메뉴 건너뛰기




Volumn 15, Issue 1, 2004, Pages 117-127

Phosphorylation of RhoGDI by Pak1 mediates dissociation of Rac GTPase

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR; P21 ACTIVATED KINASE; PLATELET DERIVED GROWTH FACTOR; PROTEIN; PROTEIN CDC42; RAC PROTEIN; RHO GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR PROTEIN; SERINE; UNCLASSIFIED DRUG;

EID: 3042839349     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2004.05.019     Document Type: Article
Times cited : (199)

References (47)
  • 2
    • 0033531955 scopus 로고    scopus 로고
    • Characterization of rac and cdc42 activation in chemoattractant- stimulated human neutrophils using a novel assay for active GTPases
    • Benard V., Bohl B.P., Bokoch G.M. Characterization of rac and cdc42 activation in chemoattractant-stimulated human neutrophils using a novel assay for active GTPases. J. Biol. Chem. 274:1999;13198-13204
    • (1999) J. Biol. Chem. , vol.274 , pp. 13198-13204
    • Benard, V.1    Bohl, B.P.2    Bokoch, G.M.3
  • 3
    • 0034213327 scopus 로고    scopus 로고
    • Rho GTPases and their effector proteins
    • Bishop A.L., Hall A. Rho GTPases and their effector proteins. Biochem. J. 348:2000;241-255
    • (2000) Biochem. J. , vol.348 , pp. 241-255
    • Bishop, A.L.1    Hall, A.2
  • 4
    • 0038554077 scopus 로고    scopus 로고
    • Biology of the p21-activated kinases
    • Bokoch G.M. Biology of the p21-activated kinases. Annu. Rev. Biochem. 72:2003;743-781
    • (2003) Annu. Rev. Biochem. , vol.72 , pp. 743-781
    • Bokoch, G.M.1
  • 5
    • 0028081350 scopus 로고
    • Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins
    • Bokoch G.M., Bohl B.P., Chuang T.H. Guanine nucleotide exchange regulates membrane translocation of Rac/Rho GTP-binding proteins. J. Biol. Chem. 269:1994;31674-31679
    • (1994) J. Biol. Chem. , vol.269 , pp. 31674-31679
    • Bokoch, G.M.1    Bohl, B.P.2    Chuang, T.H.3
  • 7
    • 0032478605 scopus 로고    scopus 로고
    • A GTPase-independent mechanism of p21-activated kinase activation. Regulation by sphingosine and other biologically active lipids
    • Bokoch G.M., Reilly A.M., Daniels R.H., King C.C., Olivera A., Spoiegel S., Knaus U.G. A GTPase-independent mechanism of p21-activated kinase activation. Regulation by sphingosine and other biologically active lipids. J. Biol. Chem. 273:1998;8137-8144
    • (1998) J. Biol. Chem. , vol.273 , pp. 8137-8144
    • Bokoch, G.M.1    Reilly, A.M.2    Daniels, R.H.3    King, C.C.4    Olivera, A.5    Spoiegel, S.6    Knaus, U.G.7
  • 8
    • 0030060157 scopus 로고    scopus 로고
    • Phosphorylation of Rho GDI stabilizes the Rho A-Rho GDI complex in neutrophil cytosol
    • Bourmeyster N., Vignais P.V. Phosphorylation of Rho GDI stabilizes the Rho A-Rho GDI complex in neutrophil cytosol. Biochem. Biophys. Res. Commun. 218:1996;54-60
    • (1996) Biochem. Biophys. Res. Commun. , vol.218 , pp. 54-60
    • Bourmeyster, N.1    Vignais, P.V.2
  • 9
    • 0027995468 scopus 로고
    • Role of bound GDP in the stability of the rho A-rho GDI complex purified from neutrophil cytosol
    • Bourmeyster N., Boquet P., Vignais P.V. Role of bound GDP in the stability of the rho A-rho GDI complex purified from neutrophil cytosol. Biochem. Biophys. Res. Commun. 205:1994;174-179
    • (1994) Biochem. Biophys. Res. Commun. , vol.205 , pp. 174-179
    • Bourmeyster, N.1    Boquet, P.2    Vignais, P.V.3
  • 10
    • 0025998840 scopus 로고
    • Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates
    • Boyle W.J., van der Geer P., Hunter T. Phosphopeptide mapping and phosphoamino acid analysis by two-dimensional separation on thin-layer cellulose plates. Methods Enzymol. 201:1991;110-149
