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Volumn 118, Issue , 2013, Pages 149-174

β-Arrestins: Modulators of small GTPase activation and function

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EID: 84879083659     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394440-5.00006-1     Document Type: Chapter
Times cited : (13)

References (103)
  • 1
    • 84855901533 scopus 로고    scopus 로고
    • Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors
    • E. Reiter, S. Ahn, A.K. Shukla, and R.J. Lefkowitz Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors Annu Rev Pharmacol Toxicol 52 2012 179 197
    • (2012) Annu Rev Pharmacol Toxicol , vol.52 , pp. 179-197
    • Reiter, E.1    Ahn, S.2    Shukla, A.K.3    Lefkowitz, R.J.4
  • 2
    • 80052038573 scopus 로고    scopus 로고
    • Beta-Arrestin-mediated receptor trafficking and signal transduction
    • S.K. Shenoy, and R.J. Lefkowitz beta-Arrestin-mediated receptor trafficking and signal transduction Trends Pharmacol Sci 32 2011 521 533
    • (2011) Trends Pharmacol Sci , vol.32 , pp. 521-533
    • Shenoy, S.K.1    Lefkowitz, R.J.2
  • 4
    • 0019440568 scopus 로고
    • Analysis of two divergent rat genomic clones homologous to the transforming gene of Harvey murine sarcoma virus
    • D. DeFeo, M.A. Gonda, and H.A. Young Analysis of two divergent rat genomic clones homologous to the transforming gene of Harvey murine sarcoma virus Proc Natl Acad Sci USA 78 1981 3328 3332
    • (1981) Proc Natl Acad Sci USA , vol.78 , pp. 3328-3332
    • Defeo, D.1    Gonda, M.A.2    Young, H.A.3
  • 5
    • 0020315258 scopus 로고
    • Human genome contains four genes homologous to transforming genes of Harvey and Kirsten murine sarcoma viruses
    • E.H. Chang, M.A. Gonda, R.W. Ellis, E.M. Scolnick, and D.R. Lowy Human genome contains four genes homologous to transforming genes of Harvey and Kirsten murine sarcoma viruses Proc Natl Acad Sci USA 79 1982 4848 4852
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4848-4852
    • Chang, E.H.1    Gonda, M.A.2    Ellis, R.W.3    Scolnick, E.M.4    Lowy, D.R.5
  • 6
    • 64049090068 scopus 로고    scopus 로고
    • Diesel exhaust particles activate the matrix-metalloproteinase-1 gene in human bronchial epithelia in a beta-arrestin-dependent manner via activation of RAS
    • J. Li, A.J. Ghio, S.H. Cho, C.E. Brinckerhoff, S.A. Simon, and W. Liedtke Diesel exhaust particles activate the matrix-metalloproteinase-1 gene in human bronchial epithelia in a beta-arrestin-dependent manner via activation of RAS Environ Health Perspect 117 2009 400 409
    • (2009) Environ Health Perspect , vol.117 , pp. 400-409
    • Li, J.1    Ghio, A.J.2    Cho, S.H.3    Brinckerhoff, C.E.4    Simon, S.A.5    Liedtke, W.6
  • 7
    • 79953140154 scopus 로고    scopus 로고
    • Demonstration of angiotensin II-induced Ras activation in the trans-Golgi network and endoplasmic reticulum using bioluminescence resonance energy transfer-based biosensors
    • A. Balla, L.S. Erdelyi, E. Soltesz-Katona, T. Balla, P. Varnai, and L. Hunyady Demonstration of angiotensin II-induced Ras activation in the trans-Golgi network and endoplasmic reticulum using bioluminescence resonance energy transfer-based biosensors J Biol Chem 286 2011 5319 5327
    • (2011) J Biol Chem , vol.286 , pp. 5319-5327
    • Balla, A.1    Erdelyi, L.S.2    Soltesz-Katona, E.3    Balla, T.4    Varnai, P.5    Hunyady, L.6
  • 8
    • 14844338481 scopus 로고    scopus 로고
    • Beta-Arrestin 1 and Galpha q/11 coordinately activate RhoA and stress fiber formation following receptor stimulation
    • W.G. Barnes, E. Reiter, J.D. Violin, X.R. Ren, G. Milligan, and R.J. Lefkowitz beta-Arrestin 1 and Galpha q/11 coordinately activate RhoA and stress fiber formation following receptor stimulation J Biol Chem 280 2005 8041 8050
    • (2005) J Biol Chem , vol.280 , pp. 8041-8050
    • Barnes, W.G.1    Reiter, E.2    Violin, J.D.3    Ren, X.R.4    Milligan, G.5    Lefkowitz, R.J.6
  • 9
    • 77149169724 scopus 로고    scopus 로고
    • The small GTPase Ral couples the angiotensin II type 1 receptor to the activation of phospholipase C-delta 1
    • C.M. Godin, L.T. Ferreira, L.B. Dale, R. Gros, S.P. Cregan, and S.S. Ferguson The small GTPase Ral couples the angiotensin II type 1 receptor to the activation of phospholipase C-delta 1 Mol Pharmacol 77 2010 388 395
    • (2010) Mol Pharmacol , vol.77 , pp. 388-395
    • Godin, C.M.1    Ferreira, L.T.2    Dale, L.B.3    Gros, R.4    Cregan, S.P.5    Ferguson, S.S.6
  • 10
    • 34248995559 scopus 로고    scopus 로고
    • Essential role for beta-arrestin 2 in the regulation of Xenopus convergent extension movements
    • G.H. Kim, and J.K. Han Essential role for beta-arrestin 2 in the regulation of Xenopus convergent extension movements EMBO J 26 2007 2513 2526
    • (2007) EMBO J , vol.26 , pp. 2513-2526
    • Kim, G.H.1    Han, J.K.2
  • 11
    • 79952265050 scopus 로고    scopus 로고
    • Beta-Arrestin 1 inhibits the GTPase-activating protein function of ARHGAP21, promoting activation of RhoA following angiotensin II type 1A receptor stimulation
    • D.F. Anthony, Y.Y. Sin, and S. Vadrevu beta-Arrestin 1 inhibits the GTPase-activating protein function of ARHGAP21, promoting activation of RhoA following angiotensin II type 1A receptor stimulation Mol Cell Biol 31 2011 1066 1075
    • (2011) Mol Cell Biol , vol.31 , pp. 1066-1075
    • Anthony, D.F.1    Sin, Y.Y.2    Vadrevu, S.3
  • 12
    • 77951622241 scopus 로고    scopus 로고
