메뉴 건너뛰기




Volumn 50, Issue 6, 2011, Pages 1070-1080

A minimal Rac activation domain in the unconventional guanine nucleotide exchange factor Dock180

Author keywords

[No Author keywords available]

Indexed keywords

NUCLEOTIDES;

EID: 79851477638     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi100971y     Document Type: Article
Times cited : (10)

References (48)
  • 1
    • 1442274703 scopus 로고    scopus 로고
    • Cdc42: New roads to travel
    • DOI 10.1016/j.tcb.2004.01.008, PII S0962892404000303
    • Cerione, R. A. (2004) Cdc42: New roads to (Pubitemid 38293455)
    • (2004) Trends in Cell Biology , vol.14 , Issue.3 , pp. 127-132
    • Cerione, R.A.1
  • 2
    • 0023813290 scopus 로고
    • The ras superfamily proteins
    • Chardin, P. (1988) The ras superfamily proteins Biochimie 70, 865-868
    • (1988) Biochimie , vol.70 , pp. 865-868
    • Chardin, P.1
  • 3
    • 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., and Hall, A. (1992) The small GTP-binding protein rac regulates growth factor-induced membrane ruffling Cell 70, 401-410
    • (1992) Cell , vol.70 , pp. 401
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 4
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon, N. and Hall, A. (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
    • Tapon, N.1    Hall, A.2
  • 5
    • 0141756144 scopus 로고    scopus 로고
    • Role of Rho-family proteins in cell adhesion and cancer
    • Malliri, A. and Collard, J. G. (2003) Role of Rho-family proteins in cell adhesion and cancer Curr. Opin. Cell Biol. 15, 583-589
    • (2003) Curr. Opin. Cell Biol. , vol.15 , pp. 583
    • Malliri, A.1    Collard, J.G.2
  • 6
    • 0031762533 scopus 로고    scopus 로고
    • Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP
    • Nassar, N., Hoffman, G. R., Manor, D., Clardy, J. C., and Cerione, R. A. (1998) Structures of Cdc42 bound to the active and catalytically compromised forms of Cdc42GAP Nat. Struct. Biol. 5, 1047-1052
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 1047
    • Nassar, N.1    Hoffman, G.R.2    Manor, D.3    Clardy, J.C.4    Cerione, R.A.5
  • 7
    • 0037138364 scopus 로고    scopus 로고
    • Signaling to the Rho GTPases: Networking with the DH domain
    • Hoffman, G. R. and Cerione, R. A. (2002) Signaling to the Rho GTPases: Networking with the DH domain FEBS Lett. 513, 85-91
    • (2002) FEBS Lett. , vol.513 , pp. 85
    • Hoffman, G.R.1    Cerione, R.A.2
  • 8
    • 69949132404 scopus 로고    scopus 로고
    • New insights into how the Rho guanine nucleotide dissociation inhibitor regulates the interaction of Cdc42 with membranes
    • Johnson, J. L., Erickson, J. W., and Cerione, R. A. (2009) New insights into how the Rho guanine nucleotide dissociation inhibitor regulates the interaction of Cdc42 with membranes J. Biol. Chem. 284, 23860-23871
    • (2009) J. Biol. Chem. , vol.284 , pp. 23860
    • Johnson, J.L.1    Erickson, J.W.2    Cerione, R.A.3
  • 9
    • 0026044409 scopus 로고
    • Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product
    • Hart, M. J., Eva, A., Evans, T., Aaronson, S. A., and Cerione, R. A. (1991) Catalysis of guanine nucleotide exchange on the CDC42Hs protein by the dbl oncogene product Nature 354, 311-314
    • (1991) Nature , vol.354 , pp. 311
    • Hart, M.J.1    Eva, A.2    Evans, T.3    Aaronson, S.A.4    Cerione, R.A.5
  • 10
    • 0030586326 scopus 로고    scopus 로고
    • Chromosomal mapping of the gene encoding DOCK180, a major Crk-binding protein, to 10q26.13-q26.3 by fluorescence in situ hybridization
