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Volumn 115, Issue , 2013, Pages 421-453

Fine-tuning of GPCR signals by intracellular G protein modulators

Author keywords

G protein activation; GPCR signaling; GPSM protein; Keywords; Nonreceptor GEF; Protein protein interaction; RGS protein

Indexed keywords


EID: 84873929438     PISSN: 18771173     EISSN: None     Source Type: Book Series    
DOI: 10.1016/B978-0-12-394587-7.00010-5     Document Type: Chapter
Times cited : (11)

References (157)
  • 1
    • 0026026818 scopus 로고
    • The GTPase superfamily: Conserved structure and molecular mechanism
    • H.R. Bourne, D.A. Sanders, and F. McCormick The GTPase superfamily: conserved structure and molecular mechanism Nature 349 1991 117 127
    • (1991) Nature , vol.349 , pp. 117-127
    • Bourne, H.R.1    Sanders, D.A.2    McCormick, F.3
  • 2
    • 79959393264 scopus 로고    scopus 로고
    • Structure-function relationships of the G domain, a canonical switch motif
    • A. Wittinghofer, and I.R. Vetter Structure-function relationships of the G domain, a canonical switch motif Annu Rev Biochem 80 2011 943 971
    • (2011) Annu Rev Biochem , vol.80 , pp. 943-971
    • Wittinghofer, A.1    Vetter, I.R.2
  • 3
    • 0023164972 scopus 로고
    • Effects of Mg2 + and the beta gamma-subunit complex on the interactions of guanine nucleotides with G proteins
    • T. Higashijima, K.M. Ferguson, P.C. Sternweis, M.D. Smigel, and A.G. Gilman Effects of Mg2 + and the beta gamma-subunit complex on the interactions of guanine nucleotides with G proteins J Biol Chem 262 1987 762 766
    • (1987) J Biol Chem , vol.262 , pp. 762-766
    • Higashijima, T.1    Ferguson, K.M.2    Sternweis, P.C.3    Smigel, M.D.4    Gilman, A.G.5
  • 5
    • 0033538337 scopus 로고    scopus 로고
    • Phospholipase C-beta1 directly accelerates GTP hydrolysis by Galphaq and acceleration is inhibited by Gbeta gamma subunits
    • P. Chidiac, and E.M. Ross Phospholipase C-beta1 directly accelerates GTP hydrolysis by Galphaq and acceleration is inhibited by Gbeta gamma subunits J Biol Chem 274 1999 19639 19643
    • (1999) J Biol Chem , vol.274 , pp. 19639-19643
    • Chidiac, P.1    Ross, E.M.2
  • 6
    • 60149112585 scopus 로고    scopus 로고
    • Regulation and physiological functions of G12/13-mediated signaling pathways
    • N. Suzuki, N. Hajicek, and T. Kozasa Regulation and physiological functions of G12/13-mediated signaling pathways Neurosignals 17 2009 55 70
    • (2009) Neurosignals , vol.17 , pp. 55-70
    • Suzuki, N.1    Hajicek, N.2    Kozasa, T.3
  • 7
    • 30944451158 scopus 로고    scopus 로고
    • RGS proteins have a signaling complex: Interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins
    • M. Abramow-Newerly, A.A. Roy, C. Nunn, and P. Chidiac RGS proteins have a signaling complex: interactions between RGS proteins and GPCRs, effectors, and auxiliary proteins Cell Signal 18 2006 579 591
    • (2006) Cell Signal , vol.18 , pp. 579-591
    • Abramow-Newerly, M.1    Roy, A.A.2    Nunn, C.3    Chidiac, P.4
  • 8
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-Activating proteins for heterotrimeric G proteins: Regulators of G protein signaling (RGS) and RGS-like proteins
    • E.M. Ross, and T.M. Wilkie GTPase-Activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins Annu Rev Biochem 69 2000 795 827
    • (2000) Annu Rev Biochem , vol.69 , pp. 795-827
    • Ross, E.M.1    Wilkie, T.M.2
  • 9
    • 0033607326 scopus 로고    scopus 로고
    • Selective regulation of Galpha(q/11) by an RGS domain in the G protein-coupled receptor kinase, GRK2
    • C.V. Carman, J.L. Parent, P.W. Day, A.N. Pronin, P.M. Sternweis, and P.B. Wedegaertner Selective regulation of Galpha(q/11) by an RGS domain in the G protein-coupled receptor kinase, GRK2 J Biol Chem 274 1999 34483 34492
    • (1999) J Biol Chem , vol.274 , pp. 34483-34492
    • Carman, C.V.1    Parent, J.L.2    Day, P.W.3    Pronin, A.N.4    Sternweis, P.M.5    Wedegaertner, P.B.6
  • 10
    • 84855349531 scopus 로고    scopus 로고
    • Group II activators of G-protein signaling and proteins containing a G-protein regulatory motif
    • J.B. Blumer, S.S. Oner, and S.M. Lanier Group II activators of G-protein signaling and proteins containing a G-protein regulatory motif Acta Physiol (Oxf) 204 2012 202 218
    • (2012) Acta Physiol (Oxf) , vol.204 , pp. 202-218
    • Blumer, J.B.1    Oner, S.S.2    Lanier, S.M.3
  • 11
    • 81955168031 scopus 로고    scopus 로고
    • How signaling between cells can orient a mitotic spindle
    • A.D. Werts, and B. Goldstein How signaling between cells can orient a mitotic spindle Semin Cell Dev Biol 22 2011 842 849
    • (2011) Semin Cell Dev Biol , vol.22 , pp. 842-849
    • Werts, A.D.1    Goldstein, B.2
  • 12
    • 79960207659 scopus 로고    scopus 로고
    • Mitotic spindle orientation in asymmetric and symmetric cell divisions during animal development
    • X. Morin, and Y. Bellaiche Mitotic spindle orientation in asymmetric and symmetric cell divisions during animal development Dev Cell 21 2011 102 119
    • (2011) Dev Cell , vol.21 , pp. 102-119
    • Morin, X.1    Bellaiche, Y.2
  • 13
    • 80755132220 scopus 로고    scopus 로고
    • Non-canonical signaling and localizations of heterotrimeric G proteins
    • T. Hewavitharana, and P.B. Wedegaertner Non-canonical signaling and localizations of heterotrimeric G proteins Cell Signal 24 2012 25 34
    • (2012) Cell Signal , vol.24 , pp. 25-34
    • Hewavitharana, T.1    Wedegaertner, P.B.2
  • 14
    • 0032030621 scopus 로고    scopus 로고
    • Rethinking receptor-G protein-effector interactions
    • P. Chidiac Rethinking receptor-G protein-effector interactions Biochem Pharmacol 55 1998 549 556
    • (1998) Biochem Pharmacol , vol.55 , pp. 549-556
    • Chidiac, P.1
  • 15
    • 0027503004 scopus 로고
    • Compartmentation of receptors and guanine nucleotide-binding proteins in NG108-15 cells: Lack of cross-talk in agonist binding among the alpha 2-Adrenergic, muscarinic, and opiate receptors
    • D. Graeser, and R.R. Neubig Compartmentation of receptors and guanine nucleotide-binding proteins in NG108-15 cells: lack of cross-talk in agonist binding among the alpha 2-Adrenergic, muscarinic, and opiate receptors Mol Pharmacol 43 1993 434 443
    • (1993) Mol Pharmacol , vol.43 , pp. 434-443
    • Graeser, D.1    Neubig, R.R.2
  • 16
    • 0026752495 scopus 로고
    • Different beta-subunits determine G-protein interaction with transmembrane receptors
    • C. Kleuss, H. Scherubl, J. Hescheler, G. Schultz, and B. Wittig Different beta-subunits determine G-protein interaction with transmembrane receptors Nature 358 1992 424 426
    • (1992) Nature , vol.358 , pp. 424-426
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 17
    • 0027530916 scopus 로고
    • Selectivity in signal transduction determined by gamma subunits of heterotrimeric G proteins
    • C. Kleuss, H. Scherubl, J. Hescheler, G. Schultz, and B. Wittig Selectivity in signal transduction determined by gamma subunits of heterotrimeric G proteins Science 259 1993 832 834
    • (1993) Science , vol.259 , pp. 832-834
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 18
    • 0025880464 scopus 로고
    • Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents
    • C. Kleuss, J. Hescheler, C. Ewel, W. Rosenthal, G. Schultz, and B. Wittig Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents Nature 353 1991 43 48
    • (1991) Nature , vol.353 , pp. 43-48
    • Kleuss, C.1    Hescheler, J.2    Ewel, C.3    Rosenthal, W.4    Schultz, G.5    Wittig, B.6
  • 19
    • 0030761020 scopus 로고    scopus 로고
    • The complex regulation of receptor-coupled G-proteins
    • M. Rodbell The complex regulation of receptor-coupled G-proteins Adv Enzyme Regul 37 1997 427 435
    • (1997) Adv Enzyme Regul , vol.37 , pp. 427-435
    • Rodbell, M.1
  • 20
    • 42549102347 scopus 로고    scopus 로고
    • G protein-coupled receptors in and on the cell nucleus: A new signaling paradigm?