    • The fate of the internalized apelin receptor is determined by different isoforms of apelin mediating differential interaction with beta-arrestin
    • D.K. Lee, S.S. Ferguson, S.R. George, and B.F. O'Dowd The fate of the internalized apelin receptor is determined by different isoforms of apelin mediating differential interaction with beta-arrestin Biochem Biophys Res Commun 395 2010 185 189
    • (2010) Biochem Biophys Res Commun , vol.395 , pp. 185-189
    • Lee, D.K.1    Ferguson, S.S.2    George, S.R.3    O'Dowd, B.F.4
  • 13
    • 0035834775 scopus 로고    scopus 로고
    • Beta arrestin-mediated ARF6 activation and beta2-adrenergic receptor endocytosis
    • A. Claing, W. Chen, and W.E. Miller Beta arrestin-mediated ARF6 activation and beta2-adrenergic receptor endocytosis J Biol Chem 276 2001 42509 42513
    • (2001) J Biol Chem , vol.276 , pp. 42509-42513
    • Claing, A.1    Chen, W.2    Miller, W.E.3
  • 14
    • 84869137855 scopus 로고    scopus 로고
    • Arf6 negatively controls the rapid recycling of the beta2AR
    • E. Macia, M. Partisani, O. Paleotti, F. Luton, and M. Franco Arf6 negatively controls the rapid recycling of the beta2AR J Cell Sci 125 2012 4026 4035
    • (2012) J Cell Sci , vol.125 , pp. 4026-4035
    • Macia, E.1    Partisani, M.2    Paleotti, O.3    Luton, F.4    Franco, M.5
  • 15
    • 78650767353 scopus 로고    scopus 로고
    • FYVE-dependent endosomal targeting of an arrestin-related protein in amoeba
    • D. Guetta, K. Langou, D. Grunwald, G. Klein, and L. Aubry FYVE-dependent endosomal targeting of an arrestin-related protein in amoeba PLoS One 5 2010 e15249
    • (2010) PLoS One , vol.5 , pp. 15249
    • Guetta, D.1    Langou, K.2    Grunwald, D.3    Klein, G.4    Aubry, L.5
  • 16
    • 0034705116 scopus 로고    scopus 로고
    • The ADP ribosylation factor nucleotide exchange factor ARNO promotes beta-arrestin release necessary for luteinizing hormone/choriogonadotropin receptor desensitization
    • S. Mukherjee, V.V. Gurevich, and J.C. Jones The ADP ribosylation factor nucleotide exchange factor ARNO promotes beta-arrestin release necessary for luteinizing hormone/choriogonadotropin receptor desensitization Proc Natl Acad Sci USA 97 2000 5901 5906
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 5901-5906
    • Mukherjee, S.1    Gurevich, V.V.2    Jones, J.C.3
  • 17
    • 34548246116 scopus 로고    scopus 로고
    • The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO ARF6 ELMO protein network
    • T. Bouschet, S. Martin, V. Kanamarlapudi, S. Mundell, and J.M. Henley The calcium-sensing receptor changes cell shape via a beta-arrestin-1 ARNO ARF6 ELMO protein network J Cell Sci 120 2007 2489 2497
    • (2007) J Cell Sci , vol.120 , pp. 2489-2497
    • Bouschet, T.1    Martin, S.2    Kanamarlapudi, V.3    Mundell, S.4    Henley, J.M.5
  • 18
    • 18544379729 scopus 로고    scopus 로고
    • Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization
    • M. Bhattacharya, P.H. Anborgh, and A.V. Babwah Beta-arrestins regulate a Ral-GDS Ral effector pathway that mediates cytoskeletal reorganization Nat Cell Biol 4 2002 547 555
    • (2002) Nat Cell Biol , vol.4 , pp. 547-555
    • Bhattacharya, M.1    Anborgh, P.H.2    Babwah, A.V.3
  • 19
    • 77954368879 scopus 로고    scopus 로고
    • Regulation of Weibel-Palade body exocytosis by alpha-synuclein in endothelial cells
    • K.S. Kim, J.Y. Park, I. Jou, and S.M. Park Regulation of Weibel-Palade body exocytosis by alpha-synuclein in endothelial cells J Biol Chem 285 2010 21416 21425
    • (2010) J Biol Chem , vol.285 , pp. 21416-21425
    • Kim, K.S.1    Park, J.Y.2    Jou, I.3    Park, S.M.4
  • 20
    • 10344229472 scopus 로고    scopus 로고
    • Arrestin regulates MAPK activation and prevents NADPH oxidase-dependent death of cells expressing CXCR2
    • M. Zhao, A. Wimmer, K. Trieu, R.G. Discipio, and I.U. Schraufstatter Arrestin regulates MAPK activation and prevents NADPH oxidase-dependent death of cells expressing CXCR2 J Biol Chem 279 2004 49259 49267
    • (2004) J Biol Chem , vol.279 , pp. 49259-49267
    • Zhao, M.1    Wimmer, A.2    Trieu, K.3    Discipio, R.G.4    Schraufstatter, I.U.5
  • 21
    • 57049149000 scopus 로고    scopus 로고
    • Beta-arrestin and casein kinase 1/2 define distinct branches of non-canonical WNT signalling pathways
    • V. Bryja, A. Schambony, L. Cajanek, I. Dominguez, E. Arenas, and G. Schulte Beta-arrestin and casein kinase 1/2 define distinct branches of non-canonical WNT signalling pathways EMBO Rep 9 2008 1244 1250
    • (2008) EMBO Rep , vol.9 , pp. 1244-1250
    • Bryja, V.1    Schambony, A.2    Cajanek, L.3    Dominguez, I.4    Arenas, E.5    Schulte, G.6
  • 22
    • 57649186957 scopus 로고    scopus 로고
    • A novel protein kinase A-independent, beta-arrestin-1-dependent signaling pathway for p38 mitogen-activated protein kinase activation by beta2-adrenergic receptors
    • K. Gong, Z. Li, M. Xu, J. Du, Z. Lv, and Y. Zhang A novel protein kinase A-independent, beta-arrestin-1-dependent signaling pathway for p38 mitogen-activated protein kinase activation by beta2-adrenergic receptors J Biol Chem 283 2008 29028 29036
    • (2008) J Biol Chem , vol.283 , pp. 29028-29036
    • Gong, K.1    Li, Z.2    Xu, M.3    Du, J.4    Lv, Z.5    Zhang, Y.6
  • 23
    • 77949497061 scopus 로고    scopus 로고
    • Light-induced translocation of Drosophila visual arrestin2 depends on Rac2
