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Volumn 19, Issue 10, 1999, Pages 6585-6597

The Borgs, a new family of Cdc42 and TC10 GTPase-interacting proteins

Author keywords

[No Author keywords available]

Indexed keywords

BINDING PROTEIN; CELL CYCLE PROTEIN;

EID: 0032851813     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.19.10.6585     Document Type: Article
Times cited : (111)

References (56)
  • 1
    • 0032538973 scopus 로고    scopus 로고
    • PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia
    • Abo, A., J. Qu, M. S. Cammarano, C. Dan, A. Fritsch, V. Baud, B. Belisle, and A. Minden. 1998. PAK4, a novel effector for Cdc42Hs, is implicated in the reorganization of the actin cytoskeleton and in the formation of filopodia. EMBO J. 17:6527-6540.
    • (1998) EMBO J. , vol.17 , pp. 6527-6540
    • Abo, A.1    Qu, J.2    Cammarano, M.S.3    Dan, C.4    Fritsch, A.5    Baud, V.6    Belisle, B.7    Minden, A.8
  • 2
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia, S., B. Derijard, R. J. Davis, and R. A. Cerione. 1995. Cdc42 and PAK-mediated signaling leads to Jun kinase 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
  • 3
    • 0026629286 scopus 로고
    • cDNA cloning and molecular characterization of MSE55, a novel human serum constituent protein that displays bone marrow stromal/endothelial cell-specific expression
    • Bahou, W. F., A. D. Campbell, and M. S. Wicha. 1992. cDNA cloning and molecular characterization of MSE55, a novel human serum constituent protein that displays bone marrow stromal/endothelial cell-specific expression. J. Biol. Chem. 267:13986-13992.
    • (1992) J. Biol. Chem. , vol.267 , pp. 13986-13992
    • Bahou, W.F.1    Campbell, A.D.2    Wicha, M.S.3
  • 4
    • 0000715366 scopus 로고
    • Site-directed mutagenesis by double polymerase chain reaction: Megaprimer method
    • B. A. White (ed.). Humana Press, Totowa, N.J.
    • Barik, S. 1993. Site-directed mutagenesis by double polymerase chain reaction: megaprimer method, p. 277-286. In B. A. White (ed.), PCR protocols: current methods and applications. Humana Press, Totowa, N.J.
    • (1993) PCR Protocols: Current Methods and Applications , pp. 277-286
    • Barik, S.1
  • 5
    • 0032487438 scopus 로고    scopus 로고
    • Fibronectin matrix regulates activation of Rho and Cdc42 GTPases and cell cycle progression
    • Bourdoulous, S., G. Orend, D. A. MacKenna, R. Pasqualini, and E. Ruoslahti. 1998. Fibronectin matrix regulates activation of Rho and Cdc42 GTPases and cell cycle progression. J. Cell Biol. 143:267-276.
    • (1998) J. Cell Biol. , vol.143 , pp. 267-276
    • Bourdoulous, S.1    Orend, G.2    MacKenna, D.A.3    Pasqualini, R.4    Ruoslahti, E.5
  • 6
    • 0028860327 scopus 로고
    • Interaction cloning of rabin3, a novel protein that associates with the Ras-like GTPase Rab3A
    • Brondyk, W. H., C. J. McKiernan, K. A. Fortner, P. Stabila, R. W. Holz, and I. G. Macara. 1995. Interaction cloning of Rabin3, a novel protein that associates with the Ras-like GTPase Rab3A. Mol. Cell. Biol. 15:1137-1143.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 1137-1143
    • Brondyk, W.H.1    McKiernan, C.J.2    Fortner, K.A.3    Stabila, P.4    Holz, R.W.5    Macara, I.G.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
  • 9
    • 0029995797 scopus 로고    scopus 로고
    • Rho-stimulated contractility drives the formation of stress fibers and focal adhesions
    • Chrzanowska-Wodnicka, M., and K. Burridge. 1996. Rho-stimulated contractility drives the formation of stress fibers and focal adhesions. J. Cell Biol. 133:1403-1415.