    • B. Boivin, G. Vaniotis, B.G. Allen, and T.E. Hebert G protein-coupled receptors in and on the cell nucleus: a new signaling paradigm? J Recept Signal Transduct Res 28 2008 15 28
    • (2008) J Recept Signal Transduct Res , vol.28 , pp. 15-28
    • Boivin, B.1    Vaniotis, G.2    Allen, B.G.3    Hebert, T.E.4
  • 22
    • 84866859313 scopus 로고    scopus 로고
    • Dissociation of heterotrimeric g proteins in cells
    • N.A. Lambert Dissociation of heterotrimeric g proteins in cells Sci Signal 1 2008 re5
    • (2008) Sci Signal , vol.1 , pp. 5
    • Lambert, N.A.1
  • 23
    • 70849112486 scopus 로고    scopus 로고
    • Cell signaling in space and time: Where proteins come together and when they're apart
    • J.D. Scott, and T. Pawson Cell signaling in space and time: where proteins come together and when they're apart Science 326 2009 1220 1224
    • (2009) Science , vol.326 , pp. 1220-1224
    • Scott, J.D.1    Pawson, T.2
  • 24
    • 77950642292 scopus 로고    scopus 로고
    • Networking with AKAPs: Context-dependent regulation of anchored enzymes
    • E.J. Welch, B.W. Jones, and J.D. Scott Networking with AKAPs: context-dependent regulation of anchored enzymes Mol Interv 10 2010 86 97
    • (2010) Mol Interv , vol.10 , pp. 86-97
    • Welch, E.J.1    Jones, B.W.2    Scott, J.D.3
  • 25
    • 84857471063 scopus 로고    scopus 로고
    • Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins
    • A.C. Magalhaes, H. Dunn, and S.S. Ferguson Regulation of GPCR activity, trafficking and localization by GPCR-interacting proteins Br J Pharmacol 165 2012 1717 1736
    • (2012) Br J Pharmacol , vol.165 , pp. 1717-1736
    • Magalhaes, A.C.1    Dunn, H.2    Ferguson, S.S.3
  • 27
    • 80053023873 scopus 로고    scopus 로고
    • Further assessment of the clinically effective dose range of etoricoxib: A randomized, double-blinded, placebo-controlled trial in rheumatoid arthritis
    • M. Greenwald, P.M. Peloso, D. Mandel, O. Soto, A. Mehta, and N. Frontera Further assessment of the clinically effective dose range of etoricoxib: a randomized, double-blinded, placebo-controlled trial in rheumatoid arthritis Curr Med Res Opin 27 2011 2033 2042
    • (2011) Curr Med Res Opin , vol.27 , pp. 2033-2042
    • Greenwald, M.1    Peloso, P.M.2    Mandel, D.3    Soto, O.4    Mehta, A.5    Frontera, N.6
  • 29
    • 12944265070 scopus 로고    scopus 로고
    • A homotropic two-state model and auto-Antagonism
    • N. Bindslev A homotropic two-state model and auto-Antagonism BMC Pharmacol 4 2004 11
    • (2004) BMC Pharmacol , vol.4 , pp. 11
    • Bindslev, N.1
  • 30
    • 78650147139 scopus 로고    scopus 로고
    • Allostery at G protein-coupled receptor homo- and heteromers: Uncharted pharmacological landscapes
    • N.J. Smith, and G. Milligan Allostery at G protein-coupled receptor homo- and heteromers: uncharted pharmacological landscapes Pharmacol Rev 62 2010 701 725
    • (2010) Pharmacol Rev , vol.62 , pp. 701-725
    • Smith, N.J.1    Milligan, G.2
  • 31
    • 10844255797 scopus 로고    scopus 로고
    • Oligomerization of G protein-coupled receptors: Past, present, and future
    • P.S. Park, S. Filipek, J.W. Wells, and K. Palczewski Oligomerization of G protein-coupled receptors: past, present, and future Biochemistry 43 2004 15643 15656
    • (2004) Biochemistry , vol.43 , pp. 15643-15656
    • Park, P.S.1    Filipek, S.2    Wells, J.W.3    Palczewski, K.4
  • 33
    • 0029922265 scopus 로고    scopus 로고
    • Identification of the cysteine residues involved in the class i disulfide bonds of the human insulin receptor: Properties of insulin receptor monomers
    • K. Lu, and G. Guidotti Identification of the cysteine residues involved in the class I disulfide bonds of the human insulin receptor: properties of insulin receptor monomers Mol Biol Cell 7 1996 679 691
    • (1996) Mol Biol Cell , vol.7 , pp. 679-691
    • Lu, K.1    Guidotti, G.2
  • 34
    • 77954870422 scopus 로고    scopus 로고
    • Transactivation of PDGFRbeta by dopamine D4 receptor does not require PDGFRbeta dimerization
    • S.S. Chi, S.M. Vetiska, R.S. Gill, M.S. Hsiung, F. Liu, and H.H. Van Tol Transactivation of PDGFRbeta by dopamine D4 receptor does not require PDGFRbeta dimerization Mol Brain 3 2010 22
    • (2010) Mol Brain , vol.3 , pp. 22
    • Chi, S.S.1    Vetiska, S.M.2    Gill, R.S.3    Hsiung, M.S.4    Liu, F.5    Van Tol, H.H.6
  • 35
    • 34250666273 scopus 로고    scopus 로고
    • A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein
    • M.R. Whorton, M.P. Bokoch, S.G. Rasmussen, B. Huang, R.N. Zare, and B. Kobilka A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein Proc Natl Acad Sci USA 104 2007 7682 7687
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 7682-7687
    • Whorton, M.R.1    Bokoch, M.P.2    Rasmussen, S.G.3    Huang, B.4    Zare, R.N.5    Kobilka, B.6
  • 36
    • 0037040173 scopus 로고    scopus 로고
    • Mutations in the carboxyl-terminal domain of phospholipase C-beta 1 delineate the dimer interface and a potential Galphaq interaction site
    • O. Ilkaeva, L.N. Kinch, R.H. Paulssen, and E.M. Ross Mutations in the carboxyl-terminal domain of phospholipase C-beta 1 delineate the dimer interface and a potential Galphaq interaction site J Biol Chem 277 2002 4294 4300
    • (2002) J Biol Chem , vol.277 , pp. 4294-4300
    • Ilkaeva, O.1    Kinch, L.N.2    Paulssen, R.H.3    Ross, E.M.4
  • 37
    • 33746046362 scopus 로고    scopus 로고
    • Higher-order organization and regulation of adenylyl cyclases
    • D.M. Cooper, and A.J. Crossthwaite Higher-order organization and regulation of adenylyl cyclases Trends Pharmacol Sci 27 2006 426 431
    • (2006) Trends Pharmacol Sci , vol.27 , pp. 426-431
    • Cooper, D.M.1    Crossthwaite, A.J.2
  • 38
    • 0026469361 scopus 로고
    • Effects of adenyl nucleotides and carbachol on cooperative interactions among G proteins
    • P. Chidiac, and J.W. Wells Effects of adenyl nucleotides and carbachol on cooperative interactions among G proteins Biochemistry 31 1992 10908 10921
    • (1992) Biochemistry , vol.31 , pp. 10908-10921
    • Chidiac, P.1    Wells, J.W.2
  • 40
    • 0031017573 scopus 로고    scopus 로고
    • RGS4 and GAIP are GTPase-Activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha
    • J.R. Hepler, D.M. Berman, A.G. Gilman, and T. Kozasa RGS4 and GAIP are GTPase-Activating proteins for Gq alpha and block activation of phospholipase C beta by gamma-thio-GTP-Gq alpha Proc Natl Acad Sci USA 94 1997 428 432
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 428-432
    • Hepler, J.R.1    Berman, D.M.2    Gilman, A.G.3    Kozasa, T.4
  • 41
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase-Activating proteins for the Gi subfamily of G protein alpha subunits
    • D.M. Berman, T.M. Wilkie, and A.G. Gilman GAIP and RGS4 are GTPase-Activating proteins for the Gi subfamily of G protein alpha subunits Cell 86 1996 445 452
    • (1996) Cell , vol.86 , pp. 445-452
    • Berman, D.M.1    Wilkie, T.M.2    Gilman, A.G.3
  • 42
    • 0035340989 scopus 로고    scopus 로고
    • Inhibition of GDP/GTP exchange on G alpha subunits by proteins containing G-protein regulatory motifs
    • M. Natochin, K.G. Gasimov, and N.O. Artemyev Inhibition of GDP/GTP exchange on G alpha subunits by proteins containing G-protein regulatory motifs Biochemistry 40 2001 5322 5328
    • (2001) Biochemistry , vol.40 , pp. 5322-5328
    • Natochin, M.1    Gasimov, K.G.2    Artemyev, N.O.3
  • 43
    • 77954220827 scopus 로고    scopus 로고
    • Receptor-regulated interaction of activator of G-protein signaling-4 and Galphai
    • S.S. Oner, E.M. Maher, B. Breton, M. Bouvier, and J.B. Blumer Receptor-regulated interaction of activator of G-protein signaling-4 and Galphai J Biol Chem 285 2010 20588 20594
    • (2010) J Biol Chem , vol.285 , pp. 20588-20594
    • Oner, S.S.1    Maher, E.M.2    Breton, B.3    Bouvier, M.4    Blumer, J.B.5
  • 44
    • 33845945903 scopus 로고    scopus 로고
