited : (504)

References (60)
  • 1
    • 0028898390 scopus 로고
    • Phosphorylation modulates catalytic function and regulation in the cAMP-dependent kinase
    • Adams, J. A., M. L. McGlone, R. Gibson, and S. S. Taylor. 1995. Phosphorylation modulates catalytic function and regulation in the cAMP-dependent kinase. Biochemistry 34:2447-2454.
    • (1995) Biochemistry , vol.34 , pp. 2447-2454
    • Adams, J.A.1    McGlone, M.L.2    Gibson, R.3    Taylor, S.S.4
  • 3
    • 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
  • 4
    • 0029134875 scopus 로고
    • Activation of an S6/H4 kinase (PAK65) from human placenta by intramolecular and intermolecular autophosphorylation
    • Benner, G. E., P. R. Dennis, and R. A. Masaracchia. 1995. Activation of an S6/H4 kinase (PAK65) 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.R.2    Masaracchia, R.A.3
  • 6
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signalling leads to JNK and p38 mitogen-activated protein kinase activation
    • Bragodia, S., B. Deriyard, 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
    • Bragodia, S.1    Deriyard, B.2    Davis, R.J.3    Cerione, R.A.4
  • 7
    • 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
  • 8
    • 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
  • 9
    • 0029594555 scopus 로고
    • p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking
    • Burbelo, P. D., S. Miyamoto, A. Utani, S. Brill, K. M. Yamada, A. Hall, and Y. Yamada. 1995. p190-B, a new member of the Rho GAP family, and Rho are induced to cluster after integrin cross-linking. J. Biol. Chem. 270:30919-30926.
    • (1995) J. Biol. Chem. , vol.270 , pp. 30919-30926
    • Burbelo, P.D.1    Miyamoto, S.2    Utani, A.3    Brill, S.4    Yamada, K.M.5    Hall, A.6    Yamada, Y.7
  • 10
    • 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
  • 11
    • 0029091498 scopus 로고
    • Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast
    • Cvrckova, F., C. de Virgilio, E. Manser, J. R. Pringle, and K. Nasmyth. 1995. Ste20-like protein kinases are required for normal localization of cell growth and for cytokinesis in budding yeast. Genes Dev. 9:1817-1830.
    • (1995) Genes Dev. , vol.9 , pp. 1817-1830
    • Cvrckova, F.1    De Virgilio, C.2    Manser, E.3    Pringle, J.R.4    Nasmyth, K.5
  • 12
    • 0028982953 scopus 로고
    • IIbβ3-mediated translocation of Cdc42Hs to the cytoskeleton in stimulated human platelets
    • IIbβ3-mediated translocation of Cdc42Hs to the cytoskeleton in stimulated human platelets. J. Biol. Chem. 270:17321-17326.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17321-17326
    • Dash, D.1    Aepfelbacher2    Siess, W.3
  • 13
    • 0025940718 scopus 로고
    • Isoprenoid modification and plasma membrane association: Critical factors for ras oncogenicity
    • Der, C. J., and A. D. Cox. 1991. Isoprenoid modification and plasma membrane association: critical factors for ras oncogenicity. Cancer Cells 3:331-140.
    • (1991) Cancer Cells , vol.3 , pp. 331-1140
    • Der, C.J.1    Cox, A.D.2
  • 14
    • 0030022232 scopus 로고    scopus 로고
    • Cytokinesis arrest and redistribution of actin-cytoskeleton regulatory components in cells expressing the Rho GTPase Cdc42Hs
    • Dutartre, H., J. Davoust, J.-P. Gorvel, and P. Chavrier. 1996. Cytokinesis arrest and redistribution of actin-cytoskeleton regulatory components in cells expressing the Rho GTPase Cdc42Hs. J. Cell Sci. 109:367-377.
