메뉴 건너뛰기




Volumn 17, Issue 2, 2010, Pages 89-99

Accessory proteins for heterotrimeric G-protein: Implication in the cardiovascular system

Author keywords

Activator of G protein signaling (AGS); Cardiovascular disease; Heterotrimeric G protein; Regulator of G protein signaling (RGS); Signal transduction

Indexed keywords

ACTIVATOR OF G PROTEIN SIGNALING 1 PROTEIN; ACTIVATOR OF G PROTEIN SIGNALING 3 PROTEIN; DEXAMETHASONE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANINE NUCLEOTIDE DISSOCIATION INHIBITOR; GUANINE NUCLEOTIDE EXCHANGE FACTOR; GUANOSINE TRIPHOSPHATASE ACTIVATING PROTEIN; NEUROMODULIN; PHOSDUCIN; PHOSDUCIN LIKE PROTEIN; PHOSPHATIDYLETHANOLAMINE BINDING PROTEIN; PRESENILIN 1; RAS PROTEIN; RECEPTOR FOR ACTIVATED C KINASE 1; RGS2 PROTEIN; RGS4 PROTEIN; SYNTAXIN 1A; TUBULIN; UNCLASSIFIED DRUG;

EID: 77649189888     PISSN: 09284680     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pathophys.2009.03.011     Document Type: Review
Times cited : (11)