    • Takai, S., Hasegawa, H., Kiyokawa, E., Yamada, K., Kurata, T., and Matsuda, M. (1996) Chromosomal mapping of the gene encoding DOCK180, a major Crk-binding protein, to 10q26.13-q26.3 by fluorescence in situ hybridization Genomics 35, 403-404
    • (1996) Genomics , vol.35 , pp. 403
    • Takai, S.1    Hasegawa, H.2    Kiyokawa, E.3    Yamada, K.4    Kurata, T.5    Matsuda, M.6
  • 12
    • 0942279704 scopus 로고    scopus 로고
    • Structural elements, mechanism, and evolutionary convergence of Rho protein-guanine nucleotide exchange factor complexes
    • Erickson, J. W. and Cerione, R. A. (2004) Structural elements, mechanism, and evolutionary convergence of Rho protein-guanine nucleotide exchange factor complexes Biochemistry 43, 837-842
    • (2004) Biochemistry , vol.43 , pp. 837
    • Erickson, J.W.1    Cerione, R.A.2
  • 13
    • 1642368421 scopus 로고    scopus 로고
    • The RhoA- and CDC42-specific exchange factor Dbs promotes expansion of immature thymocytes and deletion of double-positive and single-positive thymocytes
    • Klinger, M. B., Guilbault, B., and Kay, R. J. (2004) The RhoA- and CDC42-specific exchange factor Dbs promotes expansion of immature thymocytes and deletion of double-positive and single-positive thymocytes Eur. J. Immunol. 34, 806-816
    • (2004) Eur. J. Immunol. , vol.34 , pp. 806
    • Klinger, M.B.1    Guilbault, B.2    Kay, R.J.3
  • 14
    • 0022886091 scopus 로고
    • Identification of the protein encoded by the human diffuse B-cell lymphoma (dbl) oncogene
    • Srivastava, S. K., Wheelock, R. H., Aaronson, S. A., and Eva, A. (1986) Identification of the protein encoded by the human diffuse B-cell lymphoma (dbl) oncogene Proc. Natl. Acad. Sci. U.S.A. 83, 8868-8872
    • (1986) Proc. Natl. Acad. Sci. U.S.A. , vol.83 , pp. 8868
    • Srivastava, S.K.1    Wheelock, R.H.2    Aaronson, S.A.3    Eva, A.4
  • 15
    • 2942613827 scopus 로고    scopus 로고
    • Crystal structure of the DH/PH fragment of Dbs without bound GTPase
    • Worthylake, D. K., Rossman, K. L., and Sondek, J. (2004) Crystal structure of the DH/PH fragment of Dbs without bound GTPase Structure 12, 1078-1086
    • (2004) Structure , vol.12 , pp. 1078
    • Worthylake, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 16
    • 0037085375 scopus 로고    scopus 로고
    • Regulation of the Cool/Pix proteins: Key binding partners of the Cdc42/Rac targets, the p21-activated kinases
    • Feng, Q., Albeck, J. G., Cerione, R. A., and Yang, W. (2002) Regulation of the Cool/Pix proteins: Key binding partners of the Cdc42/Rac targets, the p21-activated kinases J. Biol. Chem. 277, 5644-5650
    • (2002) J. Biol. Chem. , vol.277 , pp. 5644
    • Feng, Q.1    Albeck, J.G.2    Cerione, R.A.3    Yang, W.4
  • 17
    • 4644343782 scopus 로고    scopus 로고
    • Novel regulatory mechanisms for the Dbl family guanine nucleotide exchange factor Cool-2/α-Pix
    • Feng, Q., Baird, D., and Cerione, R. A. (2004) Novel regulatory mechanisms for the Dbl family guanine nucleotide exchange factor Cool-2/α-Pix EMBO J. 23, 3492-3504
    • (2004) EMBO J. , vol.23 , pp. 3492
    • Feng, Q.1    Baird, D.2    Cerione, R.A.3
  • 18
    • 11844280881 scopus 로고    scopus 로고
    • The Cool-2/α-Pix protein mediates a Cdc42-Rac signaling cascade
    • Baird, D., Feng, Q., and Cerione, R. A. (2005) The Cool-2/ α-Pix protein mediates a Cdc42-Rac signaling cascade Curr. Biol. 15, 1-10
    • (2005) Curr. Biol. , vol.15 , pp. 1
    • Baird, D.1    Feng, Q.2    Cerione, R.A.3
  • 20
    • 0037115488 scopus 로고    scopus 로고
    • Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity
    • Cote, J. F. and Vuori, K. (2002) Identification of an evolutionarily conserved superfamily of DOCK180-related proteins with guanine nucleotide exchange activity J. Cell Sci. 115, 4901-4913
    • (2002) J. Cell Sci. , vol.115 , pp. 4901
    • Cote, J.F.1    Vuori, K.2
  • 23
    • 0032473981 scopus 로고    scopus 로고
    • C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180
    • Wu, Y. C. and Horvitz, H. R. (1998) C. elegans phagocytosis and cell-migration protein CED-5 is similar to human DOCK180 Nature 392, 501-504
    • (1998) Nature , vol.392 , pp. 501
    • Wu, Y.C.1    Horvitz, H.R.2
  • 24
    • 0035487807 scopus 로고    scopus 로고
    • C. elegans CED-12 acts in the conserved crkII/DOCK180/Rac pathway to control cell migration and cell corpse engulfment
    • Wu, Y. C., Tsai, M. C., Cheng, L. C., Chou, C. J., and Weng, N. Y. (2001) C. elegans CED-12 acts in the conserved crkII/DOCK180/Rac pathway to control cell migration and cell corpse engulfment Dev. Cell 1, 491-502
    • (2001) Dev. Cell , vol.1 , pp. 491
    • Wu, Y.C.1    Tsai, M.C.2    Cheng, L.C.3    Chou, C.J.4    Weng, N.Y.5
  • 25
    • 11844289581 scopus 로고    scopus 로고
    • Engulfment: Ingestion and migration with Rac, Rho and TRIO
    • DOI 10.1016/j.cub.2004.12.017, PII S0960982204009807
    • Henson, P. M. (2005) Engulfment: Ingestion and migration with Rac, Rho and TRIO Curr. Biol. 15, R29-R30 (Pubitemid 40084693)
    • (2005) Current Biology , vol.15 , Issue.1
    • Henson, P.M.1
  • 27
    • 70450222311 scopus 로고    scopus 로고
    • Cellular signaling of Dock family proteins in neural function
    • Miyamoto, Y. and Yamauchi, J. (2010) Cellular signaling of Dock family proteins in neural function Cell. Signalling 22, 175-182
    • (2010) Cell. Signalling , vol.22 , pp. 175
    • Miyamoto, Y.1    Yamauchi, J.2
  • 28
    • 33748577718 scopus 로고    scopus 로고
    • The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18
    • Watabe-Uchida, M., John, K. A., James, J. A., Newey, S. E., and Van Aelst, L. (2006) The Rac activator DOCK7 regulates neuronal polarity through local phosphorylation of stathmin/Op18 Neuron 51, 727-739
    • (2006) Neuron , vol.51 , pp. 727
    • Watabe-Uchida, M.1    John, K.A.2    James, J.A.3    Newey, S.E.4    Van Aelst, L.5
  • 30
    • 34548472221 scopus 로고    scopus 로고
    • GEF what? Dock180 and related proteins help Rac to polarize cells in new ways
    • Cote, J. F. and Vuori, K. (2007) GEF what? Dock180 and related proteins help Rac to polarize cells in new ways Trends Cell Biol. 17, 383-393
    • (2007) Trends Cell Biol. , vol.17 , pp. 383
    • Cote, J.F.1    Vuori, K.2
  • 33
    • 26244439834 scopus 로고    scopus 로고
    • The DOCK180/Elmo complex couples ARNO-mediated Arf6 activation to the downstream activation of Rac1
    • Santy, L. C., Ravichandran, K. S., and Casanova, J. E. (2005) The DOCK180/Elmo complex couples ARNO-mediated Arf6 activation to the downstream activation of Rac1 Curr. Biol. 15, 1749-1754
    • (2005) Curr. Biol. , vol.15 , pp. 1749
    • Santy, L.C.1    Ravichandran, K.S.2    Casanova, J.E.3
  • 35
    • 70249105718 scopus 로고    scopus 로고
    • Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor
    • Yang, J., Zhang, Z., Roe, S. M., Marshall, C. J., and Barford, D. (2009) Activation of Rho GTPases by DOCK exchange factors is mediated by a nucleotide sensor Science 325, 1398-1402
    • (2009) Science , vol.325 , pp. 1398
    • Yang, J.1    Zhang, Z.2    Roe, S.M.3    Marshall, C.J.4    Barford, D.5
  • 36
    • 0025139701 scopus 로고