    • (1996) J. Cell Sci. , vol.109 , pp. 367-377
    • Dutartre, H.1    Davoust, J.2    Gorvel, J.-P.3    Chavrier, P.4
  • 15
    • 0029830139 scopus 로고    scopus 로고
    • The adaptor protein Nck 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 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
  • 17
    • 0029963547 scopus 로고    scopus 로고
    • A Drosophila homolog of the Rac- and Cdc42-activated serine/threonine kinase PAK is a potential focal adhesion and focal complex protein that colocalizes with dynamic actin structures
    • Harden, N., J. Lee, H.-Y. Loh, Y.-M. Ong, I. Tan, T. Leung, E. Manser, and L. Lim. 1996. A Drosophila homolog of the Rac- and Cdc42-activated serine/threonine kinase PAK is a potential focal adhesion and focal complex protein that colocalizes with dynamic actin structures. Mol. Cell. Biol. 16:1896-1908.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1896-1908
    • Harden, N.1    Lee, J.2    Loh, H.-Y.3    Ong, Y.-M.4    Tan, I.5    Leung, T.6    Manser, E.7    Lim, L.8
  • 18
    • 0027428367 scopus 로고
    • Identification of sequences required for the efficient localization of the focal adhesion kinase pp125 FAK, to cellular focal adhesions
    • Hildebrand, J. D., M. D. Schaller, and J. T. Parsons. 1993. Identification of sequences required for the efficient localization of the focal adhesion kinase pp125 FAK, to cellular focal adhesions. J. Cell Biol. 123:993-1004.
    • (1993) J. Cell Biol. , vol.123 , pp. 993-1004
    • Hildebrand, J.D.1    Schaller, M.D.2    Parsons, J.T.3
  • 19
    • 0029955660 scopus 로고    scopus 로고
    • An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase
    • Hildebrand, J. D., J. M. Taylor, and J. T. Parsons. 1996. An SH3 domain-containing GTPase-activating protein for Rho and Cdc42 associates with focal adhesion kinase. Mol. Cell. Biol. 16:3169-3178.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 3169-3178
    • Hildebrand, J.D.1    Taylor, J.M.2    Parsons, J.T.3
  • 20
    • 0029015774 scopus 로고
    • The Rho family GTPases RhoA, Rac1, and Cdc42Hs regulate transcriptional activation by SRF
    • Hill, C. S., J. Wynne, and R. Treisman. 1995. The Rho family GTPases RhoA, Rac1, and Cdc42Hs regulate transcriptional activation by SRF. Cell 81:1159-1170.
    • (1995) Cell , vol.81 , pp. 1159-1170
    • Hill, C.S.1    Wynne, J.2    Treisman, R.3
  • 21
    • 0029985426 scopus 로고    scopus 로고
    • SH3 domain dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin
    • Hobert, O., J. W. Schilling, M. C. Beckerle, A. Ullrich, and B. Jallal. 1996. SH3 domain dependent interaction of the proto-oncogene product Vav with the focal contact protein zyxin. Oncogene 12:1577-1581.
    • (1996) Oncogene , vol.12 , pp. 1577-1581
    • Hobert, O.1    Schilling, J.W.2    Beckerle, M.C.3    Ullrich, A.4    Jallal, B.5
  • 22
    • 0028918408 scopus 로고
    • Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase
    • Hu, Q., A. Klippel, A. J. Muslin, W. J. Fantl, and L. T. Williams. 1995. Ras-dependent induction of cellular responses by constitutively active phosphatidylinositol-3 kinase. Science 268:100-102.
    • (1995) Science , vol.268 , pp. 100-102
    • Hu, Q.1    Klippel, A.2    Muslin, A.J.3    Fantl, W.J.4    Williams, L.T.5
  • 23
    • 0028567874 scopus 로고
    • Constitutive activation of MEK1 by mutation of serine phosphorylation sites
    • Huang, W., and R. L. Erickson. 1994. Constitutive activation of MEK1 by mutation of serine phosphorylation sites. Proc. Natl. Acad. Sci. USA 91: 8960-8983.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 8960-8983
    • Huang, W.1    Erickson, R.L.2
  • 24
    • 0029915841 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of the cytostatic G protein-activated protein kinase PAK1
    • Jakobi, R., C.-J. Chen, P. T. Tuazon, and J. A. Traugh. 1996. Molecular cloning and sequencing of the cytostatic G protein-activated protein kinase PAK1. J. Biol. Chem. 271:6206-6211.