    • R. Elsaesser, D. Kalra, R. Li, and C. Montell Light-induced translocation of Drosophila visual arrestin2 depends on Rac2 Proc Natl Acad Sci USA 107 2010 4740 4745
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 4740-4745
    • Elsaesser, R.1    Kalra, D.2    Li, R.3    Montell, C.4
  • 24
    • 0037016681 scopus 로고    scopus 로고
    • Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion
    • J.L. Seachrist, S.A. Laporte, and L.B. Dale Rab5 association with the angiotensin II type 1A receptor promotes Rab5 GTP binding and vesicular fusion J Biol Chem 277 2002 679 685
    • (2002) J Biol Chem , vol.277 , pp. 679-685
    • Seachrist, J.L.1    Laporte, S.A.2    Dale, L.B.3
  • 25
    • 36749006304 scopus 로고    scopus 로고
    • Differential regulation of class IA phosphoinositide 3-kinase catalytic subunits p110 alpha and beta by protease-activated receptor 2 and beta-arrestins
    • P. Wang, P. Kumar, C. Wang, and K.A. Defea Differential regulation of class IA phosphoinositide 3-kinase catalytic subunits p110 alpha and beta by protease-activated receptor 2 and beta-arrestins Biochem J 408 2007 221 230
    • (2007) Biochem J , vol.408 , pp. 221-230
    • Wang, P.1    Kumar, P.2    Wang, C.3    Defea, K.A.4
  • 26
    • 66249141288 scopus 로고    scopus 로고
    • The type III TGF-beta receptor regulates epithelial and cancer cell migration through beta-arrestin2-mediated activation of Cdc42
    • K. Mythreye, and G.C. Blobe The type III TGF-beta receptor regulates epithelial and cancer cell migration through beta-arrestin2-mediated activation of Cdc42 Proc Natl Acad Sci USA 106 2009 8221 8226
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 8221-8226
    • Mythreye, K.1    Blobe, G.C.2
  • 27
    • 28444482410 scopus 로고    scopus 로고
    • Beta-Arrestin 1 participates in platelet-activating factor receptor-mediated endocytosis of Streptococcus pneumoniae
    • J.N. Radin, C.J. Orihuela, G. Murti, C. Guglielmo, P.J. Murray, and E.I. Tuomanen beta-Arrestin 1 participates in platelet-activating factor receptor-mediated endocytosis of Streptococcus pneumoniae Infect Immun 73 2005 7827 7835
    • (2005) Infect Immun , vol.73 , pp. 7827-7835
    • Radin, J.N.1    Orihuela, C.J.2    Murti, G.3    Guglielmo, C.4    Murray, P.J.5    Tuomanen, E.I.6
  • 28
    • 0021443368 scopus 로고
    • Mechanism of activation of an N-ras gene in the human fibrosarcoma cell line HT1080
    • R. Brown, C.J. Marshall, S.G. Pennie, and A. Hall Mechanism of activation of an N-ras gene in the human fibrosarcoma cell line HT1080 EMBO J 3 1984 1321 1326
    • (1984) EMBO J , vol.3 , pp. 1321-1326
    • Brown, R.1    Marshall, C.J.2    Pennie, S.G.3    Hall, A.4
  • 29
    • 0020624456 scopus 로고
    • Activation of Ki-ras2 gene in human colon and lung carcinomas by two different point mutations
    • D.J. Capon, P.H. Seeburg, and J.P. McGrath Activation of Ki-ras2 gene in human colon and lung carcinomas by two different point mutations Nature 304 1983 507 513
    • (1983) Nature , vol.304 , pp. 507-513
    • Capon, D.J.1    Seeburg, P.H.2    McGrath, J.P.3
  • 30
    • 0021719520 scopus 로고
    • Microinjection of the oncogene form of the human H-ras (T-24) protein results in rapid proliferation of quiescent cells
    • J.R. Feramisco, M. Gross, T. Kamata, M. Rosenberg, and R.W. Sweet Microinjection of the oncogene form of the human H-ras (T-24) protein results in rapid proliferation of quiescent cells Cell 38 1984 109 117
    • (1984) Cell , vol.38 , pp. 109-117
    • Feramisco, J.R.1    Gross, M.2    Kamata, T.3    Rosenberg, M.4    Sweet, R.W.5
  • 31
    • 0021184853 scopus 로고
    • Transformation of NIH 3 T3 cells by microinjection of Ha-ras p21 protein
    • D.W. Stacey, and H.F. Kung Transformation of NIH 3 T3 cells by microinjection of Ha-ras p21 protein Nature 310 1984 508 511
    • (1984) Nature , vol.310 , pp. 508-511
    • Stacey, D.W.1    Kung, H.F.2
  • 33
    • 0031975838 scopus 로고    scopus 로고
    • Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase
    • Y. Daaka, L.M. Luttrell, and S. Ahn Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase J Biol Chem 273 1998 685 688
    • (1998) J Biol Chem , vol.273 , pp. 685-688
    • Daaka, Y.1    Luttrell, L.M.2    Ahn, S.3
  • 34
    • 0037452623 scopus 로고    scopus 로고
    • Desensitization, internalization, and signaling functions of beta-arrestins demonstrated by RNA interference
    • S. Ahn, C.D. Nelson, T.R. Garrison, W.E. Miller, and R.J. Lefkowitz Desensitization, internalization, and signaling functions of beta-arrestins demonstrated by RNA interference Proc Natl Acad Sci USA 100 2003 1740 1744
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 1740-1744
    • Ahn, S.1    Nelson, C.D.2    Garrison, T.R.3    Miller, W.E.4    Lefkowitz, R.J.5
  • 35
    • 0141593597 scopus 로고    scopus 로고
    • Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors
    • M. Azzi, P.G. Charest, and S. Angers Beta-arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors Proc Natl Acad Sci USA 100 2003 11406 11411
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 11406-11411
    • Azzi, M.1    Charest, P.G.2    Angers, S.3
  • 36
    • 0022779153 scopus 로고
    • The ral gene: A new ras related gene isolated by the use of a synthetic probe
    • P. Chardin, and A. Tavitian The ral gene: a new ras related gene isolated by the use of a synthetic probe EMBO J 5 1986 2203 2208
    • (1986) EMBO J , vol.5 , pp. 2203-2208
    • Chardin, P.1    Tavitian, A.2
  • 37
    • 0041846652 scopus 로고    scopus 로고