References (118)
  • 1
    • 33947527882 scopus 로고    scopus 로고
    • Cardiac GPCRs: GPCR signaling in healthy and failing hearts
    • Salazar N.C., Chen J., and Rockman H.A. Cardiac GPCRs: GPCR signaling in healthy and failing hearts. Biochim. Biophys. Acta 1768 (2007) 1006-1018
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 1006-1018
    • Salazar, N.C.1    Chen, J.2    Rockman, H.A.3
  • 2
    • 0026047960 scopus 로고
    • Protection against infarction afforded by preconditioning is mediated by A1 adenosine receptors in rabbit heart
    • Liu G.S., Thornton J., Van Winkle D.M., Stanley A.W., Olsson R.A., and Downey J.M. Protection against infarction afforded by preconditioning is mediated by A1 adenosine receptors in rabbit heart. Circulation 84 (1991) 350-356
    • (1991) Circulation , vol.84 , pp. 350-356
    • Liu, G.S.1    Thornton, J.2    Van Winkle, D.M.3    Stanley, A.W.4    Olsson, R.A.5    Downey, J.M.6
  • 3
    • 0027471927 scopus 로고
    • Ischemic preconditioning increases adenosine release and 5′-nucleotidase activity during myocardial ischemia and reperfusion in dogs. Implications for myocardial salvage
    • Kitakaze M., Hori M., Takashima S., Sato H., Inoue M., and Kamada T. Ischemic preconditioning increases adenosine release and 5′-nucleotidase activity during myocardial ischemia and reperfusion in dogs. Implications for myocardial salvage. Circulation 87 (1993) 208-215
    • (1993) Circulation , vol.87 , pp. 208-215
    • Kitakaze, M.1    Hori, M.2    Takashima, S.3    Sato, H.4    Inoue, M.5    Kamada, T.6
  • 5
    • 0031044250 scopus 로고    scopus 로고
    • The adenylyl cyclases as integrators of transmembrane signal transduction
    • Ishikawa Y., and Homcy C.J. The adenylyl cyclases as integrators of transmembrane signal transduction. Circ. Res. 80 (1997) 297-304
    • (1997) Circ. Res. , vol.80 , pp. 297-304
    • Ishikawa, Y.1    Homcy, C.J.2
  • 6
    • 33947407279 scopus 로고    scopus 로고
    • Expansion of signal transduction by G proteins. The second 15 years or so: from 3 to 16 alpha subunits plus betagamma dimers
    • Birnbaumer L. Expansion of signal transduction by G proteins. The second 15 years or so: from 3 to 16 alpha subunits plus betagamma dimers. Biochim. Biophys. Acta 1768 (2007) 772-793
    • (2007) Biochim. Biophys. Acta , vol.1768 , pp. 772-793
    • Birnbaumer, L.1
  • 7
    • 47749117162 scopus 로고    scopus 로고
    • G protein betagamma subunits: central mediators of G protein-coupled receptor signaling
    • Smrcka A.V. G protein betagamma subunits: central mediators of G protein-coupled receptor signaling. Cell. Mol. Life Sci. 65 (2008) 2191-2214
    • (2008) Cell. Mol. Life Sci. , vol.65 , pp. 2191-2214
    • Smrcka, A.V.1
  • 8
    • 0029067834 scopus 로고
    • Factors determining specificity of signal transduction by G-protein-coupled receptors. Regulation of signal transfer from receptor to G-protein
    • Sato M., Kataoka R., Dingus J., Wilcox M., Hildebrandt J.D., and Lanier S.M. Factors determining specificity of signal transduction by G-protein-coupled receptors. Regulation of signal transfer from receptor to G-protein. J. Biol. Chem. 270 (1995) 15269-15276
    • (1995) J. Biol. Chem. , vol.270 , pp. 15269-15276
    • Sato, M.1    Kataoka, R.2    Dingus, J.3    Wilcox, M.4    Hildebrandt, J.D.5    Lanier, S.M.6
  • 9
    • 0029860884 scopus 로고    scopus 로고
    • Characterization of a G-protein activator in the neuroblastoma-glioma cell hybrid NG108-15
    • Sato M., Ribas C., Hildebrandt J.D., and Lanier S.M. 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
  • 10
    • 0031010119 scopus 로고    scopus 로고
    • Factors determining the specificity of signal transduction by guanine nucleotide-binding protein-coupled receptors. Integration of stimulatory and inhibitory input to the effector adenylyl cyclase