    • Up-regulation of endogenous RGS2 mediates cross-desensitization between Gs and Gq signaling in osteoblasts
    • A.A. Roy, C. Nunn, H. Ming, M.X. Zou, J. Penninger, and L.A. Kirshenbaum Up-regulation of endogenous RGS2 mediates cross-desensitization between Gs and Gq signaling in osteoblasts J Biol Chem 281 2006 32684 32693
    • (2006) J Biol Chem , vol.281 , pp. 32684-32693
    • Roy, A.A.1    Nunn, C.2    Ming, H.3    Zou, M.X.4    Penninger, J.5    Kirshenbaum, L.A.6
  • 45
    • 0031006273 scopus 로고    scopus 로고
    • A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C
    • T.K. Chatterjee, A.K. Eapen, and R.A. Fisher A truncated form of RGS3 negatively regulates G protein-coupled receptor stimulation of adenylyl cyclase and phosphoinositide phospholipase C J Biol Chem 272 1997 15481 15487
    • (1997) J Biol Chem , vol.272 , pp. 15481-15487
    • Chatterjee, T.K.1    Eapen, A.K.2    Fisher, R.A.3
  • 46
    • 0037053368 scopus 로고    scopus 로고
    • Functional characterization of the G protein regulator RGS13
    • E.N. Johnson, and K.M. Druey Functional characterization of the G protein regulator RGS13 J Biol Chem 277 2002 16768 16774
    • (2002) J Biol Chem , vol.277 , pp. 16768-16774
    • Johnson, E.N.1    Druey, K.M.2
  • 47
    • 0033798792 scopus 로고    scopus 로고
    • RGS3 is a GTPase-Activating protein for g(ialpha) and g(qalpha) and a potent inhibitor of signaling by GTPase-deficient forms of g(qalpha) and g(11alpha)
    • A. Scheschonka, C.W. Dessauer, S. Sinnarajah, P. Chidiac, C.S. Shi, and J.H. Kehrl RGS3 is a GTPase-Activating protein for g(ialpha) and g(qalpha) and a potent inhibitor of signaling by GTPase-deficient forms of g(qalpha) and g(11alpha) Mol Pharmacol 58 2000 719 728
    • (2000) Mol Pharmacol , vol.58 , pp. 719-728
    • Scheschonka, A.1    Dessauer, C.W.2    Sinnarajah, S.3    Chidiac, P.4    Shi, C.S.5    Kehrl, J.H.6
  • 48
    • 0041854353 scopus 로고    scopus 로고
    • Recruitment of RGS2 and RGS4 to the plasma membrane by G proteins and receptors reflects functional interactions
    • A.A. Roy, K.E. Lemberg, and P. Chidiac Recruitment of RGS2 and RGS4 to the plasma membrane by G proteins and receptors reflects functional interactions Mol Pharmacol 64 2003 587 593
    • (2003) Mol Pharmacol , vol.64 , pp. 587-593
    • Roy, A.A.1    Lemberg, K.E.2    Chidiac, P.3
  • 49
    • 0035957996 scopus 로고    scopus 로고
    • Mechanisms governing subcellular localization and function of human RGS2
    • S.P. Heximer, H. Lim, J.L. Bernard, and K.J. Blumer Mechanisms governing subcellular localization and function of human RGS2 J Biol Chem 276 2001 14195 14203
    • (2001) J Biol Chem , vol.276 , pp. 14195-14203
    • Heximer, S.P.1    Lim, H.2    Bernard, J.L.3    Blumer, K.J.4
  • 50
    • 36348958940 scopus 로고    scopus 로고
    • Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members
    • S. Gu, J. He, W.T. Ho, S. Ramineni, D.M. Thal, and R. Natesh Unique hydrophobic extension of the RGS2 amphipathic helix domain imparts increased plasma membrane binding and function relative to other RGS R4/B subfamily members J Biol Chem 282 2007 33064 33075
    • (2007) J Biol Chem , vol.282 , pp. 33064-33075
    • Gu, S.1    He, J.2    Ho, W.T.3    Ramineni, S.4    Thal, D.M.5    Natesh, R.6
  • 51
    • 0031058739 scopus 로고    scopus 로고
    • A GTPase-Activating protein for the G protein Galphaz. Identification, purification, and mechanism of action
    • J. Wang, Y. Tu, J. Woodson, X. Song, and E.M. Ross A GTPase-Activating protein for the G protein Galphaz. Identification, purification, and mechanism of action J Biol Chem 272 1997 5732 5740
    • (1997) J Biol Chem , vol.272 , pp. 5732-5740
    • Wang, J.1    Tu, Y.2    Woodson, J.3    Song, X.4    Ross, E.M.5
  • 52
    • 33646200560 scopus 로고    scopus 로고
    • Gbetagamma inhibits Galpha GTPase-Activating proteins by inhibition of Galpha-GTP binding during stimulation by receptor
    • W. Tang, Y. Tu, S.K. Nayak, J. Woodson, M. Jehl, and E.M. Ross Gbetagamma inhibits Galpha GTPase-Activating proteins by inhibition of Galpha-GTP binding during stimulation by receptor J Biol Chem 281 2006 4746 4753
    • (2006) J Biol Chem , vol.281 , pp. 4746-4753
    • Tang, W.1    Tu, Y.2    Nayak, S.K.3    Woodson, J.4    Jehl, M.5    Ross, E.M.6
  • 53
    • 0033578385 scopus 로고    scopus 로고
    • Rapid GTP binding and hydrolysis by G(q) promoted by receptor and GTPase-Activating proteins
    • S. Mukhopadhyay, and E.M. Ross Rapid GTP binding and hydrolysis by G(q) promoted by receptor and GTPase-Activating proteins Proc Natl Acad Sci USA 96 1999 9539 9544
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 9539-9544
    • Mukhopadhyay, S.1    Ross, E.M.2
  • 54
    • 0036765564 scopus 로고    scopus 로고
    • Characterization and comparison of RGS2 and RGS4 as GTPase-Activating proteins for m2 muscarinic receptor-stimulated G(i)
    • W. Cladman, and P. Chidiac Characterization and comparison of RGS2 and RGS4 as GTPase-Activating proteins for m2 muscarinic receptor-stimulated G(i) Mol Pharmacol 62 2002 654 659
    • (2002) Mol Pharmacol , vol.62 , pp. 654-659
    • Cladman, W.1    Chidiac, P.2
  • 56
    • 0029961069 scopus 로고    scopus 로고
    • Regulation of phospholipase C-beta1 by Gq and m1 muscarinic cholinergic receptor. Steady-state balance of receptor-mediated activation and GTPase-Activating protein-promoted deactivation
    • G.H. Biddlecome, G. Berstein, and E.M. Ross Regulation of phospholipase C-beta1 by Gq and m1 muscarinic cholinergic receptor. Steady-state balance of receptor-mediated activation and GTPase-Activating protein-promoted deactivation J Biol Chem 271 1996 7999 8007
    • (1996) J Biol Chem , vol.271 , pp. 7999-8007
    • Biddlecome, G.H.1    Berstein, G.2    Ross, E.M.3
  • 57
    • 0026694917 scopus 로고
    • Phospholipase C-beta 1 is a GTPase-Activating protein for Gq/11, its physiologic regulator
    • G. Berstein, J.L. Blank, D.Y. Jhon, J.H. Exton, S.G. Rhee, and E.M. Ross Phospholipase C-beta 1 is a GTPase-Activating protein for Gq/11, its physiologic regulator Cell 70 1992 411 418
    • (1992) Cell , vol.70 , pp. 411-418
    • Berstein, G.1    Blank, J.L.2    Jhon, D.Y.3    Exton, J.H.4    Rhee, S.G.5    Ross, E.M.6
  • 58
    • 84855996266 scopus 로고    scopus 로고
    • RGS4 exerts inhibitory activities on the signaling of dopamine D2 receptor and D3 receptor through the N-terminal region
    • C. Min, S.Y. Cheong, S.J. Cheong, M. Kim, D.I. Cho, and K.M. Kim RGS4 exerts inhibitory activities on the signaling of dopamine D2 receptor and D3 receptor through the N-terminal region Pharmacol Res 65 2012 213 220
    • (2012) Pharmacol Res , vol.65 , pp. 213-220
    • Min, C.1    Cheong, S.Y.2    Cheong, S.J.3    Kim, M.4    Cho, D.I.5    Kim, K.M.6
  • 59
    • 0032567439 scopus 로고    scopus 로고
    • The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling
    • W. Zeng, X. Xu, S. Popov, S. Mukhopadhyay, P. Chidiac, and J. Swistok The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling J Biol Chem 273 1998 34687 34690
    • (1998) J Biol Chem , vol.273 , pp. 34687-34690
    • Zeng, W.1    Xu, X.2    Popov, S.3    Mukhopadhyay, S.4    Chidiac, P.5    Swistok, J.6
  • 60
    • 79952702749 scopus 로고    scopus 로고
    • Potent and selective inhibition of angiotensin AT1 receptor signaling by RGS2: Roles of its N-terminal domain
    • N. Matsuzaki, M. Nishiyama, D. Song, K. Moroi, and S. Kimura Potent and selective inhibition of angiotensin AT1 receptor signaling by RGS2: roles of its N-terminal domain Cell Signal 23 2011 1041 1049
    • (2011) Cell Signal , vol.23 , pp. 1041-1049
    • Matsuzaki, N.1    Nishiyama, M.2    Song, D.3    Moroi, K.4    Kimura, S.5
  • 61
    • 77953677609 scopus 로고    scopus 로고
    • Molecular organization of the complex between the muscarinic M3 receptor and the regulator of G protein signaling, Gbeta(5)-RGS7
