메뉴 건너뛰기




Volumn 366, Issue 2, 2007, Pages 349-365

How Regulators of G Protein Signaling Achieve Selective Regulation

Author keywords

domain; G protein coupled receptor; GTPase; RGS; selectivity

Indexed keywords

CALCIUM CHANNEL; CELL PROTEIN; DOPAMINE 2 RECEPTOR; G PROTEIN COUPLED RECEPTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE TRIPHOSPHATASE; ION CHANNEL; MESSENGER RNA; PROTEIN SUBUNIT; REGULATOR PROTEIN; RGS PROTEIN; RGS2 PROTEIN; RGS4 PROTEIN; SCAFFOLD PROTEIN;

EID: 33846376810     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2006.11.045     Document Type: Review
Times cited : (92)

References (164)
  • 2
    • 0025373974 scopus 로고
    • Ionic channels and their regulation by G protein subunits
    • Brown A.M., and Birnbaumer L. Ionic channels and their regulation by G protein subunits. Annu. Rev. Physiol. 52 (1990) 197-213
    • (1990) Annu. Rev. Physiol. , vol.52 , pp. 197-213
    • Brown, A.M.1    Birnbaumer, L.2
  • 3
    • 0033783132 scopus 로고    scopus 로고
    • GTPase-activating proteins for heterotrimeric G proteins: regulators of G protein signaling (RGS) and RGS-like proteins
    • Ross E.M., and Wilkie T.M. 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
  • 5
    • 0036490096 scopus 로고    scopus 로고
    • Regulators of G-protein signalling as new central nervous system drug targets
    • Neubig R.R., and Siderovski D.P. Regulators of G-protein signalling as new central nervous system drug targets. Nature Rev. Drug Discov. 1 (2002) 187-197
    • (2002) Nature Rev. Drug Discov. , vol.1 , pp. 187-197
    • Neubig, R.R.1    Siderovski, D.P.2
  • 6
    • 25444528729 scopus 로고    scopus 로고
    • The GAPs, GEFs, and GDIs of heterotrimeric G-protein alpha subunits
    • Siderovski D.P., and Willard F.S. 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
  • 8
    • 0034724508 scopus 로고    scopus 로고
    • Genomic characterization of the human heterotrimeric G protein α, β, and γ subunit genes
    • Hurowitz E.H., Melnyk J.M., Chen Y.J., Kouros-Mehr H., Simon M.I., and Shizuya H. Genomic characterization of the human heterotrimeric G protein α, β, and γ subunit genes. DNA Res. 7 (2000) 111-120
    • (2000) DNA Res. , vol.7 , pp. 111-120
    • Hurowitz, E.H.1    Melnyk, J.M.2    Chen, Y.J.3    Kouros-Mehr, H.4    Simon, M.I.5    Shizuya, H.6
  • 10
    • 0030029727 scopus 로고    scopus 로고
    • Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family
    • Druey K.M., Blumer K.J., Kang V.H., and Kehrl J.H. Inhibition of G-protein-mediated MAP kinase activation by a new mammalian gene family. Nature 379 (1996) 742-746
    • (1996) Nature , vol.379 , pp. 742-746
    • Druey, K.M.1    Blumer, K.J.2    Kang, V.H.3    Kehrl, J.H.4
  • 11
    • 0029808079 scopus 로고    scopus 로고
    • RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits
    • Watson N., Linder M.E., Druey K.M., Kehrl J.H., and Blumer K.J. RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits. Nature 383 (1996) 172-175
    • (1996) Nature , vol.383 , pp. 172-175
    • Watson, N.1    Linder, M.E.2    Druey, K.M.3    Kehrl, J.H.4    Blumer, K.J.5
  • 12
    • 0034598728 scopus 로고    scopus 로고
    • Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1
    • Chen C.K., Burns M.E., He W., Wensel T.G., Baylor D.A., and Simon M.I. Slowed recovery of rod photoresponse in mice lacking the GTPase accelerating protein RGS9-1. Nature 403 (2000) 557-560
    • (2000) Nature , vol.403 , pp. 557-560
    • Chen, C.K.1    Burns, M.E.2    He, W.3    Wensel, T.G.4    Baylor, D.A.5    Simon, M.I.6
  • 15
    • 0029559788 scopus 로고
    • GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain
    • De Vries L., Mousli M., Wurmser A., and Farquhar M.G. GAIP, a protein that specifically interacts with the trimeric G protein Gαi3, is a member of a protein family with a highly conserved core domain. Proc. Natl Acad. Sci. USA 92 (1995) 11916-11920
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 11916-11920
    • De Vries, L.1    Mousli, M.2    Wurmser, A.3    Farquhar, M.G.4
  • 16
    • 0030032001 scopus 로고    scopus 로고
    • EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins
    • Koelle M.R., and Horvitz H.R. EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84 (1996) 115-125
    • (1996) Cell , vol.84 , pp. 115-125
    • Koelle, M.R.1    Horvitz, H.R.2
  • 17
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein α subunits
    • Berman D.M., Wilkie T.M., and Gilman A.G. GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein α 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
  • 18
    • 0031017573 scopus 로고    scopus 로고
    • RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα
    • Hepler J.R., Berman D.M., Gilman A.G., and Kozasa T. RGS4 and GAIP are GTPase-activating proteins for Gqα and block activation of phospholipase Cβ by γ-thio-GTP-Gqα. 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
  • 19
    • 0030610240 scopus 로고    scopus 로고
    • Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells
    • Huang C., Hepler J.R., Gilman A.G., and Mumby S.M. Attenuation of Gi- and Gq-mediated signaling by expression of RGS4 or GAIP in mammalian cells. Proc. Natl Acad. Sci. USA 94 (1997) 6159-6163
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 6159-6163
    • Huang, C.1    Hepler, J.R.2    Gilman, A.G.3    Mumby, S.M.4
  • 20
    • 1842861706 scopus 로고    scopus 로고
    • Differential effects of regulator of G protein signaling (RGS) proteins on serotonin 5-HT1A, 5-HT2A, and dopamine D2 receptor-mediated signaling and adenylyl cyclase activity
    • Ghavami A., Hunt R.A., Olsen M.A., Zhang J., Smith D.L., Kalgaonkar S., et al. Differential effects of regulator of G protein signaling (RGS) proteins on serotonin 5-HT1A, 5-HT2A, and dopamine D2 receptor-mediated signaling and adenylyl cyclase activity. Cell Signal. 16 (2004) 711-721
    • (2004) Cell Signal. , vol.16 , pp. 711-721
    • Ghavami, A.1    Hunt, R.A.2    Olsen, M.A.3    Zhang, J.4    Smith, D.L.5    Kalgaonkar, S.6
  • 22
    • 0038193543 scopus 로고    scopus 로고
    • RGS6, RGS7, RGS9, and RGS11 stimulate GTPase activity of Gi family G-proteins with differential selectivity and maximal activity
    • Hooks S.B., Waldo G.L., Corbitt J., Bodor E.T., Krumins A.M., and Harden T.K. RGS6, RGS7, RGS9, and RGS11 stimulate GTPase activity of Gi family G-proteins with differential selectivity and maximal activity. J. Biol. Chem. 278 (2003) 10087-10093
    • (2003) J. Biol. Chem. , vol.278 , pp. 10087-10093
    • Hooks, S.B.1    Waldo, G.L.2    Corbitt, J.3    Bodor, E.T.4    Krumins, A.M.5    Harden, T.K.6
  • 23
    • 0033524915 scopus 로고    scopus 로고
    • RGS proteins determine signaling specificity of Gq-coupled receptors
    • Xu X., Zeng W., Popov S., Berman D.M., Davignon I., Yu K., et al. 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
  • 24
    • 0032575557 scopus 로고    scopus 로고
    • A possible role of RGS9 in phototransduction. A bridge between the cGMP-phosphodiesterase system and the guanylyl cyclase system
    • Seno K., Kishigami A., Ihara S., Maeda T., Bondarenko V.A., Nishizawa Y., et al. A possible role of RGS9 in phototransduction. A bridge between the cGMP-phosphodiesterase system and the guanylyl cyclase system. J. Biol. Chem. 273 (1998) 22169-22172
    • (1998) J. Biol. Chem. , vol.273 , pp. 22169-22172
    • Seno, K.1    Kishigami, A.2    Ihara, S.3    Maeda, T.4    Bondarenko, V.A.5    Nishizawa, Y.6
  • 25
    • 0033559843 scopus 로고    scopus 로고