    • Marjamaki A., Sato M., Bouet-Alard R., Yang Q., Limon-Boulez I., Legrand C., and Lanier S.M. Factors determining the specificity of signal transduction by guanine nucleotide-binding protein-coupled receptors. Integration of stimulatory and inhibitory input to the effector adenylyl cyclase. J. Biol. Chem. 272 (1997) 16466-16473
    • (1997) J. Biol. Chem. , vol.272 , pp. 16466-16473
    • Marjamaki, A.1    Sato, M.2    Bouet-Alard, R.3    Yang, Q.4    Limon-Boulez, I.5    Legrand, C.6    Lanier, S.M.7
  • 11
    • 33751277456 scopus 로고    scopus 로고
    • Adenylyl cyclase isoforms and vasopressin enhancement of agonist-stimulated cAMP in vascular smooth muscle cells
    • Zhang J., Sato M., Duzic E., Kubalak S.W., Lanier S.M., and Webb J.G. Adenylyl cyclase isoforms and vasopressin enhancement of agonist-stimulated cAMP in vascular smooth muscle cells. Am. J. Physiol. 273 (1997) H971-980
    • (1997) Am. J. Physiol. , vol.273
    • Zhang, J.1    Sato, M.2    Duzic, E.3    Kubalak, S.W.4    Lanier, S.M.5    Webb, J.G.6
  • 12
    • 0037184956 scopus 로고    scopus 로고
    • Pertussis toxin-insensitive activation of the heterotrimeric G-proteins Gi/Go by the NG108-15 G-protein activator
    • Ribas C., Takesono A., Sato M., Hildebrandt J.D., and Lanier S.M. Pertussis toxin-insensitive activation of the heterotrimeric G-proteins Gi/Go by the NG108-15 G-protein activator. J. Biol. Chem. 277 (2002) 50223-50225
    • (2002) J. Biol. Chem. , vol.277 , pp. 50223-50225
    • Ribas, C.1    Takesono, A.2    Sato, M.3    Hildebrandt, J.D.4    Lanier, S.M.5
  • 13
    • 1842678142 scopus 로고    scopus 로고
    • AGS3 and signal integration by Galpha(s)- and Galpha(i)-coupled receptors: AGS3 blocks the sensitization of adenylyl cyclase following prolonged stimulation of a Galpha(i)-coupled receptor by influencing processing of Galpha(i)
    • Sato M., Gettys T.W., and Lanier S.M. AGS3 and signal integration by Galpha(s)- and Galpha(i)-coupled receptors: AGS3 blocks the sensitization of adenylyl cyclase following prolonged stimulation of a Galpha(i)-coupled receptor by influencing processing of Galpha(i). J. Biol. Chem. 279 (2004) 13375-13382
    • (2004) J. Biol. Chem. , vol.279 , pp. 13375-13382
    • Sato, M.1    Gettys, T.W.2    Lanier, S.M.3
  • 14
    • 31444453235 scopus 로고    scopus 로고
    • Identification of a receptor-independent activator of G protein signaling (AGS8) in ischemic heart and its interaction with Gbetagamma
    • Sato M., Cismowski M.J., Toyota E., Smrcka A.V., Lucchesi P.A., Chilian W.M., and Lanier S.M. Identification of a receptor-independent activator of G protein signaling (AGS8) in ischemic heart and its interaction with Gbetagamma. Proc. Natl. Acad. Sci. U.S.A. 103 (2006) 797-802
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 797-802
    • Sato, M.1    Cismowski, M.J.2    Toyota, E.3    Smrcka, A.V.4    Lucchesi, P.A.5    Chilian, W.M.6    Lanier, S.M.7
  • 16
    • 0025889699 scopus 로고
    • An intracellular guanine nucleotide release protein for G0. GAP-43 stimulates isolated alpha subunits by a novel mechanism
    • Strittmatter S.M., Valenzuela D., Sudo Y., Linder M.E., and Fishman M.C. 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
  • 17
    • 0027447656 scopus 로고
    • Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o)
    • Nishimoto I., Okamoto T., Matsuura Y., Takahashi S., Murayama Y., and Ogata E. Alzheimer amyloid protein precursor complexes with brain GTP-binding protein G(o). Nature 362 (1993) 75-79
    • (1993) Nature , vol.362 , pp. 75-79
    • Nishimoto, I.1    Okamoto, T.2    Matsuura, Y.3    Takahashi, S.4    Murayama, Y.5    Ogata, E.6
  • 21
    • 0032488810 scopus 로고    scopus 로고
    • Dexamethasone rapidly induces a novel ras superfamily member-related gene in AtT-20 cells
    • Kemppainen R.J., and Behrend E.N. Dexamethasone rapidly induces a novel ras superfamily member-related gene in AtT-20 cells. J. Biol. Chem. 273 (1998) 3129-3131
    • (1998) J. Biol. Chem. , vol.273 , pp. 3129-3131
    • Kemppainen, R.J.1    Behrend, E.N.2
  • 22
    • 0034604518 scopus 로고    scopus 로고
