메뉴 건너뛰기




Volumn 23, Issue 7, 2003, Pages 2476-2488

GGAPs, a new family of bifunctional GTP-binding and GTPase-activating proteins

Author keywords

[No Author keywords available]

Indexed keywords

ANKYRIN; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; PLECKSTRIN; PROTEIN GGAP; PROTEIN KINASE; UNCLASSIFIED DRUG;

EID: 0037377735     PISSN: 02707306     EISSN: None     Source Type: Journal    
DOI: 10.1128/MCB.23.7.2476-2488.2003     Document Type: Article
Times cited : (54)

References (58)
  • 1
    • 0034269240 scopus 로고    scopus 로고
    • Structural basis for relief of autoinhibition of the Dbl homology domain of protooncogene Vav by tyrosine phosphorylation
    • Aghazadeh, B., W. E. Lowry, X. Y. Huang, and M. K. Rosen. 2000. Structural basis for relief of autoinhibition of the Dbl homology domain of protooncogene Vav by tyrosine phosphorylation. Cell 102:625-633.
    • (2000) Cell , vol.102 , pp. 625-633
    • Aghazadeh, B.1    Lowry, W.E.2    Huang, X.Y.3    Rosen, M.K.4
  • 3
    • 0034644537 scopus 로고    scopus 로고
    • Ras and Rho GTPases: A family reunion
    • Bar-Sagi, D., and A. Hall. 2000. Ras and Rho GTPases: a family reunion. Cell 103:227-238.
    • (2000) Cell , vol.103 , pp. 227-238
    • Bar-Sagi, D.1    Hall, A.2
  • 4
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits
    • Berman, D. M., T. M. Wilkie, and A. G. Gilman. 1996. GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha subunits. Cell 86:445-452.
    • (1996) Cell , vol.86 , pp. 445-452
    • Berman, D.M.1    Wilkie, T.M.2    Gilman, A.G.3
  • 5
    • 0029132785 scopus 로고
    • Intrinsic and GTPase-activating protein-stimulated Ras GTPase assays
    • Bollag, G., and F. McCormick. 1995. Intrinsic and GTPase-activating protein-stimulated Ras GTPase assays. Methods Enzymol. 255:161-170.
    • (1995) Methods Enzymol. , vol.255 , pp. 161-170
    • Bollag, G.1    McCormick, F.2
  • 6
    • 0025010979 scopus 로고
    • The GTPase superfamily: A conserved switch for diverse cell functions
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1990. The GTPase superfamily: a conserved switch for diverse cell functions. Nature 348:125-132.
    • (1990) Nature , vol.348 , pp. 125-132
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 7
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • Bourne, H. R., D. A. Sanders, and F. McCormick. 1991. The GTPase superfamily: conserved structure and molecular mechanism. Nature 349:117-127.
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 8
    • 0031784899 scopus 로고    scopus 로고
    • ASAPI, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src
    • Brown, M. T., J. Andrade, H. Radhakrishna, J. G. Donaldson, J. A. Cooper, and P. A. Randazzo. 1998. ASAPI, a phospholipid-dependent arf GTPase-activating protein that associates with and is phosphorylated by Src. Mol. Cell. Biol. 18:7038-7051.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 7038-7051
    • Brown, M.T.1    Andrade, J.2    Radhakrishna, H.3    Donaldson, J.G.4    Cooper, J.A.5    Randazzo, P.A.6
  • 10
    • 0031002348 scopus 로고    scopus 로고
    • The role of the PH domain in the signal-dependent membrane targeting of Sos
    • Chen, R. H., S. Corbalan-Garcia, and D. Bar-Sagi. 1997. The role of the PH domain in the signal-dependent membrane targeting of Sos. EMBO J. 16: 1351-1359.