    • Cloning and characterization of RGS9-2: a striatal-enriched alternatively spliced product of the RGS9 gene
    • Rahman Z., Gold S.J., Potenza M.N., Cowan C.W., Ni Y.G., He W., et al. Cloning and characterization of RGS9-2: a striatal-enriched alternatively spliced product of the RGS9 gene. J. Neurosci. 19 (1999) 2016-2026
    • (1999) J. Neurosci. , vol.19 , pp. 2016-2026
    • Rahman, Z.1    Gold, S.J.2    Potenza, M.N.3    Cowan, C.W.4    Ni, Y.G.5    He, W.6
  • 28
    • 20044362374 scopus 로고    scopus 로고
    • D2 dopamine receptors colocalize regulator of G-protein signaling 9-2 (RGS9-2) via the RGS9 DEP domain, and RGS9 knock-out mice develop dyskinesias associated with dopamine pathways
    • Kovoor A., Seyffarth P., Ebert J., Barghshoon S., Chen C.K., Schwarz S., et al. D2 dopamine receptors colocalize regulator of G-protein signaling 9-2 (RGS9-2) via the RGS9 DEP domain, and RGS9 knock-out mice develop dyskinesias associated with dopamine pathways. J. Neurosci. 25 (2005) 2157-2165
    • (2005) J. Neurosci. , vol.25 , pp. 2157-2165
    • Kovoor, A.1    Seyffarth, P.2    Ebert, J.3    Barghshoon, S.4    Chen, C.K.5    Schwarz, S.6
  • 29
    • 11144258839 scopus 로고    scopus 로고
    • RGS-Rz and RGS9-2 proteins control mu-opioid receptor desensitisation in CNS: the role of activated Gαz subunits
    • Sanchez-Blazquez P., Rodriguez-Munoz M., Montero C., and Garzon J. RGS-Rz and RGS9-2 proteins control mu-opioid receptor desensitisation in CNS: the role of activated Gαz subunits. Neuropharmacology 48 (2005) 134-150
    • (2005) Neuropharmacology , vol.48 , pp. 134-150
    • Sanchez-Blazquez, P.1    Rodriguez-Munoz, M.2    Montero, C.3    Garzon, J.4
  • 30
    • 15744387869 scopus 로고    scopus 로고
    • Activation of μ-opioid receptors transfers control of Gα subunits to the regulator of G-protein signaling RGS9-2: role in receptor desensitization
    • Garzon J., Rodriguez-Munoz M., Lopez-Fando A., and Sanchez-Blazquez P. Activation of μ-opioid receptors transfers control of Gα subunits to the regulator of G-protein signaling RGS9-2: role in receptor desensitization. J. Biol. Chem. 280 (2005) 8951-8960
    • (2005) J. Biol. Chem. , vol.280 , pp. 8951-8960
    • Garzon, J.1    Rodriguez-Munoz, M.2    Lopez-Fando, A.3    Sanchez-Blazquez, P.4
  • 31
    • 19244367478 scopus 로고    scopus 로고
    • The R7 subfamily of RGS proteins assists tachyphylaxis and acute tolerance at mu-opioid receptors
    • Garzon J., Lopez-Fando A., and Sanchez-Blazquez P. The R7 subfamily of RGS proteins assists tachyphylaxis and acute tolerance at mu-opioid receptors. Neuropsychopharmacology 28 (2003) 1983-1990
    • (2003) Neuropsychopharmacology , vol.28 , pp. 1983-1990
    • Garzon, J.1    Lopez-Fando, A.2    Sanchez-Blazquez, P.3
  • 32
    • 0034894077 scopus 로고    scopus 로고
    • Differential capacities of the RGS1, RGS16 and RGS-GAIP regulators of G protein signaling to enhance α2A-adrenoreceptor agonist-stimulated GTPase activity of Go1α
    • Hoffmann M., Ward R.J., Cavalli A., Carr I.C., and Milligan G. Differential capacities of the RGS1, RGS16 and RGS-GAIP regulators of G protein signaling to enhance α2A-adrenoreceptor agonist-stimulated GTPase activity of Go1α. J. Neurochem. 78 (2001) 797-806
    • (2001) J. Neurochem. , vol.78 , pp. 797-806
    • Hoffmann, M.1    Ward, R.J.2    Cavalli, A.3    Carr, I.C.4    Milligan, G.5
  • 33
    • 33747037013 scopus 로고    scopus 로고
    • RGS2 is upregulated by and attenuates the hypertrophic effect of α1-adrenergic activation in cultured ventricular myocytes
    • Zou M.X., Roy A.A., Zhao Q., Kirshenbaum L.A., Karmazyn M., and Chidiac P. RGS2 is upregulated by and attenuates the hypertrophic effect of α1-adrenergic activation in cultured ventricular myocytes. Cell Signal. 18 (2006) 1655-1663
    • (2006) Cell Signal. , vol.18 , pp. 1655-1663
    • Zou, M.X.1    Roy, A.A.2    Zhao, Q.3    Kirshenbaum, L.A.4    Karmazyn, M.5    Chidiac, P.6
  • 34
    • 33746843994 scopus 로고    scopus 로고
    • Regulation of cardiomyocyte signaling by RGS proteins: differential selectivity towards G proteins and susceptibility to regulation
    • Hao J., Michalek C., Zhang W., Zhu M., Xu X., and Mende U. Regulation of cardiomyocyte signaling by RGS proteins: differential selectivity towards G proteins and susceptibility to regulation. J. Mol. Cell. Cardiol. 41 (2006) 51-61
    • (2006) J. Mol. Cell. Cardiol. , vol.41 , pp. 51-61
    • Hao, J.1    Michalek, C.2    Zhang, W.3    Zhu, M.4    Xu, X.5    Mende, U.6
  • 35
    • 33646842745 scopus 로고    scopus 로고
    • Selective loss of fine tuning of Gq/11 signaling by RGS2 protein exacerbates cardiomyocyte hypertrophy
    • Zhang W., Anger T., Su J., Hao J., Xu X., Zhu M., et al. Selective loss of fine tuning of Gq/11 signaling by RGS2 protein exacerbates cardiomyocyte hypertrophy. J. Biol. Chem. 281 (2006) 5811-5820
    • (2006) J. Biol. Chem. , vol.281 , pp. 5811-5820
    • Zhang, W.1    Anger, T.2    Su, J.3    Hao, J.4    Xu, X.5    Zhu, M.6
  • 36
    • 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
    • Wang Q., Liu M., Mullah B., Siderovski D.P., and Neubig R.R. 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
  • 37
    • 27144543208 scopus 로고    scopus 로고
    • N-terminally truncated variant of the mouse GAIP/RGS19 lacks selectivity of full-length GAIP/RGS19 protein in regulating ORL1 receptor signaling
    • Xie G.X., Yanagisawa Y., Ito E., Maruyama K., Han X., Kim K.J., et al. N-terminally truncated variant of the mouse GAIP/RGS19 lacks selectivity of full-length GAIP/RGS19 protein in regulating ORL1 receptor signaling. J. Mol. Biol. 353 (2005) 1081-1092
    • (2005) J. Mol. Biol. , vol.353 , pp. 1081-1092
    • Xie, G.X.1    Yanagisawa, Y.2    Ito, E.3    Maruyama, K.4    Han, X.5    Kim, K.J.6
  • 38
    • 0037295354 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase 6 (GRK6) selectively regulates endogenous secretin receptor responsiveness in NG108-15 cells
    • Ghadessy R.S., Willets J.M., and Kelly E. G protein-coupled receptor kinase 6 (GRK6) selectively regulates endogenous secretin receptor responsiveness in NG108-15 cells. Br. J. Pharmacol. 138 (2003) 660-670
    • (2003) Br. J. Pharmacol. , vol.138 , pp. 660-670
    • Ghadessy, R.S.1    Willets, J.M.2    Kelly, E.3
  • 39
    • 0142148103 scopus 로고    scopus 로고
    • Specificity of G protein-coupled receptor kinase 6-mediated phosphorylation and regulation of single-cell m3 muscarinic acetylcholine receptor signaling
    • Willets J.M., Mistry R., Nahorski S.R., and Challiss R.A. Specificity of G protein-coupled receptor kinase 6-mediated phosphorylation and regulation of single-cell m3 muscarinic acetylcholine receptor signaling. Mol. Pharmacol. 64 (2003) 1059-1068
    • (2003) Mol. Pharmacol. , vol.64 , pp. 1059-1068
    • Willets, J.M.1    Mistry, R.2    Nahorski, S.R.3    Challiss, R.A.4
  • 41
    • 0030013246 scopus 로고    scopus 로고
    • G protein-coupled receptor kinase specificity for phosphorylation and desensitization of α2-adrenergic receptor subtypes
    • Jewell-Motz E.A., and Liggett S.B. G protein-coupled receptor kinase specificity for phosphorylation and desensitization of α2-adrenergic receptor subtypes. J. Biol. Chem. 271 (1996) 18082-18087
    • (1996) J. Biol. Chem. , vol.271 , pp. 18082-18087
    • Jewell-Motz, E.A.1    Liggett, S.B.2
  • 42
    • 0033607326 scopus 로고    scopus 로고
    • Selective regulation of Gαq/11 by an RGS domain in the G protein-coupled receptor kinase, GRK2