    • (1996) J. Cell Biol. , vol.133 , pp. 1403-1415
    • Chrzanowska-Wodnicka, M.1    Burridge, K.2
  • 10
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E. A., and J. S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science 268:233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 11
    • 0032572557 scopus 로고    scopus 로고
    • Integrin-mediated signals regulated by members of the Rho family of GTPases
    • Clark, E. A., W. G. King, J. S. Brugge, M. Symons, and R. O. Hynes. 1998. Integrin-mediated signals regulated by members of the Rho family of GTPases. J. Cell Biol. 142:573-586.
    • (1998) J. Cell Biol. , vol.142 , pp. 573-586
    • Clark, E.A.1    King, W.G.2    Brugge, J.S.3    Symons, M.4    Hynes, R.O.5
  • 12
    • 0029055812 scopus 로고
    • The small GTP-binding proteins Rac1 and Cdc42 regulate the activity of the JNK/SAPK signaling 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 signaling 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
  • 13
    • 0030047481 scopus 로고    scopus 로고
    • Signaling from G protein-coupled receptors to c-Jun kinase involves beta gamma subunits of heterotrimeric G proteins acting on a Ras and Rac1-dependent pathway
    • Coso, O. A., H. Teramoto, W. F. Simonds, and J. S. Gutkind. 1996. Signaling from G protein-coupled receptors to c-Jun kinase involves beta gamma subunits of heterotrimeric G proteins acting on a Ras and Rac1-dependent pathway. J. Biol. Chem. 271:3963-3966.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3963-3966
    • Coso, O.A.1    Teramoto, H.2    Simonds, W.F.3    Gutkind, J.S.4
  • 14
    • 0025230372 scopus 로고
    • Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line
    • Drivas, G. T., A. Shih, E. Coutavas, M. G. Rush, and P. D'Eustachio. 1990. Characterization of four novel ras-like genes expressed in a human teratocarcinoma cell line. Mol. Cell. Biol. 10:1793-1798.
    • (1990) Mol. Cell. Biol. , vol.10 , pp. 1793-1798
    • Drivas, G.T.1    Shih, A.2    Coutavas, E.3    Rush, M.G.4    D'Eustachio, P.5
  • 15
    • 0031877714 scopus 로고    scopus 로고
    • RhoE regulates actin cytoskeleton organization and cell migration
    • Guasch, R. M., P. Scambler, G. E. Jones, and A. J. Ridley. 1998. RhoE regulates actin cytoskeleton organization and cell migration. Mol. Cell. Biol. 18:4761-4771.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4761-4771
    • Guasch, R.M.1    Scambler, P.2    Jones, G.E.3    Ridley, A.J.4
  • 16
    • 0032559362 scopus 로고    scopus 로고
    • Rho GTPases and the actin cytoskeleton
    • Hall, A. 1998. Rho GTPases and the actin cytoskeleton. Science 279:509-514.
    • (1998) Science , vol.279 , pp. 509-514
    • Hall, A.1
  • 17
    • 0027958423 scopus 로고
    • Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product
    • Hart, M. J., A. Eva, D. Zangrilli, S. A. Aaronson, T. Evans, R. A. Cerione, and Y. Zheng. 1994. Cellular transformation and guanine nucleotide exchange activity are catalyzed by a common domain on the dbl oncogene product. J. Biol. Chem. 269:62-65.
    • (1994) J. Biol. Chem. , vol.269 , pp. 62-65
    • Hart, M.J.1    Eva, A.2    Zangrilli, D.3    Aaronson, S.A.4    Evans, T.5    Cerione, R.A.6    Zheng, Y.7
  • 18
    • 0030918591 scopus 로고    scopus 로고
    • MST/MLK2, a member of the mixed lineage kinase family, directly phosphorylates and activates SEK1, an activator of c-Jun N-terminal kinase/stress-activated protein kinase
    • Hirai, S., M. Katoh, M. Terada, J. M. Kyriakis, L. I. Zon, A. Rana, J. Avruch, and S. Ohno. 1997. MST/MLK2, a member of the mixed lineage kinase family, directly phosphorylates and activates SEK1, an activator of c-Jun N-terminal kinase/stress-activated protein kinase. J. Biol. Chem. 272:15167-15173.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15167-15173
    • Hirai, S.1    Katoh, M.2    Terada, M.3    Kyriakis, J.M.4    Zon, L.I.5    Rana, A.6    Avruch, J.7    Ohno, S.8
  • 19
    • 0029562867 scopus 로고
    • The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular Rho/Rac GTPases
    • Hotchin, N. A., and A. Hall. 1995. The assembly of integrin adhesion complexes requires both extracellular matrix and intracellular Rho/Rac GTPases. J. Cell Biol. 131:1857-1865.