    • Expression of epidermal growth factor receptor sequences as E. coli fusion proteins: Applications in the study of tyrosine kinase function
    • Koland, J. G., O’Brien, K. M., and Cerione, R. A. (1990) Expression of epidermal growth factor receptor sequences as E. coli fusion proteins: Applications in the study of tyrosine kinase function Biochem. Biophys. Res. Commun. 166, 90-100
    • (1990) Biochem. Biophys. Res. Commun. , vol.166 , pp. 90
    • Koland, J.G.1    Oâbrien, K.M.2    Cerione, R.A.3
  • 38
    • 23144450821 scopus 로고    scopus 로고
    • A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling
    • Cote, J. F., Motoyama, A. B., Bush, J. A., and Vuori, K. (2005) A novel and evolutionarily conserved PtdIns(3,4,5)P3-binding domain is necessary for DOCK180 signalling Nat. Cell Biol. 7, 797-807
    • (2005) Nat. Cell Biol. , vol.7 , pp. 797
    • Cote, J.F.1    Motoyama, A.B.2    Bush, J.A.3    Vuori, K.4
  • 39
    • 0034619877 scopus 로고    scopus 로고
    • Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1
    • Worthylake, D. K., Rossman, K. L., and Sondek, J. (2000) Crystal structure of Rac1 in complex with the guanine nucleotide exchange region of Tiam1 Nature 408, 682-688
    • (2000) Nature , vol.408 , pp. 682
    • Worthylake, D.K.1    Rossman, K.L.2    Sondek, J.3
  • 40
    • 0035861555 scopus 로고    scopus 로고
    • Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors
    • Gao, Y., Xing, J., Streuli, M., Leto, T. L., and Zheng, Y. (2001) Trp(56) of rac1 specifies interaction with a subset of guanine nucleotide exchange factors J. Biol. Chem. 276, 47530-47541
    • (2001) J. Biol. Chem. , vol.276 , pp. 47530
    • Gao, Y.1    Xing, J.2    Streuli, M.3    Leto, T.L.4    Zheng, Y.5
  • 42
    • 41249095365 scopus 로고    scopus 로고
    • Specific recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 guanine nucleotide exchange factors
    • Kwofie, M. A. and Skowronski, J. (2008) Specific recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 guanine nucleotide exchange factors J. Biol. Chem. 283, 3088-3096
    • (2008) J. Biol. Chem. , vol.283 , pp. 3088
    • Kwofie, M.A.1    Skowronski, J.2
  • 43
    • 32144432437 scopus 로고    scopus 로고
    • The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling
    • Arnold, K., Bordoli, L., Kopp, J., and Schwede, T. (2006) The SWISS-MODEL Workspace: A web-based environment for protein structure homology modelling Bioinformatics 22, 195-201
    • (2006) Bioinformatics , vol.22 , pp. 195
    • Arnold, K.1    Bordoli, L.2    Kopp, J.3    Schwede, T.4
  • 45
    • 15444381280 scopus 로고
    • Protein modeling by E-mail
    • Peitsch, M. C. (1995) Protein modeling by E-mail BioTechnology 13, 658-660
    • (1995) BioTechnology , vol.13 , pp. 658-660
    • Peitsch, M.C.1
  • 46
    • 46249092554 scopus 로고    scopus 로고
    • GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation
    • Hess, B., Kutzner, C., van der spoel, D., and Lindahl, E. (2008) GROMACS 4: Algorithms for Highly Efficient, Load-Balanced, and Scalable Molecular Simulation J. Chem. Theory Comput. 4, 435-447
    • (2008) J. Chem. Theory Comput. , vol.4 , pp. 435
    • Hess, B.1    Kutzner, C.2    Van Der Spoel, D.3    Lindahl, E.4
  • 47
    • 84855229636 scopus 로고    scopus 로고
    • PIC: Protein interactions calculator
    • Tina, K. G., Badra, R., and Srinivasan, N. (2007) PIC: Protein interactions calculator Nucleic Acids Res. 35 (web-server issue) W473-W476
    • (2007) Nucleic Acids Res. , vol.35 , Issue.WEB-SERVER ISSUE , pp. 473
    • Tina, K.G.1    Badra, R.2    Srinivasan, N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.