    • Carman C.V., Parent J.L., Day P.W., Pronin A.N., Sternweis P.M., Wedegaertner P.B., et al. Selective regulation of Gαq/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
  • 43
    • 0035976614 scopus 로고    scopus 로고
    • RGS-PX1, a GAP for Gαs and sorting nexin in vesicular trafficking
    • Zheng B., Ma Y.C., Ostrom R.S., Lavoie C., Gill G.N., Insel P.A., et al. RGS-PX1, a GAP for Gαs and sorting nexin in vesicular trafficking. Science 294 (2001) 1939-1942
    • (2001) Science , vol.294 , pp. 1939-1942
    • Zheng, B.1    Ma, Y.C.2    Ostrom, R.S.3    Lavoie, C.4    Gill, G.N.5    Insel, P.A.6
  • 44
    • 9444263165 scopus 로고    scopus 로고
    • Regulation of epidermal growth factor receptor degradation by heterotrimeric Gαs protein
    • Zheng B., Lavoie C., Tang T.D., Ma P., Meerloo T., Beas A., and Farquhar M.G. Regulation of epidermal growth factor receptor degradation by heterotrimeric Gαs protein. Mol. Biol. Cell. 15 (2004) 5538-5550
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 5538-5550
    • Zheng, B.1    Lavoie, C.2    Tang, T.D.3    Ma, P.4    Meerloo, T.5    Beas, A.6    Farquhar, M.G.7
  • 48
    • 12244309566 scopus 로고    scopus 로고
    • Gating properties of GIRK channels activated by Gαo- and Gαi-coupled muscarinic m2 receptors in Xenopus oocytes: the role of receptor precoupling in RGS modulation
    • Zhang Q., Pacheco M.A., and Doupnik C.A. Gating properties of GIRK channels activated by Gαo- and Gαi-coupled muscarinic m2 receptors in Xenopus oocytes: the role of receptor precoupling in RGS modulation. J. Physiol. 545 (2002) 355-373
    • (2002) J. Physiol. , vol.545 , pp. 355-373
    • Zhang, Q.1    Pacheco, M.A.2    Doupnik, C.A.3
  • 49
    • 0034730395 scopus 로고    scopus 로고
    • Changes in GIRK1/GIRK2 deactivation kinetics and basal activity in the presence and absence of RGS4
    • Ulens C., Daenens P., and Tytgat J. Changes in GIRK1/GIRK2 deactivation kinetics and basal activity in the presence and absence of RGS4. Life Sci. 67 (2000) 2305-2317
    • (2000) Life Sci. , vol.67 , pp. 2305-2317
    • Ulens, C.1    Daenens, P.2    Tytgat, J.3
  • 50
    • 0037031844 scopus 로고    scopus 로고
    • N-terminal tyrosine residues within the potassium channel Kir3 modulate GTPase activity of Gαi
    • Ippolito D.L., Temkin P.A., Rogalski S.L., and Chavkin C. N-terminal tyrosine residues within the potassium channel Kir3 modulate GTPase activity of Gαi. J. Biol. Chem. 277 (2002) 32692-32696
    • (2002) J. Biol. Chem. , vol.277 , pp. 32692-32696
    • Ippolito, D.L.1    Temkin, P.A.2    Rogalski, S.L.3    Chavkin, C.4
  • 51
    • 0035880976 scopus 로고    scopus 로고
    • Interaction between the RGS domain of RGS4 with G protein α subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel
    • Inanobe A., Fujita S., Makino Y., Matsushita K., Ishii M., Chachin M., and Kurachi Y. Interaction between the RGS domain of RGS4 with G protein α subunits mediates the voltage-dependent relaxation of the G protein-gated potassium channel. J. Physiol. 535 (2001) 133-143
    • (2001) J. Physiol. , vol.535 , pp. 133-143
    • Inanobe, A.1    Fujita, S.2    Makino, Y.3    Matsushita, K.4    Ishii, M.5    Chachin, M.6    Kurachi, Y.7
  • 52
    • 23844534545 scopus 로고    scopus 로고
    • Neuronal Kir3.1/Kir3.2a channels coupled to serotonin 1A and muscarinic m2 receptors are differentially modulated by the "short" RGS3 isoform
    • Jaen C., and Doupnik C.A. Neuronal Kir3.1/Kir3.2a channels coupled to serotonin 1A and muscarinic m2 receptors are differentially modulated by the "short" RGS3 isoform. Neuropharmacology 49 (2005) 465-476
    • (2005) Neuropharmacology , vol.49 , pp. 465-476
    • Jaen, C.1    Doupnik, C.A.2
  • 53
    • 0033151730 scopus 로고    scopus 로고
    • New roles for RGS2, 5 and 8 on the ratio-dependent modulation of recombinant GIRK channels expressed in Xenopus oocytes
    • Herlitze S., Ruppersberg J.P., and Mark M.D. New roles for RGS2, 5 and 8 on the ratio-dependent modulation of recombinant GIRK channels expressed in Xenopus oocytes. J. Physiol. 517 (1999) 341-352
    • (1999) J. Physiol. , vol.517 , pp. 341-352
    • Herlitze, S.1    Ruppersberg, J.P.2    Mark, M.D.3
  • 56
    • 0035871046 scopus 로고    scopus 로고
    • 2+ channels reconstituted in a human cell line
    • 2+ channels reconstituted in a human cell line. J. Physiol. 532 (2001) 337-347
    • (2001) J. Physiol. , vol.532 , pp. 337-347
    • Melliti, K.1    Meza, U.2    Adams, B.A.3
  • 59
    • 0034306154 scopus 로고    scopus 로고
    • G protein modulation of recombinant P/Q-type calcium channels by regulators of G protein signalling proteins
    • Mark M.D., Wittemann S., and Herlitze S. G protein modulation of recombinant P/Q-type calcium channels by regulators of G protein signalling proteins. J. Physiol. 528 (2000) 65-77
    • (2000) J. Physiol. , vol.528 , pp. 65-77
    • Mark, M.D.1    Wittemann, S.2    Herlitze, S.3
  • 61
    • 0034619893 scopus 로고    scopus 로고
    • Tyrosine-kinase-dependent recruitment of RGS12 to the N-type calcium channel
    • Schiff M.L., Siderovski D.P., Jordan J.D., Brothers G., Snow B., De Vries L., et al. Tyrosine-kinase-dependent recruitment of RGS12 to the N-type calcium channel. Nature 408 (2000) 723-727
    • (2000) Nature , vol.408 , pp. 723-727
    • Schiff, M.L.1    Siderovski, D.P.2    Jordan, J.D.3    Brothers, G.4    Snow, B.5    De Vries, L.6
  • 63
    • 0034307596 scopus 로고    scopus 로고
    • Selective regulation of N-type Ca channels by different combinations of G-protein β/γ subunits and RGS proteins
    • Zhou J.Y., Siderovski D.P., and Miller R.J. Selective regulation of N-type Ca channels by different combinations of G-protein β/γ subunits and RGS proteins. J. Neurosci. 20 (2000) 7143-7148
    • (2000) J. Neurosci. , vol.20 , pp. 7143-7148
    • Zhou, J.Y.1    Siderovski, D.P.2    Miller, R.J.3
  • 64
    • 0031710927 scopus 로고    scopus 로고
    • RGS-GAIP, a GTPase-activating protein for Gαi heterotrimeric G proteins, is located on clathrin-coated vesicles
    • De Vries L., Elenko E., McCaffery J.M., Fischer T., Hubler L., McQuistan T., et al. RGS-GAIP, a GTPase-activating protein for Gαi heterotrimeric G proteins, is located on clathrin-coated vesicles. Mol. Biol. Cell. 9 (1998) 1123-1134
    • (1998) Mol. Biol. Cell. , vol.9 , pp. 1123-1134
    • De Vries, L.1    Elenko, E.2    McCaffery, J.M.3    Fischer, T.4    Hubler, L.5    McQuistan, T.6
  • 66
    • 0034635999 scopus 로고    scopus 로고
    • Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles
    • Fischer T., Elenko E., Wan L., Thomas G., and Farquhar M.G. Membrane-associated GAIP is a phosphoprotein and can be phosphorylated by clathrin-coated vesicles. Proc. Natl Acad. Sci. USA 97 (2000) 4040-4045
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 4040-4045
    • Fischer, T.1    Elenko, E.2    Wan, L.3    Thomas, G.4    Farquhar, M.G.5
  • 67
  • 68
    • 0038444235 scopus 로고    scopus 로고
    • GAIP participates in budding of membrane carriers at the trans-Golgi network
    • Wylie F.G., Lock J.G., Jamriska L., Khromykh T., Brown D.L., and Stow J.L. GAIP participates in budding of membrane carriers at the trans-Golgi network. Traffic 4 (2003) 175-189
    • (2003) Traffic , vol.4 , pp. 175-189
    • Wylie, F.G.1    Lock, J.G.2    Jamriska, L.3    Khromykh, T.4    Brown, D.L.5    Stow, J.L.6
  • 69
    • 0036009682 scopus 로고    scopus 로고
    • GAIP, GIPC and Gαi3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function