    • (1997) EMBO J. , vol.16 , pp. 1351-1359
    • Chen, R.H.1    Corbalan-Garcia, S.2    Bar-Sagi, D.3
  • 13
    • 0033937941 scopus 로고    scopus 로고
    • Regulators and effectors of the ARF GTPases
    • Donaldson, J. G., and C. L. Jackson. 2000. Regulators and effectors of the ARF GTPases. Curr. Opin. Cell Biol. 12:475-482.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 475-482
    • Donaldson, J.G.1    Jackson, C.L.2
  • 14
    • 0034255332 scopus 로고    scopus 로고
    • Localization of G-protein-coupled receptors in health and disease
    • Edwards, S. W., C. M. Tan, and L. E. Limbird. 2000. Localization of G-protein-coupled receptors in health and disease. Trends Pharmacol. Sci. 21:304-308.
    • (2000) Trends Pharmacol. Sci. , vol.21 , pp. 304-308
    • Edwards, S.W.1    Tan, C.M.2    Limbird, L.E.3
  • 15
    • 0032775007 scopus 로고    scopus 로고
    • Regulation of phospholipase D
    • Exton, J. H. 1999. Regulation of phospholipase D. Biochim. Biophys. Acta 1439:121-133.
    • (1999) Biochim. Biophys. Acta , vol.1439 , pp. 121-133
    • Exton, J.H.1
  • 16
    • 0032493808 scopus 로고    scopus 로고
    • Small GTPases minireview series
    • Exton, J. H. 1998. Small GTPases minireview series. J. Biol. Chem. 273: 19923.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19923
    • Exton, J.H.1
  • 17
    • 0033119012 scopus 로고    scopus 로고
    • The expanding spectrum of G protein diseases
    • Farfel, Z., H. R. Bourne, and T. Iiri. 1999. The expanding spectrum of G protein diseases. N. Engl. J. Med. 340:1012-1020.
    • (1999) N. Engl. J. Med. , vol.340 , pp. 1012-1020
    • Farfel, Z.1    Bourne, H.R.2    Iiri, T.3
  • 18
    • 0031452275 scopus 로고    scopus 로고
    • GEFs, GAPs, GDIs and effectors: Taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins
    • Geyer, M., and A. Wittinghofer. 1997. GEFs, GAPs, GDIs and effectors: taking a closer (3D) look at the regulation of Ras-related GTP-binding proteins. Curr. Opin. Struct. Biol. 7:786-792.
    • (1997) Curr. Opin. Struct. Biol. , vol.7 , pp. 786-792
    • Geyer, M.1    Wittinghofer, A.2
  • 19
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman, A. G. 1987. G proteins: transducers of receptor-generated signals. Annu. Rev. Biochem. 56:615-649.
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 20
    • 0033582917 scopus 로고    scopus 로고
    • Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis
    • Goldberg, J. 1999. Structural and functional analysis of the ARF1-ARFGAP complex reveals a role for coatomer in GTP hydrolysis. Cell 96:893-902.
    • (1999) Cell , vol.96 , pp. 893-902
    • Goldberg, J.1
  • 21
    • 0032568874 scopus 로고    scopus 로고
    • G proteins and small GTPases: Distant relatives keep in touch
    • Hall, A. 1998. G proteins and small GTPases: distant relatives keep in touch. Science 280:2074-2075.
    • (1998) Science , vol.280 , pp. 2074-2075
    • Hall, A.1
  • 22
    • 0034729916 scopus 로고    scopus 로고
    • Rho GTPases: Molecular switches that control the organization and dynamics of the actin cytoskeleton
    • Hall, A., and C. D. Nobes. 2000. Rho GTPases: molecular switches that control the organization and dynamics of the actin cytoskeleton. Phil. Trans. R. Soc. Lond. B Biol. Sci. 355:965-970.