    • (1991) Methods Enzymol. , vol.201 , pp. 110-149
    • Boyle, W.J.1    Van Der Geer, P.2    Hunter, T.3
  • 11
    • 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. The mechanism of PAK activation. Autophosphorylation events in both regulatory and kinase domains control activity. J. Biol. Chem. 276:2001;17347-17353
    • (2001) J. Biol. Chem. , vol.276 , pp. 17347-17353
    • Chong, C.1    Tan, L.2    Lim, L.3    Manser, E.4
  • 12
    • 0027393663 scopus 로고
    • GDP dissociation inhibitor prevents intrinsic and GTPase activating protein-stimulated GTP hydrolysis by the Rac GTP-binding protein
    • b
    • Chuang T.H., Xu X., Knaus U.G., Hart M.J., Bokoch G.M. GDP dissociation inhibitor prevents intrinsic and GTPase activating protein-stimulated GTP hydrolysis by the Rac GTP-binding protein. J. Biol. Chem. 268:1993;775-778. b
    • (1993) J. Biol. Chem. , vol.268 , pp. 775-778
    • Chuang, T.H.1    Xu, X.2    Knaus, U.G.3    Hart, M.J.4    Bokoch, G.M.5
  • 13
    • 0030772657 scopus 로고    scopus 로고
    • Localization of p21-activated kinase 1 (Pak1) to pinocytic vesicles and cortical actin structures in stimulated cells
    • Dharmawardhane S., Sanders L.C., Martin S.S., Daniels R.H., Bokoch G.M. Localization of p21-activated kinase 1 (Pak1) to pinocytic vesicles and cortical actin structures in stimulated cells. J. Cell Biol. 138:1997;1265-1278
    • (1997) J. Cell Biol. , vol.138 , pp. 1265-1278
    • Dharmawardhane, S.1    Sanders, L.C.2    Martin, S.S.3    Daniels, R.H.4    Bokoch, G.M.5
  • 14
    • 0037081858 scopus 로고    scopus 로고
    • Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes
    • Forget M.A., Desrosiers R.R., Gingras D., Beliveau R. Phosphorylation states of Cdc42 and RhoA regulate their interactions with Rho GDP dissociation inhibitor and their extraction from biological membranes. Biochem. J. 361:2002;243-254
    • (2002) Biochem. J. , vol.361 , pp. 243-254
    • Forget, M.A.1    Desrosiers, R.R.2    Gingras, D.3    Beliveau, R.4
  • 15
    • 0025073547 scopus 로고
    • Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like small GTP-binding proteins
    • Fukumoto Y., Kaibuchi K., Hori Y., Fujioka H., Araki S., Ueda T., Kikuchi A., Takai Y. Molecular cloning and characterization of a novel type of regulatory protein (GDI) for the rho proteins, ras p21-like small GTP-binding proteins. Oncogene. 5:1990;1321-1328
    • (1990) Oncogene , vol.5 , pp. 1321-1328
    • Fukumoto, Y.1    Kaibuchi, K.2    Hori, Y.3    Fujioka, H.4    Araki, S.5    Ueda, T.6    Kikuchi, A.7    Takai, Y.8
  • 16
    • 0029830139 scopus 로고    scopus 로고
    • The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1
    • Galisteo M.L., Chernoff J., Su Y.C., Skolnik E.Y., Schlessinger J. The adaptor protein Nck links receptor tyrosine kinases with the serine-threonine kinase Pak1. J. Biol. Chem. 271:1996;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
    • 0035887166 scopus 로고    scopus 로고
    • RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates filipodia formation but does not cycle with the cytosol of mammialian cells
    • Gibson R.M., Wilson-Delfosse A.L. RhoGDI-binding-defective mutant of Cdc42Hs targets to membranes and activates filipodia formation but does not cycle with the cytosol of mammialian cells. Biochem. J. 359:2001;285-294
    • (2001) Biochem. J. , vol.359 , pp. 285-294
    • Gibson, R.M.1    Wilson-Delfosse, A.L.2
  • 18
    • 0032579315 scopus 로고    scopus 로고
    • Differential properties of D4/LyGDI versus RhoGDI: Phosphorylation and Rho GTPase selectivity