    • Lou X., McQuistan T., Orlando R.A., and Farquhar M.G. GAIP, GIPC and Gαi3 are concentrated in endocytic compartments of proximal tubule cells: putative role in regulating megalin's function. J. Am. Soc. Nephrol. 13 (2002) 918-927
    • (2002) J. Am. Soc. Nephrol. , vol.13 , pp. 918-927
    • Lou, X.1    McQuistan, T.2    Orlando, R.A.3    Farquhar, M.G.4
  • 70
    • 5444259457 scopus 로고    scopus 로고
    • RGS-7 completes a receptor-independent heterotrimeric G protein cycle to asymmetrically regulate mitotic spindle positioning in C. elegans
    • Hess H.A., Roper J.C., Grill S.W., and Koelle M.R. RGS-7 completes a receptor-independent heterotrimeric G protein cycle to asymmetrically regulate mitotic spindle positioning in C. elegans. Cell 119 (2004) 209-218
    • (2004) Cell , vol.119 , pp. 209-218
    • Hess, H.A.1    Roper, J.C.2    Grill, S.W.3    Koelle, M.R.4
  • 73
    • 28044435388 scopus 로고    scopus 로고
    • Resistance to inhibitors of cholinesterase 8A catalyzes release of Gαi-GTP and nuclear mitotic apparatus protein (NuMA) from NuMA/LGN/Gαi-GDP complexes
    • Tall G.G., and Gilman A.G. Resistance to inhibitors of cholinesterase 8A catalyzes release of Gαi-GTP and nuclear mitotic apparatus protein (NuMA) from NuMA/LGN/Gαi-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
  • 74
    • 27144525489 scopus 로고    scopus 로고
    • New roles for Gα and RGS proteins: communication continues despite pulling sisters apart
    • Wilkie T.M., and Kinch L. New roles for Gα and RGS proteins: communication continues despite pulling sisters apart. Curr. Biol. 15 (2005) R843-R854
    • (2005) Curr. Biol. , vol.15
    • Wilkie, T.M.1    Kinch, L.2
  • 75
    • 0031936503 scopus 로고    scopus 로고
    • RGS9, a GTPase accelerator for phototransduction
    • He W., Cowan C.W., and Wensel T.G. RGS9, a GTPase accelerator for phototransduction. Neuron 20 (1998) 95-102
    • (1998) Neuron , vol.20 , pp. 95-102
    • He, W.1    Cowan, C.W.2    Wensel, T.G.3
  • 76
    • 0032574719 scopus 로고    scopus 로고
    • High expression levels in cones of RGS9, the predominant GTPase accelerating protein of rods
    • Cowan C.W., Fariss R.N., Sokal I., Palczewski K., and Wensel T.G. High expression levels in cones of RGS9, the predominant GTPase accelerating protein of rods. Proc. Natl Acad. Sci. USA 95 (1998) 5351-5356
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5351-5356
    • Cowan, C.W.1    Fariss, R.N.2    Sokal, I.3    Palczewski, K.4    Wensel, T.G.5
  • 77
    • 0034817403 scopus 로고    scopus 로고
    • Inhibition of retinal guanylyl cyclase by the RGS9-1 N-terminus
    • Yu H., Bondarenko V.A., and Yamazaki A. Inhibition of retinal guanylyl cyclase by the RGS9-1 N-terminus. Biochem. Biophys. Res. Commun. 286 (2001) 12-19
    • (2001) Biochem. Biophys. Res. Commun. , vol.286 , pp. 12-19
    • Yu, H.1    Bondarenko, V.A.2    Yamazaki, A.3
  • 78
    • 0030764226 scopus 로고    scopus 로고
    • Regulators of G-protein signaling (RGS) proteins: region-specific expression of nine subtypes in rat brain
    • Gold S.J., Ni Y.G., Dohlman H.G., and Nestler E.J. Regulators of G-protein signaling (RGS) proteins: region-specific expression of nine subtypes in rat brain. J. Neurosci. 17 (1997) 8024-8037
    • (1997) J. Neurosci. , vol.17 , pp. 8024-8037
    • Gold, S.J.1    Ni, Y.G.2    Dohlman, H.G.3    Nestler, E.J.4
  • 79
    • 0032053616 scopus 로고    scopus 로고
    • RGS9: a regulator of G-protein signalling with specific expression in rat and mouse striatum
    • Thomas E.A., Danielson P.E., and Sutcliffe J.G. RGS9: a regulator of G-protein signalling with specific expression in rat and mouse striatum. J. Neurosci. Res. 52 (1998) 118-124
    • (1998) J. Neurosci. Res. , vol.52 , pp. 118-124
    • Thomas, E.A.1    Danielson, P.E.2    Sutcliffe, J.G.3
  • 80
    • 27244447616 scopus 로고    scopus 로고
    • Differential expression of the regulator of G protein signaling RGS9 protein in nociceptive pathways of different age rats
    • Kim K.J., Moriyama K., Han K.R., Sharma M., Han X., Xie G.X., and Palmer P.P. Differential expression of the regulator of G protein signaling RGS9 protein in nociceptive pathways of different age rats. Brain Res. Dev. Brain Res. 160 (2005) 28-39
    • (2005) Brain Res. Dev. Brain Res. , vol.160 , pp. 28-39
    • Kim, K.J.1    Moriyama, K.2    Han, K.R.3    Sharma, M.4    Han, X.5    Xie, G.X.6    Palmer, P.P.7
  • 81
    • 1842451741 scopus 로고    scopus 로고
    • RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells
    • von Buchholtz L., Elischer A., Tareilus E., Gouka R., Kaiser C., Breer H., and Conzelmann S. RGS21 is a novel regulator of G protein signalling selectively expressed in subpopulations of taste bud cells. Eur. J. Neurosci. 19 (2004) 1535-1544
    • (2004) Eur. J. Neurosci. , vol.19 , pp. 1535-1544
    • von Buchholtz, L.1    Elischer, A.2    Tareilus, E.3    Gouka, R.4    Kaiser, C.5    Breer, H.6    Conzelmann, S.7
  • 82
    • 0035957996 scopus 로고    scopus 로고
    • Mechanisms governing subcellular localization and function of human RGS2
    • Heximer S.P., Lim H., Bernard J.L., and Blumer K.J. 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
  • 84
    • 0035706426 scopus 로고    scopus 로고
    • Evolution of the regulators of G-protein signaling multigene family in mouse and human
    • Sierra D.A., Gilbert D.J., Householder D., Grishin N.V., Yu K., Ukidwe P., et al. Evolution of the regulators of G-protein signaling multigene family in mouse and human. Genomics 79 (2002) 177-185
    • (2002) Genomics , vol.79 , pp. 177-185
    • Sierra, D.A.1    Gilbert, D.J.2    Householder, D.3    Grishin, N.V.4    Yu, K.5    Ukidwe, P.6
  • 85
    • 0034424018 scopus 로고    scopus 로고
    • A core-promoter region functions bi-directionally for human opioid-receptor-like gene ORL1 and its 5′-adjacent gene GAIP
    • Ito E., Xie G., Maruyama K., and Palmer P.P. A core-promoter region functions bi-directionally for human opioid-receptor-like gene ORL1 and its 5′-adjacent gene GAIP. J. Mol. Biol. 304 (2000) 259-270
    • (2000) J. Mol. Biol. , vol.304 , pp. 259-270
    • Ito, E.1    Xie, G.2    Maruyama, K.3    Palmer, P.P.4
  • 86
    • 0037462971 scopus 로고    scopus 로고
    • Gene structure, dual-promoters and mRNA alternative splicing of the human and mouse regulator of G protein signaling GAIP/RGS19
    • Xie G.X., Han X., Ito E., Yanagisawa Y., Maruyama K., Sugano S., et al. Gene structure, dual-promoters and mRNA alternative splicing of the human and mouse regulator of G protein signaling GAIP/RGS19. J. Mol. Biol. 325 (2003) 721-732
    • (2003) J. Mol. Biol. , vol.325 , pp. 721-732
    • Xie, G.X.1    Han, X.2    Ito, E.3    Yanagisawa, Y.4    Maruyama, K.5    Sugano, S.6
  • 88
    • 27744598288 scopus 로고    scopus 로고
    • The RGSZ2 protein exists in a complex with μ-opioid receptors and regulates the desensitizing capacity of Gz proteins
    • Garzon J., Rodriguez-Munoz M., Lopez-Fando A., and Sanchez-Blazquez P. The RGSZ2 protein exists in a complex with μ-opioid receptors and regulates the desensitizing capacity of Gz proteins. Neuropsychopharmacology 30 (2005) 1632-1648
    • (2005) Neuropsychopharmacology , vol.30 , pp. 1632-1648
    • Garzon, J.1    Rodriguez-Munoz, M.2    Lopez-Fando, A.3    Sanchez-Blazquez, P.4
  • 90
    • 33846367289 scopus 로고    scopus 로고
    • Rodriguez-Munoz, M., Bermudez, D., Sanchez-Blazquez, P. & Garzon, J. (2006). Sumoylated RGS-Rz proteins act as scaffolds for mu-opioid receptors and G-protein complexes in mouse brain. Neuropsychopharmacology. [Epub ahead of print].