    • S.L. Sandiford, Q. Wang, K. Levay, P. Buchwald, and V.Z. Slepak Molecular organization of the complex between the muscarinic M3 receptor and the regulator of G protein signaling, Gbeta(5)-RGS7 Biochemistry 49 2010 4998 5006
    • (2010) Biochemistry , vol.49 , pp. 4998-5006
    • Sandiford, S.L.1    Wang, Q.2    Levay, K.3    Buchwald, P.4    Slepak, V.Z.5
  • 62
    • 84863121487 scopus 로고    scopus 로고
    • Neurabin scaffolding of adenosine receptor and RGS4 regulates anti-seizure effect of endogenous adenosine
    • Y. Chen, Y. Liu, C. Cottingham, L. McMahon, K. Jiao, and P. Greengard Neurabin scaffolding of adenosine receptor and RGS4 regulates anti-seizure effect of endogenous adenosine J Neurosci 32 2012 2683 2695
    • (2012) J Neurosci , vol.32 , pp. 2683-2695
    • Chen, Y.1    Liu, Y.2    Cottingham, C.3    McMahon, L.4    Jiao, K.5    Greengard, P.6
  • 63
    • 17344367802 scopus 로고    scopus 로고
    • Spinophilin regulates Ca2 + signaling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors
    • X. Wang, W. Zeng, A.A. Soyombo, W. Tang, E.M. Ross, and A.P. Barnes Spinophilin regulates Ca2 + signaling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors Nat Cell Biol 7 2005 405 411
    • (2005) Nat Cell Biol , vol.7 , pp. 405-411
    • Wang, X.1    Zeng, W.2    Soyombo, A.A.3    Tang, W.4    Ross, E.M.5    Barnes, A.P.6
  • 64
    • 84868152419 scopus 로고    scopus 로고
    • Spinophilin as a novel regulator of M3 muscarinic receptor-mediated insulin release in vitro and in vivo
    • I. Ruiz de Azua, K. Nakajima, M. Rossi, Y. Cui, W. Jou, and O. Gavrilova Spinophilin as a novel regulator of M3 muscarinic receptor-mediated insulin release in vitro and in vivo FASEB J 26 2012 4275 4286
    • (2012) FASEB J , vol.26 , pp. 4275-4286
    • Ruiz De Azua, I.1    Nakajima, K.2    Rossi, M.3    Cui, Y.4    Jou, W.5    Gavrilova, O.6
  • 65
    • 0033524915 scopus 로고    scopus 로고
    • RGS proteins determine signaling specificity of Gq-coupled receptors
    • X. Xu, W. Zeng, S. Popov, D.M. Berman, I. Davignon, and K. Yu RGS proteins determine signaling specificity of Gq-coupled receptors J Biol Chem 274 1999 3549 3556
    • (1999) J Biol Chem , vol.274 , pp. 3549-3556
    • Xu, X.1    Zeng, W.2    Popov, S.3    Berman, D.M.4    Davignon, I.5    Yu, K.6
  • 66
    • 0037067761 scopus 로고    scopus 로고
    • Receptor-selective effects of endogenous RGS3 and RGS5 to regulate mitogen-Activated protein kinase activation in rat vascular smooth muscle cells
    • Q. Wang, M. Liu, B. Mullah, D.P. Siderovski, and R.R. Neubig Receptor-selective effects of endogenous RGS3 and RGS5 to regulate mitogen-Activated protein kinase activation in rat vascular smooth muscle cells J Biol Chem 277 2002 24949 24958
    • (2002) J Biol Chem , vol.277 , pp. 24949-24958
    • Wang, Q.1    Liu, M.2    Mullah, B.3    Siderovski, D.P.4    Neubig, R.R.5
  • 67
    • 0037162557 scopus 로고    scopus 로고
    • Alternative splicing of RGS8 gene determines inhibitory function of receptor type-specific Gq signaling
    • O. Saitoh, Y. Murata, M. Odagiri, M. Itoh, H. Itoh, and T. Misaka Alternative splicing of RGS8 gene determines inhibitory function of receptor type-specific Gq signaling Proc Natl Acad Sci USA 99 2002 10138 10143
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 10138-10143
    • Saitoh, O.1    Murata, Y.2    Odagiri, M.3    Itoh, M.4    Itoh, H.5    Misaka, T.6
  • 68
    • 0037569639 scopus 로고    scopus 로고
    • The aorta and heart differentially express RGS (regulators of G-protein signaling) proteins that selectively regulate sphingosine 1-phosphate, angiotensin II and endothelin-1 signaling
    • H. Cho, K. Harrison, O. Schwartz, and J.H. Kehrl The aorta and heart differentially express RGS (regulators of G-protein signaling) proteins that selectively regulate sphingosine 1-phosphate, angiotensin II and endothelin-1 signaling Biochem J 371 2003 973 980
    • (2003) Biochem J , vol.371 , pp. 973-980
    • Cho, H.1    Harrison, K.2    Schwartz, O.3    Kehrl, J.H.4
  • 69
    • 17144381258 scopus 로고    scopus 로고
    • Regulators of G-protein signaling form a quaternary complex with the agonist, receptor, and G-protein. A novel explanation for the acceleration of signaling activation kinetics
    • A. Benians, M. Nobles, S. Hosny, and A. Tinker Regulators of G-protein signaling form a quaternary complex with the agonist, receptor, and G-protein. A novel explanation for the acceleration of signaling activation kinetics J Biol Chem 280 2005 13383 13394
    • (2005) J Biol Chem , vol.280 , pp. 13383-13394
    • Benians, A.1    Nobles, M.2    Hosny, S.3    Tinker, A.4
  • 70
    • 67651146336 scopus 로고    scopus 로고
    • Histamine H(4) receptor-RGS fusion proteins expressed in Sf9 insect cells: A sensitive and reliable approach for the functional characterization of histamine H(4) receptor ligands
    • E.H. Schneider, and R. Seifert Histamine H(4) receptor-RGS fusion proteins expressed in Sf9 insect cells: a sensitive and reliable approach for the functional characterization of histamine H(4) receptor ligands Biochem Pharmacol 78 2009 607 616
    • (2009) Biochem Pharmacol , vol.78 , pp. 607-616
    • Schneider, E.H.1    Seifert, R.2
  • 71
    • 33750330250 scopus 로고    scopus 로고
    • Modulation of subfamily B/R4 RGS protein function by 14-3-3 proteins
    • M. Abramow-Newerly, H. Ming, and P. Chidiac Modulation of subfamily B/R4 RGS protein function by 14-3-3 proteins Cell Signal 18 2006 2209 2222
    • (2006) Cell Signal , vol.18 , pp. 2209-2222
    • Abramow-Newerly, M.1    Ming, H.2    Chidiac, P.3
  • 72
    • 1042266676 scopus 로고    scopus 로고
    • Differential contribution of GTPase activation and effector antagonism to the inhibitory effect of RGS proteins on Gq-mediated signaling in vivo
    • T. Anger, W. Zhang, and U. Mende Differential contribution of GTPase activation and effector antagonism to the inhibitory effect of RGS proteins on Gq-mediated signaling in vivo J Biol Chem 279 2004 3906 3915
    • (2004) J Biol Chem , vol.279 , pp. 3906-3915
    • Anger, T.1    Zhang, W.2    Mende, U.3
  • 73
    • 2442717874 scopus 로고    scopus 로고
    • RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11alpha signaling
    • L.S. Bernstein, S. Ramineni, C. Hague, W. Cladman, P. Chidiac, and A.I. Levey RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11alpha signaling J Biol Chem 279 2004 21248 21256
    • (2004) J Biol Chem , vol.279 , pp. 21248-21256
    • Bernstein, L.S.1    Ramineni, S.2    Hague, C.3    Cladman, W.4    Chidiac, P.5    Levey, A.I.6
  • 74
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: Organizers of transmembrane signals
    • E.J. Neer Heterotrimeric G proteins: organizers of transmembrane signals Cell 80 1995 249 257
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 75
    • 33947321414 scopus 로고    scopus 로고
    • Molecular basis of guanine nucleotide dissociation inhibitor activity of human neuroglobin by chemical cross-linking and mass spectrometry
    • C. Kitatsuji, M. Kurogochi, S. Nishimura, K. Ishimori, and K. Wakasugi Molecular basis of guanine nucleotide dissociation inhibitor activity of human neuroglobin by chemical cross-linking and mass spectrometry J Mol Biol 368 2007 150 160
    • (2007) J Mol Biol , vol.368 , pp. 150-160
    • Kitatsuji, C.1    Kurogochi, M.2    Nishimura, S.3    Ishimori, K.4    Wakasugi, K.5
  • 76
    • 0141704224 scopus 로고    scopus 로고
    • Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor
    • K. Wakasugi, T. Nakano, and I. Morishima Oxidized human neuroglobin acts as a heterotrimeric Galpha protein guanine nucleotide dissociation inhibitor J Biol Chem 278 2003 36505 36512
    • (2003) J Biol Chem , vol.278 , pp. 36505-36512
    • Wakasugi, K.1    Nakano, T.2    Morishima, I.3
  • 77
  • 78
    • 0032859735 scopus 로고    scopus 로고
    • Genetic screens in yeast to identify mammalian nonreceptor modulators of G-protein signaling