    • (2000) Phil. Trans. R. Soc. Lond. B Biol. Sci. , vol.355 , pp. 965-970
    • Hall, A.1    Nobes, C.D.2
  • 24
    • 0034306280 scopus 로고    scopus 로고
    • Cytohesins and centaurins: Mediators of PI 3-kinase-regulated Arf signaling
    • Jackson, T. R., B. G. Kearns, and A. B. Theibert. 2000. Cytohesins and centaurins: mediators of PI 3-kinase-regulated Arf signaling. Trends Biochem. Sci. 25:489-495.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 489-495
    • Jackson, T.R.1    Kearns, B.G.2    Theibert, A.B.3
  • 25
    • 0033617742 scopus 로고    scopus 로고
    • Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro
    • Kikuno, R., T. Nagase, K. Ishikawa, M. Hirosawa, N. Miyajima, A. Tanaka, H. Kotani, N. Nomura, and O. Ohara. 1999. Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro. DNA Res. 6:197-205.
    • (1999) DNA Res. , vol.6 , pp. 197-205
    • Kikuno, R.1    Nagase, T.2    Ishikawa, K.3    Hirosawa, M.4    Miyajima, N.5    Tanaka, A.6    Kotani, H.7    Nomura, N.8    Ohara, O.9
  • 26
    • 0030975196 scopus 로고    scopus 로고
    • Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains
    • Klarlund, J. K., A. Guilherme, J. J. Holik, J. V. Virbasius, A. Chawla, and M. P. Czech. 1997. Signaling by phosphoinositide-3,4,5-trisphosphate through proteins containing pleckstrin and Sec7 homology domains. Science 275:1927-1930.
    • (1997) Science , vol.275 , pp. 1927-1930
    • Klarlund, J.K.1    Guilherme, A.2    Holik, J.J.3    Virbasius, J.V.4    Chawla, A.5    Czech, M.P.6
  • 28
    • 0034636080 scopus 로고    scopus 로고
    • Catecholamines, cardiac beta-adrenergic receptors, and heart failure
    • Lefkowitz, R. J., H. A. Rockman, and W. J. Koch. 2000. Catecholamines, cardiac beta-adrenergic receptors, and heart failure. Circulation 101:1634-1637.
    • (2000) Circulation , vol.101 , pp. 1634-1637
    • Lefkowitz, R.J.1    Rockman, H.A.2    Koch, W.J.3
  • 29
    • 0034604338 scopus 로고    scopus 로고
    • Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch
    • Lei, M., W. Lu, W. Meng, M. C. Parrini, M. J. Eck, B. J. Mayer, and S. C. Harrison. 2000. Structure of PAK1 in an autoinhibited conformation reveals a multistage activation switch. Cell 102:387-397.
    • (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
    • 0025317957 scopus 로고
    • Statistical test of molecular phylogenies
    • Li, W. H., and M. Gouy. 1990. Statistical test of molecular phylogenies. Methods Enzymol. 183:645-659.
    • (1990) Methods Enzymol. , vol.183 , pp. 645-659
    • Li, W.H.1    Gouy, M.2
  • 31
    • 0029947711 scopus 로고    scopus 로고
    • Regulation by cAMP-dependent protein kinease of a G-protein-mediated phospholipase C
    • Liu, M., and M. I. Simon. 1996. Regulation by cAMP-dependent protein kinease of a G-protein-mediated phospholipase C. Nature 382:83-87.
    • (1996) Nature , vol.382 , pp. 83-87
    • Liu, M.1    Simon, M.I.2
  • 32
    • 0023657439 scopus 로고
    • Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes
    • Lowe, D. G., D. J. Capon, E. Delwart, A. Y. Sakaguchi, S. L. Naylor, and D. V. Goeddel. 1987. Structure of the human and murine R-ras genes, novel genes closely related to ras proto-oncogenes. Cell 48:137-146.
    • (1987) Cell , vol.48 , pp. 137-146
    • Lowe, D.G.1    Capon, D.J.2    Delwart, E.3    Sakaguchi, A.Y.4    Naylor, S.L.5    Goeddel, D.V.6
  • 33
    • 0033575873 scopus 로고    scopus 로고
    • Function of Rieger syndrome gene in left-right asymmetry and craniofacial development
    • Lu, M. F., C. Pressman, R. Dyer, R. L. Johnson, and J. F. Martin. 1999. Function of Rieger syndrome gene in left-right asymmetry and craniofacial development. Nature 401:276-278.