    • Ral-GTPases: Approaching their 15 minutes of fame
    • L.A. Feig Ral-GTPases: approaching their 15 minutes of fame Trends Cell Biol 13 2003 419 425
    • (2003) Trends Cell Biol , vol.13 , pp. 419-425
    • Feig, L.A.1
  • 38
    • 0042353628 scopus 로고    scopus 로고
    • RAL GTPases are linchpin modulators of human tumour-cell proliferation and survival
    • Y. Chien, and M.A. White RAL GTPases are linchpin modulators of human tumour-cell proliferation and survival EMBO Rep 4 2003 800 806
    • (2003) EMBO Rep , vol.4 , pp. 800-806
    • Chien, Y.1    White, M.A.2
  • 40
    • 0033029811 scopus 로고    scopus 로고
    • Ras caught in another affair: The exchange factors for Ral
    • R.M. Wolthuis, and J.L. Bos Ras caught in another affair: the exchange factors for Ral Curr Opin Genet Dev 9 1999 112 117
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 112-117
    • Wolthuis, R.M.1    Bos, J.L.2
  • 41
    • 0031472912 scopus 로고    scopus 로고
    • Colocalization of Ras and Ral on the membrane is required for Ras-dependent Ral activation through Ral GDP dissociation stimulator
    • S. Kishida, S. Koyama, K. Matsubara, M. Kishida, Y. Matsuura, and A. Kikuchi Colocalization of Ras and Ral on the membrane is required for Ras-dependent Ral activation through Ral GDP dissociation stimulator Oncogene 15 1997 2899 2907
    • (1997) Oncogene , vol.15 , pp. 2899-2907
    • Kishida, S.1    Koyama, S.2    Matsubara, K.3    Kishida, M.4    Matsuura, Y.5    Kikuchi, A.6
  • 42
    • 0032474731 scopus 로고    scopus 로고
    • Ras-independent activation of Ral by a Ca(2 +)-dependent pathway
    • F. Hofer, R. Berdeaux, and G.S. Martin Ras-independent activation of Ral by a Ca(2 +)-dependent pathway Curr Biol 8 1998 839 842
    • (1998) Curr Biol , vol.8 , pp. 839-842
    • Hofer, F.1    Berdeaux, R.2    Martin, G.S.3
  • 43
    • 0028153277 scopus 로고
    • Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator
    • F. Hofer, S. Fields, C. Schneider, and G.S. Martin Activated Ras interacts with the Ral guanine nucleotide dissociation stimulator Proc Natl Acad Sci USA 91 1994 11089 11093
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 11089-11093
    • Hofer, F.1    Fields, S.2    Schneider, C.3    Martin, G.S.4
  • 44
    • 0028577298 scopus 로고
    • Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap
    • M. Spaargaren, and J.R. Bischoff Identification of the guanine nucleotide dissociation stimulator for Ral as a putative effector molecule of R-ras, H-ras, K-ras, and Rap Proc Natl Acad Sci USA 91 1994 12609 12613
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 12609-12613
    • Spaargaren, M.1    Bischoff, J.R.2
  • 45
    • 78751487053 scopus 로고    scopus 로고
    • RalGDS family members couple Ras to Ral signalling and that's not all
    • E. Ferro, and L. Trabalzini RalGDS family members couple Ras to Ral signalling and that's not all Cell Signal 22 2010 1804 1810
    • (2010) Cell Signal , vol.22 , pp. 1804-1810
    • Ferro, E.1    Trabalzini, L.2
  • 46
    • 0342960383 scopus 로고    scopus 로고
    • Activation of the Ral and phosphatidylinositol 3′ kinase signaling pathways by the ras-related protein TC21
    • M. Rosario, H.F. Paterson, and C.J. Marshall Activation of the Ral and phosphatidylinositol 3′ kinase signaling pathways by the ras-related protein TC21 Mol Cell Biol 21 2001 3750 3762
    • (2001) Mol Cell Biol , vol.21 , pp. 3750-3762
    • Rosario, M.1    Paterson, H.F.2    Marshall, C.J.3
  • 47
    • 0037168163 scopus 로고    scopus 로고
    • Involvement of R-Ras and Ral GTPases in estrogen-independent proliferation of breast cancer cells
    • Y. Yu, and L.A. Feig Involvement of R-Ras and Ral GTPases in estrogen-independent proliferation of breast cancer cells Oncogene 21 2002 7557 7568
    • (2002) Oncogene , vol.21 , pp. 7557-7568
    • Yu, Y.1    Feig, L.A.2
  • 48
    • 0036168098 scopus 로고    scopus 로고
    • The role of Ral A in epidermal growth factor receptor-regulated cell motility
    • J.J. Gildea, M.A. Harding, M.J. Seraj, K.M. Gulding, and D. Theodorescu The role of Ral A in epidermal growth factor receptor-regulated cell motility Cancer Res 62 2002 982 985
    • (2002) Cancer Res , vol.62 , pp. 982-985
    • Gildea, J.J.1    Harding, M.A.2    Seraj, M.J.3    Gulding, K.M.4    Theodorescu, D.5
  • 49
    • 67651151233 scopus 로고    scopus 로고
    • Beta-arrestin/Ral signaling regulates lysophosphatidic acid-mediated migration and invasion of human breast tumor cells
    • T.T. Li, M. Alemayehu, and A.I. Aziziyeh Beta-arrestin/Ral signaling regulates lysophosphatidic acid-mediated migration and invasion of human breast tumor cells Mol Cancer Res 7 2009 1064 1077
    • (2009) Mol Cancer Res , vol.7 , pp. 1064-1077
    • Li, T.T.1    Alemayehu, M.2    Aziziyeh, A.I.3
  • 50
    • 0942279490 scopus 로고    scopus 로고
    • G-protein-coupled receptor-mediated activation of rap GTPases: Characterization of a novel Galphai regulated pathway
    • J.T. Weissman, J.N. Ma, A. Essex, Y. Gao, and E.S. Burstein G-protein-coupled receptor-mediated activation of rap GTPases: characterization of a novel Galphai regulated pathway Oncogene 23 2004 241 249
    • (2004) Oncogene , vol.23 , pp. 241-249
    • Weissman, J.T.1    Ma, J.N.2    Essex, A.3    Gao, Y.4    Burstein, E.S.5
  • 51
    • 0030048696 scopus 로고    scopus 로고
    • Activation of brain B-Raf protein kinase by Rap1B small GTP-binding protein