    • (1996) J. Biol. Chem. , vol.271 , pp. 6206-6211
    • Jakobi, R.1    Chen, C.-J.2    Tuazon, P.T.3    Traugh, J.A.4
  • 25
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: Structural basis for regulation
    • Johnson, L. N., M. E. M. Noble, and D. J. Owen. 1996. Active and inactive protein kinases: structural basis for regulation. Cell 85:149-158.
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.M.2    Owen, D.J.3
  • 27
    • 0028998794 scopus 로고
    • Regulation of human leukocyte p21 -activated kinases through G-protein-coupled receptors
    • Knaus, U. G., S. Morris, H.-J. Dong, J. Chernoff, and G. M. Bokoch. 1995. Regulation of human leukocyte p21 -activated kinases through G-protein-coupled receptors. Science 269:221-223.
    • (1995) Science , vol.269 , pp. 221-223
    • Knaus, U.G.1    Morris, S.2    Dong, H.-J.3    Chernoff, J.4    Bokoch, G.M.5
  • 28
    • 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
  • 29
    • 0029779004 scopus 로고    scopus 로고
    • The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia
    • Kozma, R., S. Ahmed, A. Best, and L. Lim. 1996. The GTPase-activating protein n-chimaerin cooperates with Rac1 and Cdc42Hs to induce the formation of lamellipodia and filopodia. Mol. Cell. Biol. 16:5069-5080.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 5069-5080
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 30
    • 0028272507 scopus 로고
    • Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane
    • Leevers, S., H. F. Paterson, and C. Marshall. 1994. Requirement for Ras in Raf activation is overcome by targeting Raf to the plasma membrane. Nature 369:411-114.
    • (1994) Nature , vol.369 , pp. 411-1114
    • Leevers, S.1    Paterson, H.F.2    Marshall, C.3
  • 31
    • 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
  • 32
    • 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
  • 33
    • 1842371864 scopus 로고    scopus 로고
    • Leung, T., and L. Lim. Unpublished data
    • Leung, T., and L. Lim. Unpublished data.
  • 34
    • 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
  • 36
    • 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
  • 37
    • 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
  • 38
    • 0029044903 scopus 로고
    • Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signalling module in the fission yeast Schizosaccharomyces pombe
    • Marcus, S., A. Polverino, E. Chang, D. Robbins, M. H. Cobb, and M. Wigler. 1995. Shk1, a homolog of the Saccharomyces cerevisiae Ste20 and mammalian p65PAK protein kinases, is a component of a Ras/Cdc42 signalling module in the fission yeast Schizosaccharomyces pombe. Proc. Natl. Acad. Sci. USA 92:6180-6184.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 6180-6184
    • Marcus, S.1    Polverino, A.2    Chang, E.3    Robbins, D.4    Cobb, M.H.5    Wigler, M.6
  • 39
    • 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
  • 40
    • 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
  • 41
    • 0025009803 scopus 로고
    • Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42
    • Munemitsu, S., M. A. Innis, R. Clark, F. McCormick, A. Ullrich, and P. Polakis. 1990. Molecular cloning and expression of a G25K cDNA, the human homolog of the yeast cell cycle gene CDC42. Mol. Cell. Biol. 10: 5977-5982.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 5977-5982
    • Munemitsu, S.1    Innis, M.A.2    Clark, R.3    McCormick, F.4    Ullrich, A.5    Polakis, P.6
  • 42
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibres, lamellipodia, and filapodia
    • Nobes, C. D., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibres, lamellipodia, and filapodia. Cell 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 43
    • 0027999633 scopus 로고
    • Requirement for negative charge on activation loop of protein kinase C
    • Orr, J. W., and A. C. Newton. 1994. Requirement for negative charge on activation loop of protein kinase C. J. Biol. Chem. 269:27715-27718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27715-27718
    • Orr, J.W.1    Newton, A.C.2
  • 44
    • 0028879613 scopus 로고
    • Fission yeast pak1 + encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating
    • Ottilie, S., P. J. Miller, D. I. Johnson, C. L. Creasy, M. A. Sells, S. Bragodia, S. L. Forsburg, and J. Chernoff. 1995. Fission yeast pak1 + encodes a protein kinase that interacts with Cdc42p and is involved in the control of cell polarity and mating. EMBO J. 14:5908-5919.