    • (1999) Nature , vol.401 , pp. 276-278
    • Lu, M.F.1    Pressman, C.2    Dyer, R.3    Johnson, R.L.4    Martin, J.F.5
  • 34
  • 35
    • 0029056399 scopus 로고
    • A novel serine kinase activated by rac1/CDC42Hs-dependent autophosphorylation is related to PAK65 and STE20
    • Martin, G. A., G. Bollag, F. McCormick, and A. Abo. 1995. A novel serine kinase activated by rac1/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.3    Abo, A.4
  • 38
    • 0032555493 scopus 로고    scopus 로고
    • Molecules in the ARF orbit
    • Moss, J., and M. Vaughan. 1998. Molecules in the ARF orbit. J Biol. Chem. 273:21431-21434.
    • (1998) J Biol. Chem. , vol.273 , pp. 21431-21434
    • Moss, J.1    Vaughan, M.2
  • 39
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: Organizers of transmembrane signals
    • Neer, E. J. 1995. Heterotrimeric G proteins: organizers of transmembrane signals. Cell 80:249-257.
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 40
    • 0036158988 scopus 로고    scopus 로고
    • Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1
    • Parrini, M. C., M. Lei, S. C. Harrison, and B. J. Mayer. 2002. Pak1 kinase homodimers are autoinhibited in trans and dissociated upon activation by Cdc42 and Rac1. Mol. Cell 9:73-83.
    • (2002) Mol. Cell , vol.9 , pp. 73-83
    • Parrini, M.C.1    Lei, M.2    Harrison, S.C.3    Mayer, B.J.4
  • 42
    • 0034104590 scopus 로고    scopus 로고
    • The Ras branch of small GTPases: Ras family members don't fall far from the tree
    • Reuther, G. W., and C. J. Der. 2000. The Ras branch of small GTPases: Ras family members don't fall far from the tree. Curr. Opin. Cell Biol. 12:157-165.
    • (2000) Curr. Opin. Cell Biol. , vol.12 , pp. 157-165
    • Reuther, G.W.1    Der, C.J.2
  • 43
    • 0035575585 scopus 로고    scopus 로고
    • Rho family proteins: Coordinating cell responses
    • Ridley, A. J. 2001. Rho family proteins: coordinating cell responses. Trends Cell Biol. 11:471-477.
    • (2001) Trends Cell Biol. , vol.11 , pp. 471-477
    • Ridley, A.J.1
  • 44
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross, E. M., and T. M. Wilkie. 2000. GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins. Annu. Rev. Biochem. 69:795-827.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 45
    • 0028143698 scopus 로고
    • Mechanisms of intracellular protein transport
    • Rothman, J. E. 1994. Mechanisms of intracellular protein transport. Nature 372:55-63.
    • (1994) Nature , vol.372 , pp. 55-63
    • Rothman, J.E.1
  • 47
    • 0035463289 scopus 로고    scopus 로고
    • Rac'n Rho: The music that shapes a developing embryo
    • Settleman, J. 2001. Rac'n Rho: the music that shapes a developing embryo. Dev. Cell 1:321-331.
    • (2001) Dev. Cell , vol.1 , pp. 321-331
    • Settleman, J.1
  • 48
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon, M. I., M. P. Strathmann, and N. Gautam. 1991. Diversity of G proteins in signal transduction. Science 252:802-808.