    • T. Ohtsuka, K. Shimizu, B. Yamamori, S. Kuroda, and Y. Takai Activation of brain B-Raf protein kinase by Rap1B small GTP-binding protein J Biol Chem 271 1996 1258 1261
    • (1996) J Biol Chem , vol.271 , pp. 1258-1261
    • Ohtsuka, T.1    Shimizu, K.2    Yamamori, B.3    Kuroda, S.4    Takai, Y.5
  • 52
    • 1542344841 scopus 로고    scopus 로고
    • Hormonal regulation of phospholipase Cepsilon through distinct and overlapping pathways involving G12 and Ras family G-proteins
    • G.G. Kelley, S.E. Reks, and A.V. Smrcka Hormonal regulation of phospholipase Cepsilon through distinct and overlapping pathways involving G12 and Ras family G-proteins Biochem J 378 2004 129 139
    • (2004) Biochem J , vol.378 , pp. 129-139
    • Kelley, G.G.1    Reks, S.E.2    Smrcka, A.V.3
  • 53
    • 0026778133 scopus 로고
    • The small GTP-binding protein rho regulates the assembly of focal adhesions and actin stress fibers in response to growth factors
    • A.J. Ridley, and A. Hall 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
  • 54
    • 0032977036 scopus 로고    scopus 로고
    • Rho as a mediator of G protein-coupled receptor signaling
    • T.M. Seasholtz, M. Majumdar, and J.H. Brown Rho as a mediator of G protein-coupled receptor signaling Mol Pharmacol 55 1999 949 956
    • (1999) Mol Pharmacol , vol.55 , pp. 949-956
    • Seasholtz, T.M.1    Majumdar, M.2    Brown, J.H.3
  • 55
    • 0033604638 scopus 로고    scopus 로고
    • Signaling to Rho GTPases
    • L. Kjoller, and A. Hall Signaling to Rho GTPases Exp Cell Res 253 1999 166 179
    • (1999) Exp Cell Res , vol.253 , pp. 166-179
    • Kjoller, L.1    Hall, A.2
  • 56
    • 0032489871 scopus 로고    scopus 로고
    • Angiotensin II activates RhoA in cardiac myocytes: A critical role of RhoA in angiotensin II-induced premyofibril formation
    • H. Aoki, S. Izumo, and J. Sadoshima Angiotensin II activates RhoA in cardiac myocytes: a critical role of RhoA in angiotensin II-induced premyofibril formation Circ Res 82 1998 666 676
    • (1998) Circ Res , vol.82 , pp. 666-676
    • Aoki, H.1    Izumo, S.2    Sadoshima, J.3
  • 57
    • 0028973505 scopus 로고
    • G alpha 12 and G alpha 13 stimulate Rho-dependent stress fiber formation and focal adhesion assembly
    • A.M. Buhl, N.L. Johnson, N. Dhanasekaran, and G.L. Johnson G alpha 12 and G alpha 13 stimulate Rho-dependent stress fiber formation and focal adhesion assembly J Biol Chem 270 1995 24631 24634
    • (1995) J Biol Chem , vol.270 , pp. 24631-24634
    • Buhl, A.M.1    Johnson, N.L.2    Dhanasekaran, N.3    Johnson, G.L.4
  • 58
    • 0032568868 scopus 로고    scopus 로고
    • Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13
    • M.J. Hart, X. Jiang, and T. Kozasa Direct stimulation of the guanine nucleotide exchange activity of p115 RhoGEF by Galpha13 Science 280 1998 2112 2114
    • (1998) Science , vol.280 , pp. 2112-2114
    • Hart, M.J.1    Jiang, X.2    Kozasa, T.3
  • 59
    • 0032569051 scopus 로고    scopus 로고
    • P115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13
    • T. Kozasa, X. Jiang, and M.J. Hart p115 RhoGEF, a GTPase activating protein for Galpha12 and Galpha13 Science 280 1998 2109 2111
    • (1998) Science , vol.280 , pp. 2109-2111
    • Kozasa, T.1    Jiang, X.2    Hart, M.J.3
  • 60
    • 0033605294 scopus 로고    scopus 로고
    • A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho
    • S. Fukuhara, C. Murga, M. Zohar, T. Igishi, and J.S. Gutkind A novel PDZ domain containing guanine nucleotide exchange factor links heterotrimeric G proteins to Rho J Biol Chem 274 1999 5868 5879
    • (1999) J Biol Chem , vol.274 , pp. 5868-5879
    • Fukuhara, S.1    Murga, C.2    Zohar, M.3    Igishi, T.4    Gutkind, J.S.5
  • 61
    • 0032582343 scopus 로고    scopus 로고
    • Constitutively active Galpha12, Galpha13, and Galphaq induce Rho-dependent neurite retraction through different signaling pathways
    • H. Katoh, J. Aoki, Y. Yamaguchi, Y. Kitano, A. Ichikawa, and M. Negishi Constitutively active Galpha12, Galpha13, and Galphaq induce Rho-dependent neurite retraction through different signaling pathways J Biol Chem 273 1998 28700 28707
    • (1998) J Biol Chem , vol.273 , pp. 28700-28707
    • Katoh, H.1    Aoki, J.2    Yamaguchi, Y.3    Kitano, Y.4    Ichikawa, A.5    Negishi, M.6
  • 63
    • 0036261720 scopus 로고    scopus 로고
    • Leukemia-associated Rho guanine nucleotide exchange factor promotes G alpha q-coupled activation of RhoA
    • M.A. Booden, D.P. Siderovski, and C.J. Der Leukemia-associated Rho guanine nucleotide exchange factor promotes G alpha q-coupled activation of RhoA Mol Cell Biol 22 2002 4053 4061
    • (2002) Mol Cell Biol , vol.22 , pp. 4053-4061
    • Booden, M.A.1    Siderovski, D.P.2    Der, C.J.3
  • 64
    • 84055182505 scopus 로고    scopus 로고
    • Activated protein C promotes protease-activated receptor-1 cytoprotective signaling through beta-arrestin and dishevelled-2 scaffolds
    • U.J. Soh, and J. Trejo Activated protein C promotes protease-activated receptor-1 cytoprotective signaling through beta-arrestin and dishevelled-2 scaffolds Proc Natl Acad Sci USA 108 2011 E1372 E1380
    • (2011) Proc Natl Acad Sci USA , vol.108
    • Soh, U.J.1    Trejo, J.2
  • 65
    • 20244379418 scopus 로고    scopus 로고
    • Regulation of PTEN by Rho small GTPases
    • Z. Li, X. Dong, and Z. Wang Regulation of PTEN by Rho small GTPases Nat Cell Biol 7 2005 399 404
    • (2005) Nat Cell Biol , vol.7 , pp. 399-404
    • Li, Z.1    Dong, X.2    Wang, Z.3
  • 66