    • (1995) J. Cell Biol. , vol.131 , pp. 1857-1865
    • Hotchin, N.A.1    Hall, A.2
  • 20
    • 0031459917 scopus 로고    scopus 로고
    • Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through Pi(3)K
    • Keely, P. J., J. K. Westwick, I. P. Whitehead, C. J. Der, and L. V. Parise. 1997. Cdc42 and Rac1 induce integrin-mediated cell motility and invasiveness through Pi(3)K. Nature 390:632-636.
    • (1997) Nature , vol.390 , pp. 632-636
    • Keely, P.J.1    Westwick, J.K.2    Whitehead, I.P.3    Der, C.J.4    Parise, L.V.5
  • 22
    • 0022552131 scopus 로고
    • Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes
    • Kozak, M. 1986. Point mutations define a sequence flanking the AUG initiator codon that modulates translation by eukaryotic ribosomes. Cell 44:283-292.
    • (1986) Cell , vol.44 , pp. 283-292
    • Kozak, M.1
  • 23
    • 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
  • 24
    • 0030298138 scopus 로고    scopus 로고
    • Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of P65(Pak) and the JNK/SAPk map kinase cascade
    • Lamarche, N., N. Tapon, L. Stowers, P. D. Burbelo, P. Aspenstrom, T. Bridges, J. Chant, and A. Hall. 1996. Rac and Cdc42 induce actin polymerization and G1 cell cycle progression independently of P65(Pak) and the JNK/SAPk map kinase cascade. Cell 87:519-529.
    • (1996) Cell , vol.87 , pp. 519-529
    • Lamarche, N.1    Tapon, N.2    Stowers, L.3    Burbelo, P.D.4    Aspenstrom, P.5    Bridges, T.6    Chant, J.7    Hall, A.8
  • 25
    • 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
  • 26
    • 0030222377 scopus 로고    scopus 로고
    • Rho - A connection between membrane receptor signalling and the cytoskeleton
    • Machesky, L. M., and A. Hall. 1996. Rho - a connection between membrane receptor signalling and the cytoskeleton. Trends Cell Biol. 6:304-310.
    • (1996) Trends Cell Biol. , vol.6 , pp. 304-310
    • Machesky, L.M.1    Hall, A.2
  • 27
    • 0032585538 scopus 로고    scopus 로고
    • Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex
    • Machesky, L. M., and R. H. Insall. 1998. Scar1 and the related Wiskott-Aldrich syndrome protein, WASP, regulate the actin cytoskeleton through the Arp2/3 complex. Curr. Biol. 8:1347-1356.
    • (1998) Curr. Biol. , vol.8 , pp. 1347-1356
    • Machesky, L.M.1    Insall, R.H.2
  • 28
    • 0030756973 scopus 로고    scopus 로고
    • Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization
    • Machesky, L. M., and A. Hall. 1997. Role of actin polymerization and adhesion to extracellular matrix in Rac- and Rho-induced cytoskeletal reorganization. J. Cell Biol. 138:913-926.
    • (1997) J. Cell Biol. , vol.138 , pp. 913-926
    • Machesky, L.M.1    Hall, A.2
  • 29
    • 0030872949 scopus 로고    scopus 로고
    • Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: An essential role for ezrin/radixin/moesin proteins
    • Mackay, D. J., F. Esch, H. Furthmayr, and A. Hall. 1997. Rho- and Rac-dependent assembly of focal adhesion complexes and actin filaments in permeabilized fibroblasts: an essential role for ezrin/radixin/moesin proteins. J. Cell Biol. 138:927-938.
    • (1997) J. Cell Biol. , vol.138 , pp. 927-938
    • Mackay, D.J.1    Esch, F.2    Furthmayr, H.3    Hall, A.4
  • 30
    • 0031952518 scopus 로고    scopus 로고
    • Induction of filopodium formation by a Wasp-related actin-depolymerizing protein N-Wasp
    • Miki, H., T. Sasaki, Y. Takai, and T. Takenawa. 1998. Induction of filopodium formation by a Wasp-related actin-depolymerizing protein N-Wasp. Nature 391:93-96.