    • Gorvel J.-P., Chang T.-C., Boretto J., Azuma T., Chavrier P. Differential properties of D4/LyGDI versus RhoGDI. phosphorylation and Rho GTPase selectivity FEBS Lett. 422:1998;269-273
    • (1998) FEBS Lett. , vol.422 , pp. 269-273
    • Gorvel, J.-P.1    Chang, T.-C.2    Boretto, J.3    Azuma, T.4    Chavrier, P.5
  • 19
    • 0030992879 scopus 로고    scopus 로고
    • C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases
    • Gosser Y.Q., Nomanbhoy T.K., Aghazadeh B., Manor D., Combs C., Cerione R.A., Rosen M.K. C-terminal binding domain of Rho GDP-dissociation inhibitor directs N-terminal inhibitory peptide to GTPases. Nature. 387:1997;814-819
    • (1997) Nature , vol.387 , pp. 814-819
    • Gosser, Y.Q.1    Nomanbhoy, T.K.2    Aghazadeh, B.3    Manor, D.4    Combs, C.5    Cerione, R.A.6    Rosen, M.K.7
  • 20
    • 0034603198 scopus 로고    scopus 로고
    • Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI
    • Hoffman G.R., Nassar N., Cerione R.A. Structure of the Rho family GTP-binding protein Cdc42 in complex with the multifunctional regulator RhoGDI. Cell. 100:2000;345-356
    • (2000) Cell , vol.100 , pp. 345-356
    • Hoffman, G.R.1    Nassar, N.2    Cerione, R.A.3
  • 21
    • 0031570337 scopus 로고    scopus 로고
    • A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm
    • Keep N.H., Barnes M., Barsukov I., Badii R., Lian L.Y., Segal A.W., Moody P.C., Roberts G.C. A modulator of rho family G proteins, rhoGDI, binds these G proteins via an immunoglobulin-like domain and a flexible N-terminal arm. Structure. 5:1997;623-633
    • (1997) Structure , vol.5 , pp. 623-633
    • Keep, N.H.1    Barnes, M.2    Barsukov, I.3    Badii, R.4    Lian, L.Y.5    Segal, A.W.6    Moody, P.C.7    Roberts, G.C.8
  • 22
    • 0026664194 scopus 로고
    • Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein
    • Kikuchi A., Kuroda S., Sasaki T., Kotani K., Hirata K., Katayama M., Takai Y. Functional interactions of stimulatory and inhibitory GDP/GTP exchange proteins and their common substrate small GTP-binding protein. J. Biol. Chem. 267:1992;14611-14615
    • (1992) J. Biol. Chem. , vol.267 , pp. 14611-14615
    • Kikuchi, A.1    Kuroda, S.2    Sasaki, T.3    Kotani, K.4    Hirata, K.5    Katayama, M.6    Takai, Y.7
  • 23
    • 0034731505 scopus 로고    scopus 로고
    • P21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1)
    • King C.C., Gardiner E.M.M., Zenke F.T., Bohl B.M., Newton A.C., Hemmings B.A., Bokoch G.M. p21-activated kinase (PAK1) is phosphorylated and activated by 3-phosphoinositide-dependent kinase-1 (PDK1). J. Biol. Chem. 275:2000;41201-41209
    • (2000) J. Biol. Chem. , vol.275 , pp. 41201-41209
    • King, C.C.1    Gardiner, E.M.M.2    Zenke, F.T.3    Bohl, B.M.4    Newton, A.C.5    Hemmings, B.A.6    Bokoch, G.M.7
  • 25
    • 0028998794 scopus 로고
    • Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors
    • Knaus U.G., Morris S., Dong H.J., Chernoff J., Bokoch G.M. Regulation of human leukocyte p21-activated kinases through G protein-coupled receptors. Science. 269:1995;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
  • 26
    • 0034747401 scopus 로고    scopus 로고
    • β1PIX, the PAK-interacting exchange factor, requires localization via a coiled-coil region to promote microvillus-like structures and membrane ruffles
    • Koh C.-G., Manser E., Zhao Z.-S., Ng C.-P., Lim L. β1PIX, the PAK-interacting exchange factor, requires localization via a coiled-coil region to promote microvillus-like structures and membrane ruffles. J. Cell Sci. 114:2001;4239-4251
    • (2001) J. Cell Sci. , vol.114 , pp. 4239-4251
    • Koh, C.-G.1    Manser, E.2    Zhao, Z.-S.3    Ng, C.-P.4    Lim, L.5
  • 27
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts
    • Kozma R., Ahmed S., Best A., Lim L. The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3T3 fibroblasts. Mol. Cell. Biol. 15:1995;1942-1952
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1942-1952
    • Kozma, R.1    Ahmed, S.2    Best, A.3    Lim, L.4
  • 28
    • 0030040750 scopus 로고    scopus 로고
    • Protein kinase a phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes
    • Lang P., Gesbert F., Delespine-Carmagnat M., Stancou R., Pouchelet M., Bertoglio J. Protein kinase A phosphorylation of RhoA mediates the morphological and functional effects of cyclic AMP in cytotoxic lymphocytes. EMBO J. 15:1996;510-519
    • (1996) EMBO J. , vol.15 , pp. 510-519
    • Lang, P.1    Gesbert, F.2    Delespine-Carmagnat, M.3    Stancou, R.4    Pouchelet, M.5    Bertoglio, J.6
  • 29
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei M., Lu W., Meng W., Parrini M.C., Eck M.J., Mayer B.J., Harrison S.C. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell. 102:2000;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
  • 30
    • 0027526303 scopus 로고
    • CDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins
    • Lelias J.M., Adra C.N., Wulf G.M., Guillemot J.C., Khagad M., Caput D., Lim B. cDNA cloning of a human mRNA preferentially expressed in hematopoietic cells and with homology to a GDP-dissociation inhibitor for the rho GTP-binding proteins. Proc. Natl. Acad. Sci. USA. 90:1993;1479-1483
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1479-1483
    • Lelias, J.M.1    Adra, C.N.2    Wulf, G.M.3    Guillemot, J.C.4    Khagad, M.5    Caput, D.6    Lim, B.7
  • 31
    • 0028078824 scopus 로고
    • A brain serine/threonine protein kinase activated by Cdc42 and Rac1
    • Manser E., Leung T., Salihuddin H., Zhao Z.S., Lim L. A brain serine/threonine protein kinase activated by Cdc42 and Rac1. Nature. 367:1994;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
    • 0035933870 scopus 로고    scopus 로고
    • Protein kinase C-alpha signals rho-guanine nucleotide dissociation inhibitor phosphorylation and rho activation and regulates the endothelial cell barrier function
    • Mehta D., Rahman A., Malik A.B. Protein kinase C-alpha signals rho-guanine nucleotide dissociation inhibitor phosphorylation and rho activation and regulates the endothelial cell barrier function. J. Biol. Chem. 276:2001;22614-22620
    • (2001) J. Biol. Chem. , vol.276 , pp. 22614-22620
    • Mehta, D.1    Rahman, A.2    Malik, A.B.3
  • 34
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filipodia
    • Nobes C.D., Hall A. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filipodia. Cell. 81:1995;53-62
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 35
    • 0038660689 scopus 로고    scopus 로고
    • P21-activated kinase 1 (PAK1) interacts with the Grb2 adapter protein to couple to growth factor signaling
    • Puto L.A., Pestonjamasp K., King C.C., Bokoch G.M. p21-activated kinase 1 (PAK1) interacts with the Grb2 adapter protein to couple to growth factor signaling. J. Biol. Chem. 278:2003;9388-9393
    • (2003) J. Biol. Chem. , vol.278 , pp. 9388-9393
    • Puto, L.A.1    Pestonjamasp, K.2    King, C.C.3    Bokoch, G.M.4
  • 36
    • 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 A.J., Hall A. The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors. Cell. 70:1992;389-399
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 37
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley A.J., Paterson H.F., Johnston C.L., Diekmann D., Hall A. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:1992;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
  • 38