    • M.J. Cismowski, A. Takesono, C. Ma, J.S. Lizano, X. Xie, and H. Fuernkranz Genetic screens in yeast to identify mammalian nonreceptor modulators of G-protein signaling Nat Biotechnol 17 1999 878 883
    • (1999) Nat Biotechnol , vol.17 , pp. 878-883
    • Cismowski, M.J.1    Takesono, A.2    Ma, C.3    Lizano, J.S.4    Xie, X.5    Fuernkranz, H.6
  • 79
  • 81
    • 0033181320 scopus 로고    scopus 로고
    • The GoLoco motif: A Galphai/o binding motif and potential guanine-nucleotide exchange factor
    • D.P. Siderovski, M. Diverse-Pierluissi, and L. De Vries The GoLoco motif: a Galphai/o binding motif and potential guanine-nucleotide exchange factor Trends Biochem Sci 24 1999 340 341
    • (1999) Trends Biochem Sci , vol.24 , pp. 340-341
    • Siderovski, D.P.1    Diverse-Pierluissi, M.2    De Vries, L.3
  • 82
    • 0001793118 scopus 로고    scopus 로고
    • Identification and cDNA cloning of a novel human mosaic protein, LGN, based on interaction with G alpha i2
    • N. Mochizuki, G. Cho, B. Wen, and P.A. Insel Identification and cDNA cloning of a novel human mosaic protein, LGN, based on interaction with G alpha i2 Gene 181 1996 39 43
    • (1996) Gene , vol.181 , pp. 39-43
    • Mochizuki, N.1    Cho, G.2    Wen, B.3    Insel, P.A.4
  • 83
    • 0032751298 scopus 로고    scopus 로고
    • Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signaling proteins
    • C.P. Ponting Raf-like Ras/Rap-binding domains in RGS12- and still-life-like signaling proteins J Mol Med (Berl) 77 1999 695 698
    • (1999) J Mol Med (Berl) , vol.77 , pp. 695-698
    • Ponting, C.P.1
  • 84
    • 23944437743 scopus 로고    scopus 로고
    • AGS proteins: Receptor-independent activators of G-protein signaling
    • J.B. Blumer, M.J. Cismowski, M. Sato, and S.M. Lanier AGS proteins: receptor-independent activators of G-protein signaling Trends Pharmacol Sci 26 2005 470 476
    • (2005) Trends Pharmacol Sci , vol.26 , pp. 470-476
    • Blumer, J.B.1    Cismowski, M.J.2    Sato, M.3    Lanier, S.M.4
  • 85
    • 0034731441 scopus 로고    scopus 로고
    • AGS3 inhibits GDP dissociation from galpha subunits of the Gi family and rhodopsin-dependent activation of transducin
    • M. Natochin, B. Lester, Y.K. Peterson, M.L. Bernard, S.M. Lanier, and N.O. Artemyev AGS3 inhibits GDP dissociation from galpha subunits of the Gi family and rhodopsin-dependent activation of transducin J Biol Chem 275 2000 40981 40985
    • (2000) J Biol Chem , vol.275 , pp. 40981-40985
    • Natochin, M.1    Lester, B.2    Peterson, Y.K.3    Bernard, M.L.4    Lanier, S.M.5    Artemyev, N.O.6
  • 86
    • 0037171778 scopus 로고    scopus 로고
    • Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits
    • R.J. Kimple, M.E. Kimple, L. Betts, J. Sondek, and D.P. Siderovski Structural determinants for GoLoco-induced inhibition of nucleotide release by Galpha subunits Nature 416 2002 878 881
    • (2002) Nature , vol.416 , pp. 878-881
    • Kimple, R.J.1    Kimple, M.E.2    Betts, L.3    Sondek, J.4    Siderovski, D.P.5
  • 87
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
    • D.P. Siderovski, and F.S. Willard The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits Int J Biol Sci 1 2005 51 66
    • (2005) Int J Biol Sci , vol.1 , pp. 51-66
    • Siderovski, D.P.1    Willard, F.S.2
  • 88
    • 0035847021 scopus 로고    scopus 로고
    • Selective interaction of AGS3 with G-proteins and the influence of AGS3 on the activation state of G-proteins
    • M.L. Bernard, Y.K. Peterson, P. Chung, J. Jourdan, and S.M. Lanier Selective interaction of AGS3 with G-proteins and the influence of AGS3 on the activation state of G-proteins J Biol Chem 276 2001 1585 1593
    • (2001) J Biol Chem , vol.276 , pp. 1585-1593
    • Bernard, M.L.1    Peterson, Y.K.2    Chung, P.3    Jourdan, J.4    Lanier, S.M.5
  • 89
    • 0041315914 scopus 로고    scopus 로고
    • Receptor- and nucleotide exchange-independent mechanisms for promoting G protein subunit dissociation
    • M. Ghosh, Y.K. Peterson, S.M. Lanier, and A.V. Smrcka Receptor- and nucleotide exchange-independent mechanisms for promoting G protein subunit dissociation J Biol Chem 278 2003 34747 34750
    • (2003) J Biol Chem , vol.278 , pp. 34747-34750
    • Ghosh, M.1    Peterson, Y.K.2    Lanier, S.M.3    Smrcka, A.V.4
  • 90
    • 33144486942 scopus 로고    scopus 로고
    • Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A
    • V. Mittal, and M.E. Linder Biochemical characterization of RGS14: RGS14 activity towards G-protein alpha subunits is independent of its binding to Rap2A Biochem J 394 2006 309 315
    • (2006) Biochem J , vol.394 , pp. 309-315
    • Mittal, V.1    Linder, M.E.2
  • 91
    • 15244351924 scopus 로고    scopus 로고
    • D2 dopamine receptor activation of potassium channels is selectively decoupled by Galpha-specific GoLoco motif peptides
    • C.K. Webb, C.R. McCudden, F.S. Willard, R.J. Kimple, D.P. Siderovski, and G.S. Oxford D2 dopamine receptor activation of potassium channels is selectively decoupled by Galpha-specific GoLoco motif peptides J Neurochem 92 2005 1408 1418
    • (2005) J Neurochem , vol.92 , pp. 1408-1418
    • Webb, C.K.1    McCudden, C.R.2    Willard, F.S.3    Kimple, R.J.4    Siderovski, D.P.5    Oxford, G.S.6
  • 92
    • 22144436963 scopus 로고    scopus 로고
    • G protein betagamma subunits and AGS3 control spindle orientation and asymmetric cell fate of cerebral cortical progenitors
    • K. Sanada, and L.H. Tsai G protein betagamma subunits and AGS3 control spindle orientation and asymmetric cell fate of cerebral cortical progenitors Cell 122 2005 119 131
    • (2005) Cell , vol.122 , pp. 119-131
    • Sanada, K.1    Tsai, L.H.2
  • 93
    • 84856899959 scopus 로고    scopus 로고
    • G-protein signaling modulator-3 regulates heterotrimeric G-protein dynamics through dual association with Gbeta and Galphai protein subunits
    • P.M. Giguere, G. Laroche, E.A. Oestreich, and D.P. Siderovski G-protein signaling modulator-3 regulates heterotrimeric G-protein dynamics through dual association with Gbeta and Galphai protein subunits J Biol Chem 287 2012 4863 4874
    • (2012) J Biol Chem , vol.287 , pp. 4863-4874
    • Giguere, P.M.1    Laroche, G.2    Oestreich, E.A.3    Siderovski, D.P.4
  • 94
    • 33646393502 scopus 로고    scopus 로고
    • Modulation of basal and receptor-induced GIRK potassium channel activity and neuronal excitability by the mammalian PINS homolog LGN
    • O. Wiser, X. Qian, M. Ehlers, W.W. Ja, R.W. Roberts, and E. Reuveny Modulation of basal and receptor-induced GIRK potassium channel activity and neuronal excitability by the mammalian PINS homolog LGN Neuron 50 2006 561 573
    • (2006) Neuron , vol.50 , pp. 561-573
    • Wiser, O.1    Qian, X.2    Ehlers, M.3    Ja, W.W.4    Roberts, R.W.5    Reuveny, E.6
  • 95
    • 8844253281 scopus 로고    scopus 로고
    • A Purkinje cell specific GoLoco domain protein, L7/Pcp-2, modulates receptor-mediated inhibition of Cav2.1 Ca2 + channels in a dose-dependent manner
    • M. Kinoshita-Kawada, J. Oberdick, and M. Xi Zhu A Purkinje cell specific GoLoco domain protein, L7/Pcp-2, modulates receptor-mediated inhibition of Cav2.1 Ca2 + channels in a dose-dependent manner Brain Res Mol Brain Res 132 2004 73 86
    • (2004) Brain Res Mol Brain Res , vol.132 , pp. 73-86
    • Kinoshita-Kawada, M.1    Oberdick, J.2    Xi Zhu, M.3
  • 97
    • 77958533744 scopus 로고    scopus 로고
    • Regulation of the AGS3.G{alpha}i signaling complex by a seven-transmembrane span receptor
    • S.S. Oner, N. An, A. Vural, B. Breton, M. Bouvier, and J.B. Blumer Regulation of the AGS3.G{alpha}i signaling complex by a seven-transmembrane span receptor J Biol Chem 285 2010 33949 33958
    • (2010) J Biol Chem , vol.285 , pp. 33949-33958
    • Oner, S.S.1    An, N.2    Vural, A.3    Breton, B.4    Bouvier, M.5    Blumer, J.B.6
  • 98
    • 77950589178 scopus 로고    scopus 로고