    • (1998) Nature , vol.391 , pp. 93-96
    • Miki, H.1    Sasaki, T.2    Takai, Y.3    Takenawa, T.4
  • 31
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling 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 signaling 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
  • 32
    • 0033531237 scopus 로고    scopus 로고
    • A balance of signaling by Rho family small GTPases RhoA, Rac1 and Cdc42 coordinates cytoskeletal morphology but not cell survival
    • Moorman, J. P., D. Luu, J. Wickham, D. A. Bobak, and C. S. Hahn. 1999. A balance of signaling by Rho family small GTPases RhoA, Rac1 and Cdc42 coordinates cytoskeletal morphology but not cell survival. Oncogene 18:47-57.
    • (1999) Oncogene , vol.18 , pp. 47-57
    • Moorman, J.P.1    Luu, D.2    Wickham, J.3    Bobak, D.A.4    Hahn, C.S.5
  • 33
    • 0032558696 scopus 로고    scopus 로고
    • Distinct cellular effects and interactions of the Rho-family GTPase TC10
    • Neudauer, C. L., G. Joberty, N. Tatsis, and I. G. Macara. 1998. Distinct cellular effects and interactions of the Rho-family GTPase TC10. Curr. Biol. 8:1151-1160.
    • (1998) Curr. Biol. , vol.8 , pp. 1151-1160
    • Neudauer, C.L.1    Joberty, G.2    Tatsis, N.3    Macara, I.G.4
  • 34
    • 0033594123 scopus 로고    scopus 로고
    • Rho GTPases control polarity, protrusion, and adhesion during cell movement
    • Nobes, C., D. and Hall, A. 1999. Rho GTPases control polarity, protrusion, and adhesion during cell movement. J. Cell Biol. 144:1235-1244.
    • (1999) J. Cell Biol. , vol.144 , pp. 1235-1244
    • Nobes, C.D.1    Hall, A.2
  • 35
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 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
  • 36
    • 0032489841 scopus 로고    scopus 로고
    • A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion
    • Nobes, C. D., I. Lauritzen, M. G. Mattei, S. Paris, A. Hall, and P. Chardin. 1998. A new member of the Rho family, Rnd1, promotes disassembly of actin filament structures and loss of cell adhesion. J. Cell Biol. 141:187-197.
    • (1998) J. Cell Biol. , vol.141 , pp. 187-197
    • Nobes, C.D.1    Lauritzen, I.2    Mattei, M.G.3    Paris, S.4    Hall, A.5    Chardin, P.6
  • 37
    • 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
  • 38
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X.-D., W. B. Kiosses, and M. A. Schwartz. 1999. Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18:578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.-D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 39
    • 0030766846 scopus 로고    scopus 로고
    • Growth factor activation of MAP kinase requires cell adhesion
    • Renshaw, M. W., X.-D. Ren, and M. A. Schwartz. 1997 Growth factor activation of MAP kinase requires cell adhesion. EMBO J. 16:5592-5599.
    • (1997) EMBO J. , vol.16 , pp. 5592-5599
    • Renshaw, M.W.1    Ren, X.-D.2    Schwartz, M.A.3
  • 40
    • 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., and A. Hall. 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
  • 41
    • 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
  • 42
    • 0033574722 scopus 로고    scopus 로고
    • The interaction between N-WASP and the Arp2/3 complex links Cdc42-dependent signals to actin assembly
    • Rohatgi, R., L. Ma, H. Miki, M. Lopez, T. Kirchhausen, T. Takenawa, and M. W. Kischner. 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    Kischner, M.W.7
  • 44
    • 0032583205 scopus 로고    scopus 로고
    • Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase
    • Sander, E. E., S. van Delft, J. P. den Klooster, T. Reid, R. A. van der Kammen, F. Michiels, and J. G. Collard. 1998. Matrix-dependent Tiam1/Rac signaling in epithelial cells promotes either cell-cell adhesion or cell migration and is regulated by phosphatidylinositol 3-kinase. J. Cell Biol. 143:1385-1398.