  • 91
    • 0030738476 scopus 로고    scopus 로고
    • The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro
    • Popov S., Yu K., Kozasa T., and Wilkie T.M. The regulators of G protein signaling (RGS) domains of RGS4, RGS10, and GAIP retain GTPase activating protein activity in vitro. Proc. Natl Acad. Sci. USA 94 (1997) 7216-7220
    • (1997) Proc. Natl Acad. Sci. USA , vol.94 , pp. 7216-7220
    • Popov, S.1    Yu, K.2    Kozasa, T.3    Wilkie, T.M.4
  • 92
    • 0033580817 scopus 로고    scopus 로고
    • Structural basis for the selectivity of the RGS protein, GAIP, for Gαi family members. Identification of a single amino acid determinant for selective interaction of Gαi subunits with GAIP
    • Woulfe D.S., and Stadel J.M. Structural basis for the selectivity of the RGS protein, GAIP, for Gαi family members. Identification of a single amino acid determinant for selective interaction of Gαi subunits with GAIP. J. Biol. Chem. 274 (1999) 17718-17724
    • (1999) J. Biol. Chem. , vol.274 , pp. 17718-17724
    • Woulfe, D.S.1    Stadel, J.M.2
  • 93
    • 0030448762 scopus 로고    scopus 로고
    • GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits
    • De Vries L., Elenko E., Hubler L., Jones T.L., and Farquhar M.G. GAIP is membrane-anchored by palmitoylation and interacts with the activated (GTP-bound) form of Gαi subunits. Proc. Natl Acad. Sci. USA 93 (1996) 15203-15208
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 15203-15208
    • De Vries, L.1    Elenko, E.2    Hubler, L.3    Jones, T.L.4    Farquhar, M.G.5
  • 94
    • 0030982264 scopus 로고    scopus 로고
    • 4-activated Giα1: stabilization of the transition state for GTP hydrolysis
    • 4-activated Giα1: stabilization of the transition state for GTP hydrolysis. Cell 89 (1997) 251-261
    • (1997) Cell , vol.89 , pp. 251-261
    • Tesmer, J.J.1    Berman, D.M.2    Gilman, A.G.3    Sprang, S.R.4
  • 95
    • 0034691314 scopus 로고    scopus 로고
    • NMR structure of free RGS4 reveals an induced conformational change upon binding Gα
    • Moy F.J., Chanda P.K., Cockett M.I., Edris W., Jones P.G., Mason K., et al. NMR structure of free RGS4 reveals an induced conformational change upon binding Gα. Biochemistry 39 (2000) 7063-7073
    • (2000) Biochemistry , vol.39 , pp. 7063-7073
    • Moy, F.J.1    Chanda, P.K.2    Cockett, M.I.3    Edris, W.4    Jones, P.G.5    Mason, K.6
  • 96
    • 0033609905 scopus 로고    scopus 로고
    • Solution structure of human GAIP (Gα interacting protein): a regulator of G protein signaling
    • de Alba E., De Vries L., Farquhar M.G., and Tjandra N. Solution structure of human GAIP (Gα interacting protein): a regulator of G protein signaling. J. Mol. Biol. 291 (1999) 927-939
    • (1999) J. Mol. Biol. , vol.291 , pp. 927-939
    • de Alba, E.1    De Vries, L.2    Farquhar, M.G.3    Tjandra, N.4
  • 97
    • 0032578353 scopus 로고    scopus 로고
    • A single mutation Asp229 → Ser confers upon Gsα the ability to interact with regulators of G protein signaling
    • Natochin M., and Artemyev N.O. A single mutation Asp229 → Ser confers upon Gsα the ability to interact with regulators of G protein signaling. Biochemistry 37 (1998) 13776-13780
    • (1998) Biochemistry , vol.37 , pp. 13776-13780
    • Natochin, M.1    Artemyev, N.O.2
  • 98
    • 0035931919 scopus 로고    scopus 로고
    • Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å
    • Slep K.C., Kercher M.A., He W., Cowan C.W., Wensel T.G., and Sigler P.B. Structural determinants for regulation of phosphodiesterase by a G protein at 2.0 Å. Nature 409 (2001) 1071-1077
    • (2001) Nature , vol.409 , pp. 1071-1077
    • Slep, K.C.1    Kercher, M.A.2    He, W.3    Cowan, C.W.4    Wensel, T.G.5    Sigler, P.B.6
  • 99
    • 0034652331 scopus 로고    scopus 로고
    • A regulator of G protein signaling interaction surface linked to effector specificity
    • Sowa M.E., He W., Wensel T.G., and Lichtarge O. A regulator of G protein signaling interaction surface linked to effector specificity. Proc. Natl Acad. Sci. USA 97 (2000) 1483-1488
    • (2000) Proc. Natl Acad. Sci. USA , vol.97 , pp. 1483-1488
    • Sowa, M.E.1    He, W.2    Wensel, T.G.3    Lichtarge, O.4
  • 101
    • 0033564683 scopus 로고    scopus 로고
    • Modulation of the affinity and selectivity of RGS protein interaction with Gα subunits by a conserved asparagine/serine residue
    • Posner B.A., Mukhopadhyay S., Tesmer J.J., Gilman A.G., and Ross E.M. Modulation of the affinity and selectivity of RGS protein interaction with Gα subunits by a conserved asparagine/serine residue. Biochemistry 38 (1999) 7773-7779
    • (1999) Biochemistry , vol.38 , pp. 7773-7779
    • Posner, B.A.1    Mukhopadhyay, S.2    Tesmer, J.J.3    Gilman, A.G.4    Ross, E.M.5
  • 102
    • 4344691146 scopus 로고    scopus 로고
    • Assays for G-protein-coupled receptor signaling using RGS-insensitive Gα subunits
    • Clark M.J., and Traynor J.R. Assays for G-protein-coupled receptor signaling using RGS-insensitive Gα subunits. Methods Enzymol. 389 (2004) 155-169
    • (2004) Methods Enzymol. , vol.389 , pp. 155-169
    • Clark, M.J.1    Traynor, J.R.2
  • 104
    • 0037399926 scopus 로고    scopus 로고
    • The N-terminal non-RGS domain of human regulator of G-protein signalling 1 contributes to its ability to inhibit pheromone receptor signalling in yeast
    • Somerville W., Song W., Kong J.L., Panetta R., and Greenwood M.T. The N-terminal non-RGS domain of human regulator of G-protein signalling 1 contributes to its ability to inhibit pheromone receptor signalling in yeast. Cell Signal. 15 (2003) 413-421
    • (2003) Cell Signal. , vol.15 , pp. 413-421
    • Somerville, W.1    Song, W.2    Kong, J.L.3    Panetta, R.4    Greenwood, M.T.5
  • 105
    • 0034604693 scopus 로고    scopus 로고
    • Cytoplasmic, nuclear, and Golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs
    • Chatterjee T.K., and Fisher R.A. Cytoplasmic, nuclear, and Golgi localization of RGS proteins. Evidence for N-terminal and RGS domain sequences as intracellular targeting motifs. J. Biol. Chem. 275 (2000) 24013-24021
    • (2000) J. Biol. Chem. , vol.275 , pp. 24013-24021
    • Chatterjee, T.K.1    Fisher, R.A.2
  • 108
    • 2442717874 scopus 로고    scopus 로고
    • RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11α signaling
    • Bernstein L.S., Ramineni S., Hague C., Cladman W., Chidiac P., Levey A.I., and Hepler J.R. RGS2 binds directly and selectively to the M1 muscarinic acetylcholine receptor third intracellular loop to modulate Gq/11α 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    Hepler, J.R.7
  • 109
    • 0035931884 scopus 로고    scopus 로고
    • RGS2 regulates signal transduction in olfactory neurons by attenuating activation of adenylyl cyclase III
    • Sinnarajah S., Dessauer C.W., Srikumar D., Chen J., Yuen J., Yilma S., et al. RGS2 regulates signal transduction in olfactory neurons by attenuating activation of adenylyl cyclase III. Nature 409 (2001) 1051-1055
    • (2001) Nature , vol.409 , pp. 1051-1055
    • Sinnarajah, S.1    Dessauer, C.W.2    Srikumar, D.3    Chen, J.4    Yuen, J.5    Yilma, S.6
  • 110
    • 0037844848 scopus 로고    scopus 로고
    • Identification of RGS2 and type V adenylyl cyclase interaction sites
    • Salim S., Sinnarajah S., Kehrl J.H., and Dessauer C.W. Identification of RGS2 and type V adenylyl cyclase interaction sites. J. Biol. Chem. 278 (2003) 15842-15849
    • (2003) J. Biol. Chem. , vol.278 , pp. 15842-15849
    • Salim, S.1    Sinnarajah, S.2    Kehrl, J.H.3    Dessauer, C.W.4
  • 111
    • 0032567439 scopus 로고    scopus 로고
    • The N-terminal domain of RGS4 confers receptor-selective inhibition of G protein signaling
    • Zeng W., Xu X., Popov S., Mukhopadhyay S., Chidiac P., Swistok J., et al. 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
  • 112
    • 0035827527 scopus 로고    scopus 로고
    • Binding of regulator of G protein signaling (RGS) proteins to phospholipids bilayers. Contribution of location and/or orientation to GTPase-activating protein activity