    • The proline-rich N-terminal domain of G18 exhibits a novel G protein regulatory function
    • P. Zhao, C.H. Nguyen, and P. Chidiac The proline-rich N-terminal domain of G18 exhibits a novel G protein regulatory function J Biol Chem 285 2010 9008 9017
    • (2010) J Biol Chem , vol.285 , pp. 9008-9017
    • Zhao, P.1    Nguyen, C.H.2    Chidiac, P.3
  • 99
    • 53149142138 scopus 로고    scopus 로고
    • Ric-8A catalyzes guanine nucleotide exchange on G alphai1 bound to the GPR/GoLoco exchange inhibitor AGS3
    • C.J. Thomas, G.G. Tall, A. Adhikari, and S.R. Sprang Ric-8A catalyzes guanine nucleotide exchange on G alphai1 bound to the GPR/GoLoco exchange inhibitor AGS3 J Biol Chem 283 2008 23150 23160
    • (2008) J Biol Chem , vol.283 , pp. 23150-23160
    • Thomas, C.J.1    Tall, G.G.2    Adhikari, A.3    Sprang, S.R.4
  • 100
    • 33847781275 scopus 로고    scopus 로고
    • Mechanistic pathways and biological roles for receptor-independent activators of G-protein signaling
    • J.B. Blumer, A.V. Smrcka, and S.M. Lanier Mechanistic pathways and biological roles for receptor-independent activators of G-protein signaling Pharmacol Ther 113 2007 488 506
    • (2007) Pharmacol Ther , vol.113 , pp. 488-506
    • Blumer, J.B.1    Smrcka, A.V.2    Lanier, S.M.3
  • 101
    • 0030740849 scopus 로고    scopus 로고
    • Sensitization to the behavioral effects of cocaine: Modulation by dynorphin and kappa-opioid receptor agonists
    • T.S. Shippenberg, and W. Rea Sensitization to the behavioral effects of cocaine: modulation by dynorphin and kappa-opioid receptor agonists Pharmacol Biochem Behav 57 1997 449 455
    • (1997) Pharmacol Biochem Behav , vol.57 , pp. 449-455
    • Shippenberg, T.S.1    Rea, W.2
  • 102
    • 4043053853 scopus 로고    scopus 로고
    • Activator of G protein signaling 3: A gatekeeper of cocaine sensitization and drug seeking
    • M.S. Bowers, K. McFarland, R.W. Lake, Y.K. Peterson, C.C. Lapish, and M.L. Gregory Activator of G protein signaling 3: a gatekeeper of cocaine sensitization and drug seeking Neuron 42 2004 269 281
    • (2004) Neuron , vol.42 , pp. 269-281
    • Bowers, M.S.1    McFarland, K.2    Lake, R.W.3    Peterson, Y.K.4    Lapish, C.C.5    Gregory, M.L.6
  • 103
    • 77955985368 scopus 로고    scopus 로고
    • Activators of G-protein signaling 3: A drug addiction molecular gateway
    • M.S. Bowers Activators of G-protein signaling 3: a drug addiction molecular gateway Behav Pharmacol 21 2010 500 513
    • (2010) Behav Pharmacol , vol.21 , pp. 500-513
    • Bowers, M.S.1
  • 105
    • 79957620875 scopus 로고    scopus 로고
    • Ric-8B is a GTP-dependent G protein alphas guanine nucleotide exchange factor
    • P. Chan, M. Gabay, F.A. Wright, and G.G. Tall Ric-8B is a GTP-dependent G protein alphas guanine nucleotide exchange factor J Biol Chem 286 2011 19932 19942
    • (2011) J Biol Chem , vol.286 , pp. 19932-19942
    • Chan, P.1    Gabay, M.2    Wright, F.A.3    Tall, G.G.4
  • 106
    • 62549124627 scopus 로고    scopus 로고
    • GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates Akt signaling
    • M. Garcia-Marcos, P. Ghosh, and M.G. Farquhar GIV is a nonreceptor GEF for G alpha i with a unique motif that regulates Akt signaling Proc Natl Acad Sci USA 106 2009 3178 3183
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 3178-3183
    • Garcia-Marcos, M.1    Ghosh, P.2    Farquhar, M.G.3
  • 107
    • 0034604518 scopus 로고    scopus 로고
    • Activation of heterotrimeric G-protein signaling by a ras-related protein. Implications for signal integration
    • M.J. Cismowski, C. Ma, C. Ribas, X. Xie, M. Spruyt, and J.S. Lizano Activation of heterotrimeric G-protein signaling by a ras-related protein. Implications for signal integration J Biol Chem 275 2000 23421 23424
    • (2000) J Biol Chem , vol.275 , pp. 23421-23424
    • Cismowski, M.J.1    Ma, C.2    Ribas, C.3    Xie, X.4    Spruyt, M.5    Lizano, J.S.6
  • 108
    • 0025889699 scopus 로고
    • An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism
    • S.M. Strittmatter, D. Valenzuela, Y. Sudo, M.E. Linder, and M.C. Fishman An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism J Biol Chem 266 1991 22465 22471
    • (1991) J Biol Chem , vol.266 , pp. 22465-22471
    • Strittmatter, S.M.1    Valenzuela, D.2    Sudo, Y.3    Linder, M.E.4    Fishman, M.C.5
  • 110
    • 0035955736 scopus 로고    scopus 로고
    • Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling
    • T. Kroslak, T. Koch, E. Kahl, and V. Hollt Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling J Biol Chem 276 2001 39772 39778
    • (2001) J Biol Chem , vol.276 , pp. 39772-39778
    • Kroslak, T.1    Koch, T.2    Kahl, E.3    Hollt, V.4
  • 111
  • 112
    • 0032568846 scopus 로고    scopus 로고
    • Regulation of brain G-protein go by Alzheimer's disease gene presenilin-1
    • A. Smine, X. Xu, K. Nishiyama, T. Katada, P. Gambetti, and S.P. Yadav Regulation of brain G-protein go by Alzheimer's disease gene presenilin-1 J Biol Chem 273 1998 16281 16288
    • (1998) J Biol Chem , vol.273 , pp. 16281-16288
    • Smine, A.1    Xu, X.2    Nishiyama, K.3    Katada, T.4    Gambetti, P.5    Yadav, S.P.6
  • 113
    • 38849206178 scopus 로고    scopus 로고
    • Coactivation of G protein signaling by cell-surface receptors and an intracellular exchange factor
    • M.J. Lee, and H.G. Dohlman Coactivation of G protein signaling by cell-surface receptors and an intracellular exchange factor Curr Biol 18 2008 211 215
    • (2008) Curr Biol , vol.18 , pp. 211-215
    • Lee, M.J.1    Dohlman, H.G.2
  • 114
    • 80051486142 scopus 로고    scopus 로고
    • G Protein binding sites on Calnuc (nucleobindin 1) and NUCB2 (nucleobindin 2) define a new class of G(alpha)i-regulatory motifs
    • M. Garcia-Marcos, P.S. Kietrsunthorn, H. Wang, P. Ghosh, and M.G. Farquhar G Protein binding sites on Calnuc (nucleobindin 1) and NUCB2 (nucleobindin 2) define a new class of G(alpha)i-regulatory motifs J Biol Chem 286 2011 28138 28149
    • (2011) J Biol Chem , vol.286 , pp. 28138-28149
    • Garcia-Marcos, M.1    Kietrsunthorn, P.S.2    Wang, H.3    Ghosh, P.4    Farquhar, M.G.5
  • 115
    • 34250816197 scopus 로고    scopus 로고
    • E2F8 is a nonreceptor activator of heterotrimeric G proteins
    • I.S. Hagemann, K.D. Narzinski, and T.J. Baranski E2F8 is a nonreceptor activator of heterotrimeric G proteins J Mol Signal 2 2007 3
    • (2007) J Mol Signal , vol.2 , pp. 3
    • Hagemann, I.S.1    Narzinski, K.D.2    Baranski, T.J.3
  • 116
    • 0029860884 scopus 로고    scopus 로고
    • Characterization of a G-protein activator in the neuroblastoma-glioma cell hybrid NG108-15
    • M. Sato, C. Ribas, J.D. Hildebrandt, and S.M. Lanier Characterization of a G-protein activator in the neuroblastoma-glioma cell hybrid NG108-15 J Biol Chem 271 1996 30052 30060
    • (1996) J Biol Chem , vol.271 , pp. 30052-30060
    • Sato, M.1    Ribas, C.2    Hildebrandt, J.D.3    Lanier, S.M.4
  • 117
    • 4143085992 scopus 로고    scopus 로고
    • Single transmembrane spanning heterotrimeric g protein-coupled receptors and their signaling cascades
    • T.B. Patel Single transmembrane spanning heterotrimeric g protein-coupled receptors and their signaling cascades Pharmacol Rev 56 2004 371 385
    • (2004) Pharmacol Rev , vol.56 , pp. 371-385
    • Patel, T.B.1
  • 118
    • 77953798290 scopus 로고    scopus 로고
    • Heterotrimeric G protein signaling outside the realm of seven transmembrane domain receptors
    • C. Marty, and R.D. Ye Heterotrimeric G protein signaling outside the realm of seven transmembrane domain receptors Mol Pharmacol 78 2010 12 18
    • (2010) Mol Pharmacol , vol.78 , pp. 12-18
    • Marty, C.1    Ye, R.D.2
  • 120
    • 61349146609 scopus 로고    scopus 로고
    • Insulin-like growth factor-2/mannose-6 phosphate receptors
    • H.M. El-Shewy, and L.M. Luttrell Insulin-like growth factor-2/mannose-6 phosphate receptors Vitam Horm 80 2009 667 697