    • (1998) J. Cell Biol. , vol.143 , pp. 1385-1398
    • Sander, E.E.1    Van Delft, S.2    Den Klooster, J.P.3    Reid, T.4    Van Der Kammen, R.A.5    Michiels, F.6    Collard, J.G.7
  • 45
    • 0033605738 scopus 로고    scopus 로고
    • Inhibition of myosin light chain kinase by p21-activated kinase
    • Sanders, L. C., F. Matsumura, G. M. Bokoch, and P. de Lanerolle. 1999. Inhibition of myosin light chain kinase by p21-activated kinase. Science 283:2083-2085.
    • (1999) Science , vol.283 , pp. 2083-2085
    • Sanders, L.C.1    Matsumura, F.2    Bokoch, G.M.3    De Lanerolle, P.4
  • 47
    • 0033577902 scopus 로고    scopus 로고
    • p21-Activated kinase (Pak1) regulates cell motility in mammalian fibroblasts
    • Sells, M. A., J. T. Boyd, and J. Chernoff. 1999. p21-Activated kinase (Pak1) regulates cell motility in mammalian fibroblasts. J. Cell Biol. 145:837-849.
    • (1999) J. Cell Biol. , vol.145 , pp. 837-849
    • Sells, M.A.1    Boyd, J.T.2    Chernoff, J.3
  • 48
  • 49
    • 0032538888 scopus 로고    scopus 로고
    • The essential role of profilin in the assembly of actin for microspike formation
    • Suetsugu, S., H. Miki, and T. Takenawa. 1998. The essential role of profilin in the assembly of actin for microspike formation. EMBO J. 17:6516-6526.
    • (1998) EMBO J. , vol.17 , pp. 6516-6526
    • Suetsugu, S.1    Miki, H.2    Takenawa, T.3
  • 50
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in Mdck cells
    • Takaishi, K., T. Sasaki, H. Kotani, H. Nishioka, and Y. Takai. 1997. Regulation of cell-cell adhesion by Rac and Rho small G proteins in Mdck cells. J. Cell Biol. 139:1047-1059.
    • (1997) J. Cell Biol. , vol.139 , pp. 1047-1059
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 51
    • 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
  • 52
    • 0032473569 scopus 로고    scopus 로고
    • A new Rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways
    • Tapon, N., K. Nagata, N. Lamarche, and A. Hall. 1998. A new Rac target POSH is an SH3-containing scaffold protein involved in the JNK and NF-kappaB signalling pathways. EMBO J. 17:1395-1404.
    • (1998) EMBO J. , vol.17 , pp. 1395-1404
    • Tapon, N.1    Nagata, K.2    Lamarche, N.3    Hall, A.4
  • 53
    • 0032545394 scopus 로고    scopus 로고
    • The function of the p190 Rho GTPase-activating protein is controlled by its N-terminal GTP binding domain
    • Tatsis, N., D. A. Lannigan, and I. G. Macara. 1998. The function of the p190 Rho GTPase-activating protein is controlled by its N-terminal GTP binding domain. J. Biol. Chem. 273:34631-34638.
    • (1998) J. Biol. Chem. , vol.273 , pp. 34631-34638
    • Tatsis, N.1    Lannigan, D.A.2    Macara, I.G.3
  • 54
    • 0025908897 scopus 로고
    • The Ras protein family: Evolutionary tree and role of conserved amino acids
    • Valencia, A., P. Chardin, A. Wittinghofer, and C. Sander. 1991. The Ras protein family: evolutionary tree and role of conserved amino acids. Bio-chemistry 30:4637-4648.
    • (1991) Bio-chemistry , vol.30 , pp. 4637-4648
    • Valencia, A.1    Chardin, P.2    Wittinghofer, A.3    Sander, C.4
  • 55
    • 0030968580 scopus 로고    scopus 로고
    • Rho GTPases and signaling networks
    • Van Aelst, L., and C. D'Souza-Schorey. 1997. Rho GTPases and signaling networks. Genes Dev. 11:2295-2322.
    • (1997) Genes Dev. , vol.11 , pp. 2295-2322
    • Van Aelst, L.1    D'Souza-Schorey, C.2


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