    • Tu Y., Woodson J., and Ross E.M. Binding of regulator of G protein signaling (RGS) proteins to phospholipids bilayers. Contribution of location and/or orientation to GTPase-activating protein activity. J. Biol. Chem. 276 (2001) 20160-20166
    • (2001) J. Biol. Chem. , vol.276 , pp. 20160-20166
    • Tu, Y.1    Woodson, J.2    Ross, E.M.3
  • 113
    • 0033603315 scopus 로고    scopus 로고
    • Amino terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling
    • Druey K.M., Ugur O., Caron J.M., Chen C.K., Backlund P.S., and Jones T.L. Amino terminal cysteine residues of RGS16 are required for palmitoylation and modulation of Gi- and Gq-mediated signaling. J. Biol. Chem. 274 (1999) 18836-18842
    • (1999) J. Biol. Chem. , vol.274 , pp. 18836-18842
    • Druey, K.M.1    Ugur, O.2    Caron, J.M.3    Chen, C.K.4    Backlund, P.S.5    Jones, T.L.6
  • 114
    • 0032940102 scopus 로고    scopus 로고
    • RGS3 inhibits G protein-mediated signaling via translocation to the membrane and binding to Gα11
    • Dulin N.O., Sorokin A., Reed E., Elliott S., Kehrl J.H., and Dunn M.J. RGS3 inhibits G protein-mediated signaling via translocation to the membrane and binding to Gα11. Mol. Cell Biol. 19 (1999) 714-723
    • (1999) Mol. Cell Biol. , vol.19 , pp. 714-723
    • Dulin, N.O.1    Sorokin, A.2    Reed, E.3    Elliott, S.4    Kehrl, J.H.5    Dunn, M.J.6
  • 115
    • 0035895612 scopus 로고    scopus 로고
    • Characterization of RGS5 in regulation of G protein-coupled receptor signaling
    • Zhou J., Moroi K., Nishiyama M., Usui H., Seki N., Ishida J., et al. Characterization of RGS5 in regulation of G protein-coupled receptor signaling. Life Sci. 68 (2001) 1457-1469
    • (2001) Life Sci. , vol.68 , pp. 1457-1469
    • Zhou, J.1    Moroi, K.2    Nishiyama, M.3    Usui, H.4    Seki, N.5    Ishida, J.6
  • 117
    • 0037162557 scopus 로고    scopus 로고
    • Alternative splicing of RGS8 gene determines inhibitory function of receptor type-specific Gq signaling
    • Saitoh O., Murata Y., Odagiri M., Itoh M., Itoh H., Misaka T., and Kubo Y. 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    Kubo, Y.7
  • 118
    • 0035449061 scopus 로고    scopus 로고
    • + channel kinetics by distinct domains of RGS8
    • + channel kinetics by distinct domains of RGS8. J. Physiol. 535 (2001) 335-347
    • (2001) J. Physiol. , vol.535 , pp. 335-347
    • Jeong, S.W.1    Ikeda, S.R.2
  • 119
    • 0037631598 scopus 로고    scopus 로고
    • Regulators of G protein signaling proteins as determinants of the rate of desensitization of presynaptic calcium channels
    • Diverse-Pierluissi M.A., Fischer T., Jordan J.D., Schiff M., Ortiz D.F., Farquhar M.G., and De Vries L. Regulators of G protein signaling proteins as determinants of the rate of desensitization of presynaptic calcium channels. J. Biol. Chem. 274 (1999) 14490-14494
    • (1999) J. Biol. Chem. , vol.274 , pp. 14490-14494
    • Diverse-Pierluissi, M.A.1    Fischer, T.2    Jordan, J.D.3    Schiff, M.4    Ortiz, D.F.5    Farquhar, M.G.6    De Vries, L.7
  • 120
    • 33645109501 scopus 로고    scopus 로고
    • The effect of RGS12 on PDGFβ receptor signalling to p42/p44 mitogen activated protein kinase in mammalian cells
    • Sambi B.S., Hains M.D., Waters C.M., Connell M.C., Willard F.S., Kimple A.J., et al. The effect of RGS12 on PDGFβ receptor signalling to p42/p44 mitogen activated protein kinase in mammalian cells. Cell Signal. 18 (2006) 971-981
    • (2006) Cell Signal. , vol.18 , pp. 971-981
    • Sambi, B.S.1    Hains, M.D.2    Waters, C.M.3    Connell, M.C.4    Willard, F.S.5    Kimple, A.J.6
  • 121
    • 0032573221 scopus 로고    scopus 로고
    • A G protein γ subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gβ5 subunits
    • Snow B.E., Krumins A.M., Brothers G.M., Lee S.F., Wall M.A., Chung S., et al. A G protein γ subunit-like domain shared between RGS11 and other RGS proteins specifies binding to Gβ5 subunits. Proc. Natl Acad. Sci. USA 95 (1998) 13307-13312
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 13307-13312
    • Snow, B.E.1    Krumins, A.M.2    Brothers, G.M.3    Lee, S.F.4    Wall, M.A.5    Chung, S.6
  • 122
    • 0033038913 scopus 로고    scopus 로고
    • Fidelity of G protein β-subunit association by the G protein γ-subunit-like domains of RGS6, RGS7, and RGS11
    • Snow B.E., Betts L., Mangion J., Sondek J., and Siderovski D.P. Fidelity of G protein β-subunit association by the G protein γ-subunit-like domains of RGS6, RGS7, and RGS11. Proc. Natl Acad. Sci. USA 96 (1999) 6489-6494
    • (1999) Proc. Natl Acad. Sci. USA , vol.96 , pp. 6489-6494
    • Snow, B.E.1    Betts, L.2    Mangion, J.3    Sondek, J.4    Siderovski, D.P.5
  • 123
    • 0037404433 scopus 로고    scopus 로고
    • Direct interactions between the heterotrimeric G protein subunit Gβ5 and the G protein γ subunit-like domain-containing regulator of G protein signaling 11: gain of function of cyan fluorescent protein-tagged Gγ3
    • Zhou J.Y., Toth P.T., and Miller R.J. Direct interactions between the heterotrimeric G protein subunit Gβ5 and the G protein γ subunit-like domain-containing regulator of G protein signaling 11: gain of function of cyan fluorescent protein-tagged Gγ3. J. Pharmacol. Expt. Ther. 305 (2003) 460-466
    • (2003) J. Pharmacol. Expt. Ther. , vol.305 , pp. 460-466
    • Zhou, J.Y.1    Toth, P.T.2    Miller, R.J.3
  • 124
    • 0034602868 scopus 로고    scopus 로고
    • Co-expression of Gβ5 enhances the function of two Gγ subunit-like domain-containing regulators of G protein signaling proteins
    • Kovoor A., Chen C.K., He W., Wensel T.G., Simon M.I., and Lester H.A. Co-expression of Gβ5 enhances the function of two Gγ subunit-like domain-containing regulators of G protein signaling proteins. J. Biol. Chem. 275 (2000) 3397-3402
    • (2000) J. Biol. Chem. , vol.275 , pp. 3397-3402
    • Kovoor, A.1    Chen, C.K.2    He, W.3    Wensel, T.G.4    Simon, M.I.5    Lester, H.A.6
  • 125
    • 0037872689 scopus 로고    scopus 로고
    • Instability of GGL domain-containing RGS proteins in mice lacking the G protein β-subunit Gβ5
    • Chen C.K., Eversole-Cire P., Zhang H., Mancino V., Chen Y.J., He W., et al. Instability of GGL domain-containing RGS proteins in mice lacking the G protein β-subunit Gβ5. Proc. Natl Acad. Sci. USA 100 (2003) 6604-6609
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 6604-6609
    • Chen, C.K.1    Eversole-Cire, P.2    Zhang, H.3    Mancino, V.4    Chen, Y.J.5    He, W.6
  • 126
    • 14044273637 scopus 로고    scopus 로고
    • R7BP, a novel neuronal protein interacting with RGS proteins of the R7 family
    • Martemyanov K.A., Yoo P.J., Skiba N.P., and Arshavsky V.Y. R7BP, a novel neuronal protein interacting with RGS proteins of the R7 family. J. Biol. Chem. 280 (2005) 5133-5136
    • (2005) J. Biol. Chem. , vol.280 , pp. 5133-5136
    • Martemyanov, K.A.1    Yoo, P.J.2    Skiba, N.P.3    Arshavsky, V.Y.4
  • 127
    • 22344431893 scopus 로고    scopus 로고
    • Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family
    • Drenan R.M., Doupnik C.A., Boyle M.P., Muglia L.J., Huettner J.E., Linder M.E., and Blumer K.J. Palmitoylation regulates plasma membrane-nuclear shuttling of R7BP, a novel membrane anchor for the RGS7 family. J. Cell Biol. 169 (2005) 623-633
    • (2005) J. Cell Biol. , vol.169 , pp. 623-633
    • Drenan, R.M.1    Doupnik, C.A.2    Boyle, M.P.3    Muglia, L.J.4    Huettner, J.E.5    Linder, M.E.6    Blumer, K.J.7
  • 128
    • 33744962677 scopus 로고    scopus 로고
    • Subcellular targeting of RGS9-2 is controlled by multiple molecular determinants on its membrane anchor, R7BP
    • Song J.H., Waataja J.J., and Martemyanov K.A. Subcellular targeting of RGS9-2 is controlled by multiple molecular determinants on its membrane anchor, R7BP. J. Biol. Chem. 281 (2006) 15361-15369
    • (2006) J. Biol. Chem. , vol.281 , pp. 15361-15369
    • Song, J.H.1    Waataja, J.J.2    Martemyanov, K.A.3
  • 129
    • 0037162461 scopus 로고    scopus 로고
    • R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein, RGS9-1