    • (2009) Vitam Horm , vol.80 , pp. 667-697
    • El-Shewy, H.M.1    Luttrell, L.M.2
  • 122
    • 84863692164 scopus 로고    scopus 로고
    • Ric-8: Different cellular roles for a heterotrimeric G-protein GEF
    • M.V. Hinrichs, M. Torrejon, M. Montecino, and J. Olate Ric-8: different cellular roles for a heterotrimeric G-protein GEF J Cell Biochem 113 2012 2797 2805
    • (2012) J Cell Biochem , vol.113 , pp. 2797-2805
    • Hinrichs, M.V.1    Torrejon, M.2    Montecino, M.3    Olate, J.4
  • 123
    • 0037424298 scopus 로고    scopus 로고
    • Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor
    • G.G. Tall, A.M. Krumins, and A.G. Gilman Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor J Biol Chem 278 2003 8356 8362
    • (2003) J Biol Chem , vol.278 , pp. 8356-8362
    • Tall, G.G.1    Krumins, A.M.2    Gilman, A.G.3
  • 124
    • 33645830270 scopus 로고    scopus 로고
    • Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells
    • A. Nishimura, M. Okamoto, Y. Sugawara, N. Mizuno, J. Yamauchi, and H. Itoh Ric-8A potentiates Gq-mediated signal transduction by acting downstream of G protein-coupled receptor in intact cells Genes Cells 11 2006 487 498
    • (2006) Genes Cells , vol.11 , pp. 487-498
    • Nishimura, A.1    Okamoto, M.2    Sugawara, Y.3    Mizuno, N.4    Yamauchi, J.5    Itoh, H.6
  • 125
    • 0037401761 scopus 로고    scopus 로고
    • Human brain synembryn interacts with Gsalpha and Gqalpha and is translocated to the plasma membrane in response to isoproterenol and carbachol
    • C. Klattenhoff, M. Montecino, X. Soto, L. Guzman, X. Romo, and M.A. Garcia Human brain synembryn interacts with Gsalpha and Gqalpha and is translocated to the plasma membrane in response to isoproterenol and carbachol J Cell Physiol 195 2003 151 157
    • (2003) J Cell Physiol , vol.195 , pp. 151-157
    • Klattenhoff, C.1    Montecino, M.2    Soto, X.3    Guzman, L.4    Romo, X.5    Garcia, M.A.6
  • 126
    • 17644404436 scopus 로고    scopus 로고
    • Ric-8B, an olfactory putative GTP exchange factor, amplifies signal transduction through the olfactory-specific G-protein Galphaolf
    • L.E. Von Dannecker, A.F. Mercadante, and B. Malnic Ric-8B, an olfactory putative GTP exchange factor, amplifies signal transduction through the olfactory-specific G-protein Galphaolf J Neurosci 25 2005 3793 3800
    • (2005) J Neurosci , vol.25 , pp. 3793-3800
    • Von Dannecker, L.E.1    Mercadante, A.F.2    Malnic, B.3
  • 127
    • 34548726080 scopus 로고    scopus 로고
    • Regulation of type v adenylate cyclase by Ric8a, a guanine nucleotide exchange factor
    • S.C. Wang, H.L. Lai, Y.T. Chiu, R. Ou, C.L. Huang, and Y. Chern Regulation of type V adenylate cyclase by Ric8a, a guanine nucleotide exchange factor Biochem J 406 2007 383 388
    • (2007) Biochem J , vol.406 , pp. 383-388
    • Wang, S.C.1    Lai, H.L.2    Chiu, Y.T.3    Ou, R.4    Huang, C.L.5    Chern, Y.6
  • 128
    • 84857463931 scopus 로고    scopus 로고
    • NCAM180 regulates Ric8A membrane localization and potentiates beta-Adrenergic response
    • M.C. Amoureux, S. Nicolas, and G. Rougon NCAM180 regulates Ric8A membrane localization and potentiates beta-Adrenergic response PLoS One 7 2012 e32216
    • (2012) PLoS One , vol.7 , pp. 32216
    • Amoureux, M.C.1    Nicolas, S.2    Rougon, G.3
  • 129
    • 28844481199 scopus 로고    scopus 로고
    • Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins
    • B. Hampoelz, O. Hoeller, S.K. Bowman, D. Dunican, and J.A. Knoblich Drosophila Ric-8 is essential for plasma-membrane localization of heterotrimeric G proteins Nat Cell Biol 7 2005 1099 1105
    • (2005) Nat Cell Biol , vol.7 , pp. 1099-1105
    • Hampoelz, B.1    Hoeller, O.2    Bowman, S.K.3    Dunican, D.4    Knoblich, J.A.5
  • 130
    • 81855183850 scopus 로고    scopus 로고
    • Ric-8 proteins are molecular chaperones that direct nascent G protein alpha subunit membrane association
    • M. Gabay, M.E. Pinter, F.A. Wright, P. Chan, A.J. Murphy, and D.M. Valenzuela Ric-8 proteins are molecular chaperones that direct nascent G protein alpha subunit membrane association Sci Signal 4 2011 ra79
    • (2011) Sci Signal , vol.4 , pp. 79
    • Gabay, M.1    Pinter, M.E.2    Wright, F.A.3    Chan, P.4    Murphy, A.J.5    Valenzuela, D.M.6
  • 131
    • 78649713805 scopus 로고    scopus 로고
    • Nucleotide exchange factor RIC-8 is indispensable in mammalian early development
    • T. Tonissoo, S. Lulla, R. Meier, M. Saare, K. Ruisu, and M. Pooga Nucleotide exchange factor RIC-8 is indispensable in mammalian early development Dev Dyn 239 2010 3404 3415
    • (2010) Dev Dyn , vol.239 , pp. 3404-3415
    • Tonissoo, T.1    Lulla, S.2    Meier, R.3    Saare, M.4    Ruisu, K.5    Pooga, M.6
  • 132
    • 77951215559 scopus 로고    scopus 로고
    • Ric-8B stabilizes the alpha subunit of stimulatory G protein by inhibiting its ubiquitination
    • Y. Nagai, A. Nishimura, K. Tago, N. Mizuno, and H. Itoh Ric-8B stabilizes the alpha subunit of stimulatory G protein by inhibiting its ubiquitination J Biol Chem 285 2010 11114 11120
    • (2010) J Biol Chem , vol.285 , pp. 11114-11120
    • Nagai, Y.1    Nishimura, A.2    Tago, K.3    Mizuno, N.4    Itoh, H.5
  • 134
    • 78951480403 scopus 로고    scopus 로고
    • Purification of heterotrimeric G protein alpha subunits by GST-Ric-8 association: Primary characterization of purified G alpha(olf)
    • P. Chan, M. Gabay, F.A. Wright, W. Kan, S.S. Oner, and S.M. Lanier Purification of heterotrimeric G protein alpha subunits by GST-Ric-8 association: primary characterization of purified G alpha(olf) J Biol Chem 286 2011 2625 2635
    • (2011) J Biol Chem , vol.286 , pp. 2625-2635
    • Chan, P.1    Gabay, M.2    Wright, F.A.3    Kan, W.4    Oner, S.S.5    Lanier, S.M.6
  • 135
    • 80051557240 scopus 로고    scopus 로고
    • AGS-3 alters Caenorhabditis elegans behavior after food deprivation via RIC-8 activation of the neural G protein G alphao
    • C. Hofler, and M.R. Koelle AGS-3 alters Caenorhabditis elegans behavior after food deprivation via RIC-8 activation of the neural G protein G alphao J Neurosci 31 2011 11553 11562
    • (2011) J Neurosci , vol.31 , pp. 11553-11562
    • Hofler, C.1    Koelle, M.R.2
  • 136
    • 48949120507 scopus 로고    scopus 로고
    • Differential dissociation of G protein heterotrimers
    • G.J. Digby, P.R. Sethi, and N.A. Lambert Differential dissociation of G protein heterotrimers J Physiol 586 2008 3325 3335
    • (2008) J Physiol , vol.586 , pp. 3325-3335
    • Digby, G.J.1    Sethi, P.R.2    Lambert, N.A.3
  • 137
    • 48249106623 scopus 로고    scopus 로고
    • Activation of Galphai3 triggers cell migration via regulation of GIV
    • P. Ghosh, M. Garcia-Marcos, S.J. Bornheimer, and M.G. Farquhar Activation of Galphai3 triggers cell migration via regulation of GIV J Cell Biol 182 2008 381 393
    • (2008) J Cell Biol , vol.182 , pp. 381-393
    • Ghosh, P.1    Garcia-Marcos, M.2    Bornheimer, S.J.3    Farquhar, M.G.4
  • 138
    • 84857128930 scopus 로고    scopus 로고
    • Functional characterization of the guanine nucleotide exchange factor (GEF) motif of GIV protein reveals a threshold effect in signaling
    • M. Garcia-Marcos, P.S. Kietrsunthorn, Y. Pavlova, M.A. Adia, P. Ghosh, and M.G. Farquhar Functional characterization of the guanine nucleotide exchange factor (GEF) motif of GIV protein reveals a threshold effect in signaling Proc Natl Acad Sci USA 109 2012 1961 1966
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 1961-1966
    • Garcia-Marcos, M.1    Kietrsunthorn, P.S.2    Pavlova, Y.3    Adia, M.A.4    Ghosh, P.5    Farquhar, M.G.6
  • 139
    • 85046980000 scopus 로고    scopus 로고
    • GIV/Girdin is a rheostat that fine-tunes growth factor signals during tumor progression
    • P. Ghosh, M. Garcia-Marcos, and M.G. Farquhar GIV/Girdin is a rheostat that fine-tunes growth factor signals during tumor progression Cell Adh Migr 5 2011 237 248