    • 34447299716 scopus 로고    scopus 로고
    • The p110delta isoform of PI 3-kinase negatively controls RhoA and PTEN
    • E.A. Papakonstanti, A.J. Ridley, and B. Vanhaesebroeck The p110delta isoform of PI 3-kinase negatively controls RhoA and PTEN EMBO J 26 2007 3050 3061
    • (2007) EMBO J , vol.26 , pp. 3050-3061
    • Papakonstanti, E.A.1    Ridley, A.J.2    Vanhaesebroeck, B.3
  • 67
    • 79960038559 scopus 로고    scopus 로고
    • Distinct functional outputs of PTEN signalling are controlled by dynamic association with beta-arrestins
    • E. Lima-Fernandes, H. Enslen, and E. Camand Distinct functional outputs of PTEN signalling are controlled by dynamic association with beta-arrestins EMBO J 30 2011 2557 2568
    • (2011) EMBO J , vol.30 , pp. 2557-2568
    • Lima-Fernandes, E.1    Enslen, H.2    Camand, E.3
  • 68
    • 0024425981 scopus 로고
    • Rac, a novel ras-related family of proteins that are botulinum toxin substrates
    • J. Didsbury, R.F. Weber, G.M. Bokoch, T. Evans, and R. Snyderman rac, a novel ras-related family of proteins that are botulinum toxin substrates J Biol Chem 264 1989 16378 16382
    • (1989) J Biol Chem , vol.264 , pp. 16378-16382
    • Didsbury, J.1    Weber, R.F.2    Bokoch, G.M.3    Evans, T.4    Snyderman, R.5
  • 69
    • 0030824832 scopus 로고    scopus 로고
    • Characterization of RAC3, a novel member of the Rho family
    • L. Haataja, J. Groffen, and N. Heisterkamp Characterization of RAC3, a novel member of the Rho family J Biol Chem 272 1997 20384 20388
    • (1997) J Biol Chem , vol.272 , pp. 20384-20388
    • Haataja, L.1    Groffen, J.2    Heisterkamp, N.3
  • 70
    • 2342418629 scopus 로고    scopus 로고
    • Rho-family GTPases: It's not only Rac and Rho (and i like it)
    • K. Wennerberg, and C.J. Der Rho-family GTPases: it's not only Rac and Rho (and I like it) J Cell Sci 117 2004 1301 1312
    • (2004) J Cell Sci , vol.117 , pp. 1301-1312
    • Wennerberg, K.1    Der, C.J.2
  • 72
    • 33750529948 scopus 로고    scopus 로고
    • VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin
    • J. Gavard, and J.S. Gutkind VEGF controls endothelial-cell permeability by promoting the beta-arrestin-dependent endocytosis of VE-cadherin Nat Cell Biol 8 2006 1223 1234
    • (2006) Nat Cell Biol , vol.8 , pp. 1223-1234
    • Gavard, J.1    Gutkind, J.S.2
  • 73
    • 0022844766 scopus 로고
    • Purification of the major GTP-binding proteins from human placental membranes
    • T. Evans, M.L. Brown, E.D. Fraser, and J.K. Northup Purification of the major GTP-binding proteins from human placental membranes J Biol Chem 261 1986 7052 7059
    • (1986) J Biol Chem , vol.261 , pp. 7052-7059
    • Evans, T.1    Brown, M.L.2    Fraser, E.D.3    Northup, J.K.4
  • 74
    • 0025686144 scopus 로고
    • Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): Identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42
    • K. Shinjo, J.G. Koland, and M.J. Hart Molecular cloning of the gene for the human placental GTP-binding protein Gp (G25K): identification of this GTP-binding protein as the human homolog of the yeast cell-division-cycle protein CDC42 Proc Natl Acad Sci USA 87 1990 9853 9857
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 9853-9857
    • Shinjo, K.1    Koland, J.G.2    Hart, M.J.3
  • 75
    • 23944516797 scopus 로고    scopus 로고
    • 5-HT7 receptor is coupled to G alpha subunits of heterotrimeric G12-protein to regulate gene transcription and neuronal morphology
    • E. Kvachnina, G. Liu, and A. Dityatev 5-HT7 receptor is coupled to G alpha subunits of heterotrimeric G12-protein to regulate gene transcription and neuronal morphology J Neurosci 25 2005 7821 7830
    • (2005) J Neurosci , vol.25 , pp. 7821-7830
    • Kvachnina, E.1    Liu, G.2    Dityatev, A.3
  • 76
    • 0037063314 scopus 로고    scopus 로고
    • Endothelin suppresses cell migration via the JNK signaling pathway in a manner dependent upon Src kinase, Rac1, and Cdc42
    • J. Yamauchi, Y. Miyamoto, and H. Kokubu Endothelin suppresses cell migration via the JNK signaling pathway in a manner dependent upon Src kinase, Rac1, and Cdc42 FEBS Lett 527 2002 284 288
    • (2002) FEBS Lett , vol.527 , pp. 284-288
    • Yamauchi, J.1    Miyamoto, Y.2    Kokubu, H.3
  • 77
    • 12544256290 scopus 로고    scopus 로고
    • Angiotensin II and epidermal growth factor induce cyclooxygenase-2 expression in intestinal epithelial cells through small GTPases using distinct signaling pathways
    • L.W. Slice, T. Chiu, and E. Rozengurt Angiotensin II and epidermal growth factor induce cyclooxygenase-2 expression in intestinal epithelial cells through small GTPases using distinct signaling pathways J Biol Chem 280 2005 1582 1593
    • (2005) J Biol Chem , vol.280 , pp. 1582-1593
    • Slice, L.W.1    Chiu, T.2    Rozengurt, E.3
  • 78
    • 0028986034 scopus 로고
    • The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3 T3 fibroblasts
    • R. Kozma, S. Ahmed, A. Best, and L. Lim The Ras-related protein Cdc42Hs and bradykinin promote formation of peripheral actin microspikes and filopodia in Swiss 3 T3 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
  • 79
    • 0033785506 scopus 로고    scopus 로고
    • Cyclic AMP and protein kinase A stimulate Cdc42: Role of A(2) adenosine receptors in human mast cells
    • I. Feoktistov, A.E. Goldstein, and I. Biaggioni Cyclic AMP and protein kinase A stimulate Cdc42: role of A(2) adenosine receptors in human mast cells Mol Pharmacol 58 2000 903 910