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 49
    • 0029924577 scopus 로고    scopus 로고
    • ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain
    • Vitale, N., J. Moss, and M. Vaughan. 1996. ARD1, a 64-kDa bifunctional protein containing an 18-kDa GTP-binding ADP-ribosylation factor domain and a 46-kDa GTPase-activating domain. Proc. Natl. Acad. Sci. USA 93: 1941-1944.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1941-1944
    • Vitale, N.1    Moss, J.2    Vaughan, M.3
  • 50
    • 0032579518 scopus 로고    scopus 로고
    • Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1)
    • Vitale, N., J. Moss, and M. Vaughan. 1998. Molecular characterization of the GTPase-activating domain of ADP-ribosylation factor domain protein 1 (ARD1). J. Biol. Chem. 273:2553-2560.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2553-2560
    • Vitale, N.1    Moss, J.2    Vaughan, M.3
  • 52
    • 0035827554 scopus 로고    scopus 로고
    • Phosphorylation and regulation of G-protein-activated phospholipase C-beta 3 by cGMP-dependent protein kinases
    • Xia, C., Z. Bao, C. Yue, B. M. Sanborn, and M. Liu. 2001. Phosphorylation and regulation of G-protein-activated phospholipase C-beta 3 by cGMP-dependent protein kinases. J. Biol. Chem. 276:19770-19777.
    • (2001) J. Biol. Chem. , vol.276 , pp. 19770-19777
    • Xia, C.1    Bao, Z.2    Yue, C.3    Sanborn, B.M.4    Liu, M.5
  • 53
    • 0035932983 scopus 로고    scopus 로고
    • Regulation of the p21-activated kinase (PAK) by a human Gβ-like WD-repeat protein, hPIP1
    • Xia, C., W. Ma, L. J. Stafford, S. Marcus, W. C. Xiong, and M. Liu. 2001. Regulation of the p21-activated kinase (PAK) by a human Gβ-like WD-repeat protein, hPIP1. Proc. Natl. Acad. Sci. USA 98:6174-6179.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 6174-6179
    • Xia, C.1    Ma, W.2    Stafford, L.J.3    Marcus, S.4    Xiong, W.C.5    Liu, M.6
  • 54
    • 0031025991 scopus 로고    scopus 로고
    • Three-dimensional structure of the tyrosine kinase c-Src
    • Xu, W., S. C. Harrison, and M. J. Eck. 1997. Three-dimensional structure of the tyrosine kinase c-Src. Nature 385:595-602.
    • (1997) Nature , vol.385 , pp. 595-602
    • Xu, W.1    Harrison, S.C.2    Eck, M.J.3
  • 56
    • 0034682668 scopus 로고    scopus 로고
    • The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins
    • Zhang, B., Y. Zhang, Z. Wang, and Y. Zheng. 2000. The role of Mg2+ cofactor in the guanine nucleotide exchange and GTP hydrolysis reactions of Rho family GTP-binding proteins. J. Biol. Chem. 275:25299-25307.
    • (2000) J. Biol. Chem. , vol.275 , pp. 25299-25307
    • Zhang, B.1    Zhang, Y.2    Wang, Z.3    Zheng, Y.4
  • 57
    • 0027504343 scopus 로고
    • Biochemical comparisons of the Saccharomyces cerevisiac Bem2 and Bem3 proteins. Delineation of a limit Cdc42 GTPase-activating protein domain
    • Zheng, Y., M. J. Hart, K. Shinjo, T. Evans, A. Bender, and R. A. Cerione. 1993. Biochemical comparisons of the Saccharomyces cerevisiac Bem2 and Bem3 proteins. Delineation of a limit Cdc42 GTPase-activating protein domain. J. Biol. Chem. 268:24629-24634.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24629-24634
    • Zheng, Y.1    Hart, M.J.2    Shinjo, K.3    Evans, T.4    Bender, A.5    Cerione, R.A.6
  • 58
    • 0035487646 scopus 로고    scopus 로고
    • The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway
    • Zhou, Z., E. Caron, E. Hartwieg, A. Hall, and H. R. Horvitz. 2001. The C. elegans PH domain protein CED-12 regulates cytoskeletal reorganization via a Rho/Rac GTPase signaling pathway. Dev. Cell 1:477-489.
    • (2001) Dev. Cell , vol.1 , pp. 477-489
    • Zhou, Z.1    Caron, E.2    Hartwieg, E.3    Hall, A.4    Horvitz, H.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.