    • (2011) Cell Adh Migr , vol.5 , pp. 237-248
    • Ghosh, P.1    Garcia-Marcos, M.2    Farquhar, M.G.3
  • 140
    • 60549097417 scopus 로고    scopus 로고
    • The cationic region of Rhes mediates its interactions with specific Gbeta subunits
    • C. Hill, A. Goddard, G. Ladds, and J. Davey The cationic region of Rhes mediates its interactions with specific Gbeta subunits Cell Physiol Biochem 23 2009 1 8
    • (2009) Cell Physiol Biochem , vol.23 , pp. 1-8
    • Hill, C.1    Goddard, A.2    Ladds, G.3    Davey, J.4
  • 141
    • 0842286707 scopus 로고    scopus 로고
    • The small GTP-binding protein, Rhes, regulates signal transduction from G protein-coupled receptors
    • P. Vargiu, R. De Abajo, J.A. Garcia-Ranea, A. Valencia, P. Santisteban, and P. Crespo The small GTP-binding protein, Rhes, regulates signal transduction from G protein-coupled receptors Oncogene 23 2004 559 568
    • (2004) Oncogene , vol.23 , pp. 559-568
    • Vargiu, P.1    De Abajo, R.2    Garcia-Ranea, J.A.3    Valencia, A.4    Santisteban, P.5    Crespo, P.6
  • 142
    • 0037192796 scopus 로고    scopus 로고
    • Dexras1/AGS-1 inhibits signal transduction from the Gi-coupled formyl peptide receptor to Erk-1/2 MAP kinases
    • T.E. Graham, E.R. Prossnitz, and R.I. Dorin Dexras1/AGS-1 inhibits signal transduction from the Gi-coupled formyl peptide receptor to Erk-1/2 MAP kinases J Biol Chem 277 2002 10876 10882
    • (2002) J Biol Chem , vol.277 , pp. 10876-10882
    • Graham, T.E.1    Prossnitz, E.R.2    Dorin, R.I.3
  • 144
    • 79954503153 scopus 로고    scopus 로고
    • Rhes and AGS1/Dexras1 affect signaling by dopamine D1 receptors through adenylyl cyclase
    • L.M. Harrison, and Y. He Rhes and AGS1/Dexras1 affect signaling by dopamine D1 receptors through adenylyl cyclase J Neurosci Res 89 2011 874 882
    • (2011) J Neurosci Res , vol.89 , pp. 874-882
    • Harrison, L.M.1    He, Y.2
  • 145
    • 27144449951 scopus 로고    scopus 로고
    • Specific in vivo binding of activator of G protein signaling 1 to the Gbeta1 subunit
    • R. Hiskens, M. Vatish, C. Hill, J. Davey, and G. Ladds Specific in vivo binding of activator of G protein signaling 1 to the Gbeta1 subunit Biochem Biophys Res Commun 337 2005 1038 1046
    • (2005) Biochem Biophys Res Commun , vol.337 , pp. 1038-1046
    • Hiskens, R.1    Vatish, M.2    Hill, C.3    Davey, J.4    Ladds, G.5
  • 146
    • 0033634643 scopus 로고    scopus 로고
    • Dexras1: A G protein specifically coupled to neuronal nitric oxide synthase via CAPON
    • M. Fang, S.R. Jaffrey, A. Sawa, K. Ye, X. Luo, and S.H. Snyder Dexras1: a G protein specifically coupled to neuronal nitric oxide synthase via CAPON Neuron 28 2000 183 193
    • (2000) Neuron , vol.28 , pp. 183-193
    • Fang, M.1    Jaffrey, S.R.2    Sawa, A.3    Ye, K.4    Luo, X.5    Snyder, S.H.6
  • 147
    • 84863096119 scopus 로고    scopus 로고
    • Striatum specific protein, Rhes regulates AKT pathway
    • S. Bang, C. Steenstra, and S.F. Kim Striatum specific protein, Rhes regulates AKT pathway Neurosci Lett 521 2012 142 147
    • (2012) Neurosci Lett , vol.521 , pp. 142-147
    • Bang, S.1    Steenstra, C.2    Kim, S.F.3
  • 148
    • 19744364926 scopus 로고    scopus 로고
    • Dexras1 blocks receptor-mediated heterologous sensitization of adenylyl cyclase 1
    • C.H. Nguyen, and V.J. Watts Dexras1 blocks receptor-mediated heterologous sensitization of adenylyl cyclase 1 Biochem Biophys Res Commun 332 2005 913 920
    • (2005) Biochem Biophys Res Commun , vol.332 , pp. 913-920
    • Nguyen, C.H.1    Watts, V.J.2
  • 149
    • 0037134434 scopus 로고    scopus 로고
    • Activator of G-protein signaling 1 blocks GIRK channel activation by a G-protein-coupled receptor: Apparent disruption of receptor signaling complexes
    • A. Takesono, M.W. Nowak, M. Cismowski, E. Duzic, and S.M. Lanier Activator of G-protein signaling 1 blocks GIRK channel activation by a G-protein-coupled receptor: apparent disruption of receptor signaling complexes J Biol Chem 277 2002 13827 13830
    • (2002) J Biol Chem , vol.277 , pp. 13827-13830
    • Takesono, A.1    Nowak, M.W.2    Cismowski, M.3    Duzic, E.4    Lanier, S.M.5
  • 150
    • 57349084180 scopus 로고    scopus 로고
    • The monomeric G proteins AGS1 and Rhes selectively influence Galphai-dependent signaling to modulate N-type (CaV2.2) calcium channels
    • A. Thapliyal, R.A. Bannister, C. Hanks, and B.A. Adams The monomeric G proteins AGS1 and Rhes selectively influence Galphai-dependent signaling to modulate N-type (CaV2.2) calcium channels Am J Physiol Cell Physiol 295 2008 C1417 C1426
    • (2008) Am J Physiol Cell Physiol , vol.295
    • Thapliyal, A.1    Bannister, R.A.2    Hanks, C.3    Adams, B.A.4
  • 152
    • 5444260164 scopus 로고    scopus 로고
    • RIC-8 is required for GPR-1/2-dependent Galpha function during asymmetric division of C. elegans embryos
    • K. Afshar, F.S. Willard, K. Colombo, C.A. Johnston, C.R. McCudden, and D.P. Siderovski RIC-8 is required for GPR-1/2-dependent Galpha function during asymmetric division of C. elegans embryos Cell 119 2004 219 230
    • (2004) Cell , vol.119 , pp. 219-230
    • Afshar, K.1    Willard, F.S.2    Colombo, K.3    Johnston, C.A.4    McCudden, C.R.5    Siderovski, D.P.6
  • 153
    • 6944256893 scopus 로고    scopus 로고
    • Control of embryonic spindle positioning and Galpha activity by C. elegans RIC-8
    • C. Couwenbergs, A.C. Spilker, and M. Gotta Control of embryonic spindle positioning and Galpha activity by C. elegans RIC-8 Curr Biol 14 2004 1871 1876
    • (2004) Curr Biol , vol.14 , pp. 1871-1876
    • Couwenbergs, C.1    Spilker, A.C.2    Gotta, M.3
  • 154
    • 27844524595 scopus 로고    scopus 로고
    • Drosophila Ric-8 regulates Galphai cortical localization to promote Galphai-dependent planar orientation of the mitotic spindle during asymmetric cell division
    • N.B. David, C.A. Martin, M. Segalen, F. Rosenfeld, F. Schweisguth, and Y. Bellaiche Drosophila Ric-8 regulates Galphai cortical localization to promote Galphai-dependent planar orientation of the mitotic spindle during asymmetric cell division Nat Cell Biol 7 2005 1083 1090
    • (2005) Nat Cell Biol , vol.7 , pp. 1083-1090
    • David, N.B.1    Martin, C.A.2    Segalen, M.3    Rosenfeld, F.4    Schweisguth, F.5    Bellaiche, Y.6
  • 155
    • 28044435388 scopus 로고    scopus 로고
    • Resistance to inhibitors of cholinesterase 8A catalyzes release of Galphai-GTP and nuclear mitotic apparatus protein (NuMA) from NuMA/LGN/Galphai-GDP complexes
    • G.G. Tall, and A.G. Gilman Resistance to inhibitors of cholinesterase 8A catalyzes release of Galphai-GTP and nuclear mitotic apparatus protein (NuMA) from NuMA/LGN/Galphai-GDP complexes Proc Natl Acad Sci USA 102 2005 16584 16589
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 16584-16589
    • Tall, G.G.1    Gilman, A.G.2
  • 156
    • 79952093818 scopus 로고    scopus 로고
    • Activation of the regulator of G protein signaling 14-Galphai1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A
    • C.P. Vellano, F.J. Shu, S. Ramineni, C.K. Yates, G.G. Tall, and J.R. Hepler Activation of the regulator of G protein signaling 14-Galphai1-GDP signaling complex is regulated by resistance to inhibitors of cholinesterase-8A Biochemistry 50 2011 752 762
    • (2011) Biochemistry , vol.50 , pp. 752-762
    • Vellano, C.P.1    Shu, F.J.2    Ramineni, S.3    Yates, C.K.4    Tall, G.G.5    Hepler, J.R.6
  • 157
    • 0035209331 scopus 로고    scopus 로고
    • RGS14 is a bifunctional regulator of Galphai/o activity that exists in multiple populations in brain
    • S. Hollinger, J.B. Taylor, E.H. Goldman, and J.R. Hepler RGS14 is a bifunctional regulator of Galphai/o activity that exists in multiple populations in brain J Neurochem 79 2001 941 949
    • (2001) J Neurochem , vol.79 , pp. 941-949
    • Hollinger, S.1    Taylor, J.B.2    Goldman, E.H.3    Hepler, J.R.4


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