    • (2000) Mol Pharmacol , vol.58 , pp. 903-910
    • Feoktistov, I.1    Goldstein, A.E.2    Biaggioni, I.3
  • 80
    • 0023478620 scopus 로고
    • Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: Molecular cloning of YPT-related cDNAs from a rat brain library
    • N. Touchot, P. Chardin, and A. Tavitian Four additional members of the ras gene superfamily isolated by an oligonucleotide strategy: molecular cloning of YPT-related cDNAs from a rat brain library Proc Natl Acad Sci USA 84 1987 8210 8214
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 8210-8214
    • Touchot, N.1    Chardin, P.2    Tavitian, A.3
  • 81
    • 0021015541 scopus 로고
    • A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product
    • D. Gallwitz, C. Donath, and C. Sander A yeast gene encoding a protein homologous to the human c-has/bas proto-oncogene product Nature 306 1983 704 707
    • (1983) Nature , vol.306 , pp. 704-707
    • Gallwitz, D.1    Donath, C.2    Sander, C.3
  • 82
    • 0242321269 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor endocytosis and trafficking by Rab GTPases
    • J.L. Seachrist, and S.S. Ferguson Regulation of G protein-coupled receptor endocytosis and trafficking by Rab GTPases Life Sci 74 2003 225 235
    • (2003) Life Sci , vol.74 , pp. 225-235
    • Seachrist, J.L.1    Ferguson, S.S.2
  • 83
    • 0028981467 scopus 로고
    • Ligand-stimulated beta 2-adrenergic receptor internalization via the constitutive endocytic pathway into rab5-containing endosomes
    • R.H. Moore, N. Sadovnikoff, and S. Hoffenberg Ligand-stimulated beta 2-adrenergic receptor internalization via the constitutive endocytic pathway into rab5-containing endosomes J Cell Sci 108 Pt. 9 1995 2983 2991
    • (1995) J Cell Sci , vol.108 , Issue.PART 9 , pp. 2983-2991
    • Moore, R.H.1    Sadovnikoff, N.2    Hoffenberg, S.3
  • 85
    • 78651295086 scopus 로고    scopus 로고
    • Rab GTPases bind at a common site within the angiotensin II type i receptor carboxyl-terminal tail: Evidence that Rab4 regulates receptor phosphorylation, desensitization, and resensitization
    • J.L. Esseltine, L.B. Dale, and S.S. Ferguson Rab GTPases bind at a common site within the angiotensin II type I receptor carboxyl-terminal tail: evidence that Rab4 regulates receptor phosphorylation, desensitization, and resensitization Mol Pharmacol 79 2011 175 184
    • (2011) Mol Pharmacol , vol.79 , pp. 175-184
    • Esseltine, J.L.1    Dale, L.B.2    Ferguson, S.S.3
  • 86
    • 27744469168 scopus 로고    scopus 로고
    • The intracellular trafficking of the G protein-coupled receptor TPbeta depends on a direct interaction with Rab11
    • E. Hamelin, C. Theriault, G. Laroche, and J.L. Parent The intracellular trafficking of the G protein-coupled receptor TPbeta depends on a direct interaction with Rab11 J Biol Chem 280 2005 36195 36205
    • (2005) J Biol Chem , vol.280 , pp. 36195-36205
    • Hamelin, E.1    Theriault, C.2    Laroche, G.3    Parent, J.L.4
  • 87
    • 59849102081 scopus 로고    scopus 로고
    • Rab11 regulates the recycling of the beta2-adrenergic receptor through a direct interaction
    • A. Parent, E. Hamelin, P. Germain, and J.L. Parent Rab11 regulates the recycling of the beta2-adrenergic receptor through a direct interaction Biochem J 418 2009 163 172
    • (2009) Biochem J , vol.418 , pp. 163-172
    • Parent, A.1    Hamelin, E.2    Germain, P.3    Parent, J.L.4
  • 88
    • 77953317400 scopus 로고    scopus 로고
    • Interaction of the human prostacyclin receptor with Rab11: Characterization of a novel Rab11 binding domain within alpha-helix 8 that is regulated by palmitoylation
    • H.M. Reid, E.P. Mulvaney, E.C. Turner, and B.T. Kinsella Interaction of the human prostacyclin receptor with Rab11: characterization of a novel Rab11 binding domain within alpha-helix 8 that is regulated by palmitoylation J Biol Chem 285 2010 18709 18726
    • (2010) J Biol Chem , vol.285 , pp. 18709-18726
    • Reid, H.M.1    Mulvaney, E.P.2    Turner, E.C.3    Kinsella, B.T.4
  • 89
    • 0033527663 scopus 로고    scopus 로고
    • Association of beta-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization
    • R.H. Oakley, S.A. Laporte, J.A. Holt, L.S. Barak, and M.G. Caron Association of beta-arrestin with G protein-coupled receptors during clathrin-mediated endocytosis dictates the profile of receptor resensitization J Biol Chem 274 1999 32248 32257
    • (1999) J Biol Chem , vol.274 , pp. 32248-32257
    • Oakley, R.H.1    Laporte, S.A.2    Holt, J.A.3    Barak, L.S.4    Caron, M.G.5
  • 90
    • 1842477154 scopus 로고    scopus 로고
    • Regulation of angiotensin II type 1A receptor intracellular retention, degradation, and recycling by Rab5, Rab7, and Rab11 GTPases
    • L.B. Dale, J.L. Seachrist, A.V. Babwah, and S.S. Ferguson Regulation of angiotensin II type 1A receptor intracellular retention, degradation, and recycling by Rab5, Rab7, and Rab11 GTPases J Biol Chem 279 2004 13110 13118
    • (2004) J Biol Chem , vol.279 , pp. 13110-13118
    • Dale, L.B.1    Seachrist, J.L.2    Babwah, A.V.3    Ferguson, S.S.4
  • 91
    • 0022978533 scopus 로고
    • The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein
    • R.A. Kahn, and A.G. Gilman The protein cofactor necessary for ADP-ribosylation of Gs by cholera toxin is itself a GTP binding protein J Biol Chem 261 1986 7906 7911
    • (1986) J Biol Chem , vol.261 , pp. 7906-7911
    • Kahn, R.A.1    Gilman, A.G.2
  • 92