    • 0027237511 scopus 로고
    • Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes
    • Scherle P., Behrens T., Staudt L.M. Ly-GDI, a GDP-dissociation inhibitor of the RhoA GTP-binding protein, is expressed preferentially in lymphocytes. Proc. Natl. Acad. Sci. USA. 90:1993;7568-7572
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 7568-7572
    • Scherle, P.1    Behrens, T.2    Staudt, L.M.3
  • 40
    • 0242363237 scopus 로고    scopus 로고
    • Yip3 catalyses the dissociation of endosomal Rab-GDI complexes
    • Sivars U., Aivazian D., Pfeffer S.R. Yip3 catalyses the dissociation of endosomal Rab-GDI complexes. Nature. 425:2003;856-859
    • (2003) Nature , vol.425 , pp. 856-859
    • Sivars, U.1    Aivazian, D.2    Pfeffer, S.R.3
  • 41
    • 0019888557 scopus 로고
    • The regulatory component of adenylate cyclase. Purification and properties
    • Sternweis P.C., Northup J.K., Smigel M.D., Gilman A.G. The regulatory component of adenylate cyclase. Purification and properties. J. Biol. Chem. 256:1981;11517-11526
    • (1981) J. Biol. Chem. , vol.256 , pp. 11517-11526
    • Sternweis, P.C.1    Northup, J.K.2    Smigel, M.D.3    Gilman, A.G.4
  • 42
    • 0030846295 scopus 로고    scopus 로고
    • Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein
    • Takahashi K., Sasaki T., Mammoto A., Takaishi K., Kameyama T., Tsukita S., Takai Y. Direct interaction of the Rho GDP dissociation inhibitor with ezrin/radixin/moesin initiates the activation of the Rho small G protein. J. Biol. Chem. 272:1997;23371-23375
    • (1997) J. Biol. Chem. , vol.272 , pp. 23371-23375
    • Takahashi, K.1    Sasaki, T.2    Mammoto, A.3    Takaishi, K.4    Kameyama, T.5    Tsukita, S.6    Takai, Y.7
  • 43
    • 0025295180 scopus 로고
    • Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein
    • Ueda T., Kikuchi A., Ohga N., Yamamoto J., Takai Y. Purification and characterization from bovine brain cytosol of a novel regulatory protein inhibiting the dissociation of GDP from and the subsequent binding of GTP to rhoB p20, a ras p21-like GTP-binding protein. J. Biol. Chem. 265:1990;9373-9380
    • (1990) J. Biol. Chem. , vol.265 , pp. 9373-9380
    • Ueda, T.1    Kikuchi, A.2    Ohga, N.3    Yamamoto, J.4    Takai, Y.5
  • 44
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst L., D'Souza-Schorey C. Rho GTPases and signaling networks. Genes Dev. 11:1997;2295-2322
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2
  • 45
    • 0028239341 scopus 로고
    • The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family: Its properties in comparison with those of Smg GDS
    • Yaku H., Sasaki T., Takai Y. The Dbl oncogene product as a GDP/GTP exchange protein for the Rho family. its properties in comparison with those of Smg GDS Biochem. Biophys. Res. Commun. 198:1994;811-817
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 811-817
    • Yaku, H.1    Sasaki, T.2    Takai, Y.3
  • 46
    • 0037408391 scopus 로고    scopus 로고
    • The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI
    • Yamashita T., Tohyama M. The p75 receptor acts as a displacement factor that releases Rho from Rho-GDI. Nat. Neurosci. 6:2003;461-467
    • (2003) Nat. Neurosci. , vol.6 , pp. 461-467
    • Yamashita, T.1    Tohyama, M.2
  • 47
    • 0032748298 scopus 로고    scopus 로고
    • Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity
    • Zenke F.T., King C.C., Bohl B.P., Bokoch G.M. Identification of a central phosphorylation site in p21-activated kinase regulating autoinhibition and kinase activity. J. Biol. Chem. 274:1999;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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.