    • (1995) EMBO J. , vol.14 , pp. 5908-5919
    • Ottilie, S.1    Miller, P.J.2    Johnson, D.I.3    Creasy, C.L.4    Sells, M.A.5    Bragodia, S.6    Forsburg, S.L.7    Chernoff, J.8
  • 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. Cobbs, 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    Cobbs, M.H.6    Marcus, S.7
  • 47
    • 0026654125 scopus 로고
    • The small GTP-hinding 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-hinding 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
    • 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
  • 49
    • 0026694947 scopus 로고
    • In-gel digestion of proteins for internal sequence analysis after one- Or two-dimensional gel electrophoresis
    • Rosenfeld, J., J. Capdevielle, J. C. Guillemot, and P. Ferrara. 1992. In-gel digestion of proteins for internal sequence analysis after one-or two-dimensional gel electrophoresis. Anal. Biochem. 203:173-179.
    • (1992) Anal. Biochem. , vol.203 , pp. 173-179
    • Rosenfeld, J.1    Capdevielle, J.2    Guillemot, J.C.3    Ferrara, P.4
  • 50
    • 0029157469 scopus 로고
    • Role for the Rho-family GTPase Cdc42 in yeast mating pheromone signal pathway
    • Simon, M.-N., C. de Virgillo, 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    De Virgillo, C.2    Souza, B.3    Pringle, J.R.4    Abo, A.5    Reed, S.I.6
  • 51
    • 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
  • 52
    • 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
  • 53
    • 0029757748 scopus 로고    scopus 로고
    • Identification of a novel Rac1-interacting protein involved in membrane ruffling
    • Van Aelst, L., T. Joneson, 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    Joneson, T.2    Bar-Sagi, D.3
  • 55
    • 0029066439 scopus 로고
    • Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae
    • Wu, C., M. Whiteway, D. Y. Thomas, and E. Leberer. 1995. Molecular characterization of Ste20p, a potential mitogen-activated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cerevisiae. J. Biol. Chem. 270:15984-15992.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15984-15992
    • Wu, C.1    Whiteway, M.2    Thomas, D.Y.3    Leberer, E.4
  • 56
    • 0025881086 scopus 로고
    • Cloning, expression and transcriptional properties of the human enhancer factor TEF-1
    • Xiao, J. H., I. Davidson, H. Matthes, J.-M. Garnier, and P. Chambon. 1991. Cloning, expression and transcriptional properties of the human enhancer factor TEF-1. Cell 65:551-568.
    • (1991) Cell , vol.65 , pp. 551-568
    • Xiao, J.H.1    Davidson, I.2    Matthes, H.3    Garnier, J.-M.4    Chambon, P.5
  • 57
    • 0029644242 scopus 로고
    • Activity of the MAP kinase ERK2 is controlled by a flexible surface loop
    • Zhang, J., F. Zhang, O. Ebert, M. H. Cobb, and E. J. Goldsmith. 1995. Activity of the MAP kinase ERK2 is controlled by a flexible surface loop. Structure 3:299-307.
    • (1995) Structure , vol.3 , pp. 299-307
    • Zhang, J.1    Zhang, F.2    Ebert, O.3    Cobb, M.H.4    Goldsmith, E.J.5
  • 58
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the down-stream mediator Pak1
    • Zhang, S., J. Han, M. A. Sells, J. Chenoff, U. G. Knaus, R. J. Ulevitch, and G. M. Bokoch. 1995. Rho family GTPases regulate p38 mitogen-activated protein kinase through the down-stream 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    Chenoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 59
    • 0029118202 scopus 로고
    • Pheromone signalling in Saccharomyces cerevisiae requires the small GTP-binding protein Cdc42p and its activator CDC24
    • Zhao, 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
    • Zhao, Z.-S.1    Leung, T.2    Manser, E.3    Lim, L.4
  • 60
    • 1842411673 scopus 로고    scopus 로고
    • Zhao, Z.-S., C. Chong, E. Manser, and L. Lim. Unpublished data
    • Zhao, Z.-S., C. Chong, E. Manser, and L. Lim. Unpublished data.


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