    • 23644438026 scopus 로고    scopus 로고
    • Structural basis for the activation of cholera toxin by human ARF6-GTP
    • C.J. O'Neal, M.G. Jobling, R.K. Holmes, and W.G. Hol Structural basis for the activation of cholera toxin by human ARF6-GTP Science 309 2005 1093 1096
    • (2005) Science , vol.309 , pp. 1093-1096
    • O'Neal, C.J.1    Jobling, M.G.2    Holmes, R.K.3    Hol, W.G.4
  • 93
    • 33646184680 scopus 로고    scopus 로고
    • ARF proteins: Roles in membrane traffic and beyond
    • C. D'Souza-Schorey, and P. Chavrier ARF proteins: roles in membrane traffic and beyond Nat Rev Mol Cell Biol 7 2006 347 358
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 347-358
    • D'Souza-Schorey, C.1    Chavrier, P.2
  • 94
    • 0031037998 scopus 로고    scopus 로고
    • Regulated exocytosis in chromaffin cells. A potential role for a secretory granule-associated ARF6 protein
    • M.C. Galas, J.B. Helms, N. Vitale, D. Thierse, D. Aunis, and M.F. Bader Regulated exocytosis in chromaffin cells. A potential role for a secretory granule-associated ARF6 protein J Biol Chem 272 1997 2788 2793
    • (1997) J Biol Chem , vol.272 , pp. 2788-2793
    • Galas, M.C.1    Helms, J.B.2    Vitale, N.3    Thierse, D.4    Aunis, D.5    Bader, M.F.6
  • 95
    • 34250313651 scopus 로고    scopus 로고
    • Active Arf6 recruits ARNO/cytohesin GEFs to the PM by binding their PH domains
    • L.A. Cohen, A. Honda, P. Varnai, F.D. Brown, T. Balla, and J.G. Donaldson Active Arf6 recruits ARNO/cytohesin GEFs to the PM by binding their PH domains Mol Biol Cell 18 2007 2244 2253
    • (2007) Mol Biol Cell , vol.18 , pp. 2244-2253
    • Cohen, L.A.1    Honda, A.2    Varnai, P.3    Brown, F.D.4    Balla, T.5    Donaldson, J.G.6
  • 96
    • 0141668939 scopus 로고    scopus 로고
    • ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor
    • R. Mitchell, D.N. Robertson, P.J. Holland, D. Collins, E.M. Lutz, and M.S. Johnson ADP-ribosylation factor-dependent phospholipase D activation by the M3 muscarinic receptor J Biol Chem 278 2003 33818 33830
    • (2003) J Biol Chem , vol.278 , pp. 33818-33830
    • Mitchell, R.1    Robertson, D.N.2    Holland, P.J.3    Collins, D.4    Lutz, E.M.5    Johnson, M.S.6
  • 97
    • 61349176557 scopus 로고    scopus 로고
    • ADP-ribosylation factor 1 controls the activation of the phosphatidylinositol 3-kinase pathway to regulate epidermal growth factor-dependent growth and migration of breast cancer cells
    • P.L. Boulay, M. Cotton, P. Melancon, and A. Claing ADP-ribosylation factor 1 controls the activation of the phosphatidylinositol 3-kinase pathway to regulate epidermal growth factor-dependent growth and migration of breast cancer cells J Biol Chem 283 2008 36425 36434
    • (2008) J Biol Chem , vol.283 , pp. 36425-36434
    • Boulay, P.L.1    Cotton, M.2    Melancon, P.3    Claing, A.4
  • 98
    • 0032564277 scopus 로고    scopus 로고
    • Beta2-adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein
    • R.T. Premont, A. Claing, and N. Vitale Beta2-adrenergic receptor regulation by GIT1, a G protein-coupled receptor kinase-associated ADP ribosylation factor GTPase-activating protein Proc Natl Acad Sci USA 95 1998 14082 14087
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 14082-14087
    • Premont, R.T.1    Claing, A.2    Vitale, N.3
  • 99
    • 14044252159 scopus 로고    scopus 로고
    • G protein-coupled receptor endocytosis in ARF6-depleted cells
    • T. Houndolo, P.L. Boulay, and A. Claing G protein-coupled receptor endocytosis in ARF6-depleted cells J Biol Chem 280 2005 5598 5604
    • (2005) J Biol Chem , vol.280 , pp. 5598-5604
    • Houndolo, T.1    Boulay, P.L.2    Claing, A.3
  • 100
    • 34548420952 scopus 로고    scopus 로고
    • ARF6 regulates angiotensin II type 1 receptor endocytosis by controlling the recruitment of AP-2 and clathrin
    • M.E. Poupart, D. Fessart, M. Cotton, S.A. Laporte, and A. Claing ARF6 regulates angiotensin II type 1 receptor endocytosis by controlling the recruitment of AP-2 and clathrin Cell Signal 19 2007 2370 2378
    • (2007) Cell Signal , vol.19 , pp. 2370-2378
    • Poupart, M.E.1    Fessart, D.2    Cotton, M.3    Laporte, S.A.4    Claing, A.5
  • 101
    • 20444370234 scopus 로고    scopus 로고
    • The small G-protein Arf6GTP recruits the AP-2 adaptor complex to membranes
    • O. Paleotti, E. Macia, and F. Luton The small G-protein Arf6GTP recruits the AP-2 adaptor complex to membranes J Biol Chem 280 2005 21661 21666
    • (2005) J Biol Chem , vol.280 , pp. 21661-21666
    • Paleotti, O.1    Macia, E.2    Luton, F.3
  • 102
    • 84858612683 scopus 로고    scopus 로고
    • Identification of a nuclear localization sequence in beta-arrestin-1 and its functional implications
    • C.Z. Hoeppner, N. Cheng, and R.D. Ye Identification of a nuclear localization sequence in beta-arrestin-1 and its functional implications J Biol Chem 287 2012 8932 8943
    • (2012) J Biol Chem , vol.287 , pp. 8932-8943
    • Hoeppner, C.Z.1    Cheng, N.2    Ye, R.D.3
  • 103
    • 34547512353 scopus 로고    scopus 로고
    • Functional specialization of beta-arrestin interactions revealed by proteomic analysis
    • K. Xiao, D.B. McClatchy, and A.K. Shukla Functional specialization of beta-arrestin interactions revealed by proteomic analysis Proc Natl Acad Sci USA 104 2007 12011 12016
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 12011-12016
    • Xiao, K.1    McClatchy, D.B.2    Shukla, A.K.3


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