    • Hu G., and Wensel T.G. R9AP, a membrane anchor for the photoreceptor GTPase accelerating protein, RGS9-1. Proc. Natl Acad. Sci. USA 99 (2002) 9755-9760
    • (2002) Proc. Natl Acad. Sci. USA , vol.99 , pp. 9755-9760
    • Hu, G.1    Wensel, T.G.2
  • 130
    • 0038529736 scopus 로고    scopus 로고
    • Activation of RGS9-1 GTPase acceleration by its membrane anchor, R9AP
    • Hu G., Zhang Z., and Wensel T.G. Activation of RGS9-1 GTPase acceleration by its membrane anchor, R9AP. J. Biol. Chem. 278 (2003) 14550-14554
    • (2003) J. Biol. Chem. , vol.278 , pp. 14550-14554
    • Hu, G.1    Zhang, Z.2    Wensel, T.G.3
  • 131
    • 0345687489 scopus 로고    scopus 로고
    • The DEP domain determines subcellular targeting of the GTPase activating protein RGS9 in vivo
    • Martemyanov K.A., Lishko P.V., Calero N., Keresztes G., Sokolov M., Strissel K.J., et al. The DEP domain determines subcellular targeting of the GTPase activating protein RGS9 in vivo. J. Neurosci. 23 (2003) 10175-10181
    • (2003) J. Neurosci. , vol.23 , pp. 10175-10181
    • Martemyanov, K.A.1    Lishko, P.V.2    Calero, N.3    Keresztes, G.4    Sokolov, M.5    Strissel, K.J.6
  • 133
    • 0035800830 scopus 로고    scopus 로고
    • RGS12 and RGS14 GoLoco motifs are Gαi interaction sites with guanine nucleotide dissociation inhibitor activity
    • Kimple R.J., De Vries L., Tronchere H., Behe C.I., Morris R.A., Farquhar M.G., and Siderovski D.P. RGS12 and RGS14 GoLoco motifs are Gαi interaction sites with guanine nucleotide dissociation inhibitor activity. J. Biol. Chem. 276 (2001) 29275-29281
    • (2001) J. Biol. Chem. , vol.276 , pp. 29275-29281
    • Kimple, R.J.1    De Vries, L.2    Tronchere, H.3    Behe, C.I.4    Morris, R.A.5    Farquhar, M.G.6    Siderovski, D.P.7
  • 134
    • 0037171778 scopus 로고    scopus 로고
    • Structural determinants for GoLoco-induced inhibition of nucleotide release by Gα subunits
    • Kimple R.J., Kimple M.E., Betts L., Sondek J., and Siderovski D.P. Structural determinants for GoLoco-induced inhibition of nucleotide release by Gα 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
  • 135
    • 8744291072 scopus 로고    scopus 로고
    • The RGS14 GoLoco domain discriminates among Gαi isoforms
    • Mittal V., and Linder M.E. The RGS14 GoLoco domain discriminates among Gαi isoforms. J. Biol. Chem. 279 (2004) 46772-46778
    • (2004) J. Biol. Chem. , vol.279 , pp. 46772-46778
    • Mittal, V.1    Linder, M.E.2
  • 136
    • 4344624682 scopus 로고    scopus 로고
    • GoLoco motif peptides as probes of Gα subunit specificity in coupling of G-protein-coupled receptors to ion channels
    • Oxford G.S., and Webb C.K. GoLoco motif peptides as probes of Gα subunit specificity in coupling of G-protein-coupled receptors to ion channels. Methods Enzymol. 390 (2004) 437-450
    • (2004) Methods Enzymol. , vol.390 , pp. 437-450
    • Oxford, G.S.1    Webb, C.K.2
  • 137
    • 22844433094 scopus 로고    scopus 로고
    • Selective inhibition of α1A-adrenergic receptor signaling by RGS2 association with the receptor third intracellular loop
    • Hague C., Bernstein L.S., Ramineni S., Chen Z., Minneman K.P., and Hepler J.R. Selective inhibition of α1A-adrenergic receptor signaling by RGS2 association with the receptor third intracellular loop. J. Biol. Chem. 280 (2005) 27289-27295
    • (2005) J. Biol. Chem. , vol.280 , pp. 27289-27295
    • Hague, C.1    Bernstein, L.S.2    Ramineni, S.3    Chen, Z.4    Minneman, K.P.5    Hepler, J.R.6
  • 138
    • 32244436712 scopus 로고    scopus 로고
    • Selective interactions between G protein subunits and RGS4 with the C-terminal domains of the μ- and δ-opioid receptors regulate opioid receptor signaling
    • Georgoussi Z., Leontiadis L., Mazarakou G., Merkouris M., Hyde K., and Hamm H. Selective interactions between G protein subunits and RGS4 with the C-terminal domains of the μ- and δ-opioid receptors regulate opioid receptor signaling. Cell Signal. 18 (2006) 771-782
    • (2006) Cell Signal. , vol.18 , pp. 771-782
    • Georgoussi, Z.1    Leontiadis, L.2    Mazarakou, G.3    Merkouris, M.4    Hyde, K.5    Hamm, H.6
  • 139
    • 0035957236 scopus 로고    scopus 로고
    • RGS4 inhibits platelet-activating factor receptor phosphorylation and cellular responses
    • Richardson R.M., Marjoram R.J., Barr A.J., and Snyderman R. RGS4 inhibits platelet-activating factor receptor phosphorylation and cellular responses. Biochemistry 40 (2001) 3583-3588
    • (2001) Biochemistry , vol.40 , pp. 3583-3588
    • Richardson, R.M.1    Marjoram, R.J.2    Barr, A.J.3    Snyderman, R.4
  • 140
    • 0037077031 scopus 로고    scopus 로고
    • Regulation of the gonadotropin-releasing hormone receptor (GnRHR) by RGS proteins: role of the GnRHR carboxyl-terminus
    • Castro-Fernandez C., and Conn P.M. Regulation of the gonadotropin-releasing hormone receptor (GnRHR) by RGS proteins: role of the GnRHR carboxyl-terminus. Mol. Cell. Endocrinol. 191 (2002) 149-156
    • (2002) Mol. Cell. Endocrinol. , vol.191 , pp. 149-156
    • Castro-Fernandez, C.1    Conn, P.M.2
  • 141
    • 15644373915 scopus 로고    scopus 로고
    • GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain
    • Snow B.E., Hall R.A., Krumins A.M., Brothers G.M., Bouchard D., Brothers C.A., et al. GTPase activating specificity of RGS12 and binding specificity of an alternatively spliced PDZ (PSD-95/Dlg/ZO-1) domain. J. Biol. Chem. 273 (1998) 17749-17755
    • (1998) J. Biol. Chem. , vol.273 , pp. 17749-17755
    • Snow, B.E.1    Hall, R.A.2    Krumins, A.M.3    Brothers, G.M.4    Bouchard, D.5    Brothers, C.A.6
  • 142
    • 0034623163 scopus 로고    scopus 로고
    • 14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity
    • Benzing T., Yaffe M.B., Arnould T., Sellin L., Schermer B., Schilling B., et al. 14-3-3 interacts with regulator of G protein signaling proteins and modulates their activity. J. Biol. Chem. 275 (2000) 28167-28172
    • (2000) J. Biol. Chem. , vol.275 , pp. 28167-28172
    • Benzing, T.1    Yaffe, M.B.2    Arnould, T.3    Sellin, L.4    Schermer, B.5    Schilling, B.6
  • 143
    • 0037031884 scopus 로고    scopus 로고
    • Interaction of 14-3-3 protein with regulator of G protein signaling 7 is dynamically regulated by tumor necrosis factor-α
    • Benzing T., Kottgen M., Johnson M., Schermer B., Zentgraf H., Walz G., and Kim E. Interaction of 14-3-3 protein with regulator of G protein signaling 7 is dynamically regulated by tumor necrosis factor-α. J. Biol. Chem. 277 (2002) 32954-32962
    • (2002) J. Biol. Chem. , vol.277 , pp. 32954-32962
    • Benzing, T.1    Kottgen, M.2    Johnson, M.3    Schermer, B.4    Zentgraf, H.5    Walz, G.6    Kim, E.7
  • 144
    • 0036684568 scopus 로고    scopus 로고
    • RGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domain
    • Niu J., Scheschonka A., Druey K.M., Davis A., Reed E., Kolenko V., et al. RGS3 interacts with 14-3-3 via the N-terminal region distinct from the RGS (regulator of G-protein signalling) domain. Biochem. J. 365 (2002) 677-684
    • (2002) Biochem. J. , vol.365 , pp. 677-684
    • Niu, J.1    Scheschonka, A.2    Druey, K.M.3    Davis, A.4    Reed, E.5    Kolenko, V.6
  • 145
    • 27844511015 scopus 로고    scopus 로고
    • A key serine for the GTPase-activating protein function of regulator of G protein signaling proteins is not a general target for 14-3-3 interactions
    • Ward R.J., and Milligan G. A key serine for the GTPase-activating protein function of regulator of G protein signaling proteins is not a general target for 14-3-3 interactions. Mol. Pharmacol. 68 (2005) 1821-1830
    • (2005) Mol. Pharmacol. , vol.68 , pp. 1821-1830
    • Ward, R.J.1    Milligan, G.2
  • 146
    • 0032780332 scopus 로고    scopus 로고
    • Upregulation of RGS7 may contribute to tumor necrosis factor-induced changes in central nervous function
    • Benzing T., Brandes R., Sellin L., Schermer B., Lecker S., Walz G., and Kim E. Upregulation of RGS7 may contribute to tumor necrosis factor-induced changes in central nervous function. Nature Med. 5 (1999) 913-918
    • (1999) Nature Med. , vol.5 , pp. 913-918
    • Benzing, T.1    Brandes, R.2    Sellin, L.3    Schermer, B.4    Lecker, S.5    Walz, G.6    Kim, E.7
  • 147
    • 0037478669 scopus 로고    scopus 로고
    • Promotion of Gαi3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIP
    • Fischer T., De Vries L., Meerloo T., and Farquhar M.G. Promotion of Gαi3 subunit down-regulation by GIPN, a putative E3 ubiquitin ligase that interacts with RGS-GAIP. Proc. Natl Acad. Sci. USA 100 (2003) 8270-8275
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 8270-8275
    • Fischer, T.1    De Vries, L.2    Meerloo, T.3    Farquhar, M.G.4
  • 148
    • 0032514630 scopus 로고    scopus 로고
    • GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP
    • De Vries L., Lou X., Zhao G., Zheng B., and Farquhar M.G. GIPC, a PDZ domain containing protein, interacts specifically with the C terminus of RGS-GAIP. Proc. Natl Acad. Sci. USA 95 (1998) 12340-12345
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 12340-12345
    • De Vries, L.1    Lou, X.2    Zhao, G.3    Zheng, B.4    Farquhar, M.G.5
  • 149
    • 6344241436 scopus 로고    scopus 로고
    • GIPC recruits GAIP (RGS19) to attenuate dopamine D2 receptor signaling
    • Jeanneteau F., Guillin O., Diaz J., Griffon N., and Sokoloff P. GIPC recruits GAIP (RGS19) to attenuate dopamine D2 receptor signaling. Mol. Biol. Cell. 15 (2004) 4926-4937
    • (2004) Mol. Biol. Cell. , vol.15 , pp. 4926-4937
    • Jeanneteau, F.1    Guillin, O.2    Diaz, J.3    Griffon, N.4    Sokoloff, P.5
  • 150
    • 0038505967 scopus 로고    scopus 로고
    • GIPC interacts with the β1-adrenergic receptor and regulates β1-adrenergic receptor-mediated ERK activation
    • Hu L.A., Chen W., Martin N.P., Whalen E.J., Premont R.T., and Lefkowitz R.J. GIPC interacts with the β1-adrenergic receptor and regulates β1-adrenergic receptor-mediated ERK activation. J. Biol. Chem. 278 (2003) 26295-26301
    • (2003) J. Biol. Chem. , vol.278 , pp. 26295-26301
    • Hu, L.A.1    Chen, W.2    Martin, N.P.3    Whalen, E.J.4    Premont, R.T.5    Lefkowitz, R.J.6
  • 151
    • 0037155160 scopus 로고    scopus 로고
    • GIPC participates in G protein signaling downstream of insulin-like growth factor 1 receptor
    • Booth R.A., Cummings C., Tiberi M., and Liu X.J. GIPC participates in G protein signaling downstream of insulin-like growth factor 1 receptor. J. Biol. Chem. 277 (2002) 6719-6725
    • (2002) J. Biol. Chem. , vol.277 , pp. 6719-6725
    • Booth, R.A.1    Cummings, C.2    Tiberi, M.3    Liu, X.J.4
  • 152
    • 0035158872 scopus 로고    scopus 로고
    • GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways
    • Lou X., Yano H., Lee F., Chao M.V., and Farquhar M.G. GIPC and GAIP form a complex with TrkA: a putative link between G protein and receptor tyrosine kinase pathways. Mol. Biol. Cell. 12 (2001) 615-627
    • (2001) Mol. Biol. Cell. , vol.12 , pp. 615-627
    • Lou, X.1    Yano, H.2    Lee, F.3    Chao, M.V.4    Farquhar, M.G.5
  • 153
    • 0035955713 scopus 로고    scopus 로고
    • A novel mechanism for regulating transforming growth factor β (TGF-β) signaling. Functional modulation of type III TGF-β receptor expression through interaction with the PDZ domain protein, GIPC
    • Blobe G.C., Liu X., Fang S.J., How T., and Lodish H.F. A novel mechanism for regulating transforming growth factor β (TGF-β) signaling. Functional modulation of type III TGF-β receptor expression through interaction with the PDZ domain protein, GIPC. J. Biol. Chem. 276 (2001) 39608-39617
    • (2001) J. Biol. Chem. , vol.276 , pp. 39608-39617
    • Blobe, G.C.1    Liu, X.2    Fang, S.J.3    How, T.4    Lodish, H.F.5
  • 154
    • 3042659111 scopus 로고    scopus 로고
    • Spinophilin blocks arrestin actions in vitro and in vivo at G protein-coupled receptors
    • Wang Q., Zhao J., Brady A.E., Feng J., Allen P.B., Lefkowitz R.J., et al. Spinophilin blocks arrestin actions in vitro and in vivo at G protein-coupled receptors. Science 304 (2004) 1940-1944
    • (2004) Science , vol.304 , pp. 1940-1944
    • Wang, Q.1    Zhao, J.2    Brady, A.E.3    Feng, J.4    Allen, P.B.5    Lefkowitz, R.J.6
  • 155
    • 17344367802 scopus 로고    scopus 로고
    • 2+ signalling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors
    • 2+ signalling by binding the N-terminal domain of RGS2 and the third intracellular loop of G-protein-coupled receptors. Nature Cell Biol. 7 (2005) 405-411
    • (2005) Nature 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
  • 157
    • 0037184945 scopus 로고    scopus 로고
    • Regulated interactions of the α2A adrenergic receptor with spinophilin, 14-3-3ζ, and arrestin 3
    • Wang Q., and Limbird L.E. Regulated interactions of the α2A adrenergic receptor with spinophilin, 14-3-3ζ, and arrestin 3. J. Biol. Chem. 277 (2002) 50589-50596
    • (2002) J. Biol. Chem. , vol.277 , pp. 50589-50596
    • Wang, Q.1    Limbird, L.E.2
  • 159
    • 17844410054 scopus 로고    scopus 로고
    • α2-Adrenergic agonist enrichment of spinophilin at the cell surface involves βγ subunits of Gi proteins and is preferentially induced by the α2A-subtype
    • Brady A.E., Wang Q., Allen P.B., Rizzo M., Greengard P., and Limbird L.E. α2-Adrenergic agonist enrichment of spinophilin at the cell surface involves βγ subunits of Gi proteins and is preferentially induced by the α2A-subtype. Mol. Pharmacol. 67 (2005) 1690-1696
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1690-1696
    • Brady, A.E.1    Wang, Q.2    Allen, P.B.3    Rizzo, M.4    Greengard, P.5    Limbird, L.E.6
  • 160
    • 0033538487 scopus 로고    scopus 로고
    • Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1-interacting protein
    • Smith F.D., Oxford G.S., and Milgram S.L. Association of the D2 dopamine receptor third cytoplasmic loop with spinophilin, a protein phosphatase-1-interacting protein. J. Biol. Chem. 274 (1999) 19894-19900
    • (1999) J. Biol. Chem. , vol.274 , pp. 19894-19900
    • Smith, F.D.1    Oxford, G.S.2    Milgram, S.L.3
  • 161
    • 0042672922 scopus 로고    scopus 로고
    • Homer 2 tunes G protein-coupled receptors stimulus intensity by regulating RGS proteins and PLCβ GAP activities
    • Shin D.M., Dehoff M., Luo X., Kang S.H., Tu J., Nayak S.K., et al. Homer 2 tunes G protein-coupled receptors stimulus intensity by regulating RGS proteins and PLCβ GAP activities. J. Cell Biol. 162 (2003) 293-303
    • (2003) J. Cell Biol. , vol.162 , pp. 293-303
    • Shin, D.M.1    Dehoff, M.2    Luo, X.3    Kang, S.H.4    Tu, J.5    Nayak, S.K.6
  • 162
    • 33645642111 scopus 로고    scopus 로고
    • Brain-specific regulator of G-protein signaling 9-2 selectively interacts with α-actinin-2 to regulate calcium-dependent inactivation of NMDA receptors
    • Bouhamdan M., Yan H.D., Yan X.H., Bannon M.J., and Andrade R. Brain-specific regulator of G-protein signaling 9-2 selectively interacts with α-actinin-2 to regulate calcium-dependent inactivation of NMDA receptors. J. Neurosci. 26 (2006) 2522-2530
    • (2006) J. Neurosci. , vol.26 , pp. 2522-2530
    • Bouhamdan, M.1    Yan, H.D.2    Yan, X.H.3    Bannon, M.J.4    Andrade, R.5
  • 163
    • 0034703054 scopus 로고    scopus 로고
    • Novel alternative splicing and nuclear localization of human RGS12 gene products
    • Chatterjee T.K., and Fisher R.A. Novel alternative splicing and nuclear localization of human RGS12 gene products. J. Biol. Chem. 275 (2000) 29660-29671
    • (2000) J. Biol. Chem. , vol.275 , pp. 29660-29671
    • Chatterjee, T.K.1    Fisher, R.A.2
  • 164
    • 0034705237 scopus 로고    scopus 로고
    • 2+/Calmodulin reverses phosphatidylinositol 3,4,5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity
    • 2+/Calmodulin reverses phosphatidylinositol 3,4,5-trisphosphate-dependent inhibition of regulators of G protein-signaling GTPase-activating protein activity. J. Biol. Chem. 275 (2000) 18962-18968
    • (2000) J. Biol. Chem. , vol.275 , pp. 18962-18968
    • Popov, S.G.1    Krishna, U.M.2    Falck, J.R.3    Wilkie, T.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.