    • Activation of heterotrimeric G-protein signaling by a ras-related protein. Implications for signal integration
    • Cismowski M.J., Ma C., Ribas C., Xie X., Spruyt M., Lizano J.S., Lanier S.M., and Duzic E. 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    Lanier, S.M.7    Duzic, E.8
  • 23
    • 0035018861 scopus 로고    scopus 로고
    • Dexras1/AGS-1, a steroid hormone-induced guanosine triphosphate-binding protein, inhibits 3′,5′-cyclic adenosine monophosphate-stimulated secretion in AtT-20 corticotroph cells
    • Graham T.E., Key T.A., Kilpatrick K., and Dorin R.I. Dexras1/AGS-1, a steroid hormone-induced guanosine triphosphate-binding protein, inhibits 3′,5′-cyclic adenosine monophosphate-stimulated secretion in AtT-20 corticotroph cells. Endocrinology 142 (2001) 2631-2640
    • (2001) Endocrinology , vol.142 , pp. 2631-2640
    • Graham, T.E.1    Key, T.A.2    Kilpatrick, K.3    Dorin, R.I.4
  • 25
    • 0034003003 scopus 로고    scopus 로고
    • Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein
    • Yeung K., Janosch P., McFerran B., Rose D.W., Mischak H., Sedivy J.M., and Kolch W. Mechanism of suppression of the Raf/MEK/extracellular signal-regulated kinase pathway by the raf kinase inhibitor protein. Mol. Cell. Biol. 20 (2000) 3079-3085
    • (2000) Mol. Cell. Biol. , vol.20 , pp. 3079-3085
    • Yeung, K.1    Janosch, P.2    McFerran, B.3    Rose, D.W.4    Mischak, H.5    Sedivy, J.M.6    Kolch, W.7
  • 26
    • 0346874333 scopus 로고    scopus 로고
    • Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2
    • Lorenz K., Lohse M.J., and Quitterer U. Protein kinase C switches the Raf kinase inhibitor from Raf-1 to GRK-2. Nature 426 (2003) 574-579
    • (2003) Nature , vol.426 , pp. 574-579
    • Lorenz, K.1    Lohse, M.J.2    Quitterer, U.3
  • 27
    • 0025084434 scopus 로고
    • Purification, cloning, and tissue distribution of a 23-kDa rat protein isolated by morphine affinity chromatography
    • Grandy D.K., Hanneman E., Bunzow J., Shih M., Machida C.A., Bidlack J.M., and Civelli O. Purification, cloning, and tissue distribution of a 23-kDa rat protein isolated by morphine affinity chromatography. Mol. Endocrinol. 4 (1990) 1370-1376
    • (1990) Mol. Endocrinol. , vol.4 , pp. 1370-1376
    • Grandy, D.K.1    Hanneman, E.2    Bunzow, J.3    Shih, M.4    Machida, C.A.5    Bidlack, J.M.6    Civelli, O.7
  • 28
    • 0035955736 scopus 로고    scopus 로고
    • Human phosphatidylethanolamine-binding protein facilitates heterotrimeric G protein-dependent signaling
    • Kroslak T., Koch T., Kahl E., and Hollt V. 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
  • 29
    • 0037424298 scopus 로고    scopus 로고
    • Mammalian Ric-8A (synembryn) is a heterotrimeric Galpha protein guanine nucleotide exchange factor
    • Tall G.G., Krumins A.M., and Gilman A.G. 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
  • 30
    • 0030771361 scopus 로고    scopus 로고
    • Role of subunit diversity in signaling by heterotrimeric G proteins
    • Hildebrandt J.D. Role of subunit diversity in signaling by heterotrimeric G proteins. Biochem. Pharmacol. 54 (1997) 325-339
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 325-339
    • Hildebrandt, J.D.1
  • 31
    • 0033572358 scopus 로고    scopus 로고
    • The G protein subunit gene families
    • Downes G.B., and Gautam N. The G protein subunit gene families. Genomics 62 (1999) 544-552
    • (1999) Genomics , vol.62 , pp. 544-552
    • Downes, G.B.1    Gautam, N.2
  • 32
    • 33745972929 scopus 로고    scopus 로고
    • Non-receptor activators of heterotrimeric G-protein signaling (AGS proteins)
    • Cismowski M.J. Non-receptor activators of heterotrimeric G-protein signaling (AGS proteins). Semin. Cell Dev. Biol. 17 (2006) 334-344
    • (2006) Semin. Cell Dev. Biol. , vol.17 , pp. 334-344
    • Cismowski, M.J.1
  • 33
    • 33847781275 scopus 로고    scopus 로고
    • Mechanistic pathways and biological roles for receptor-independent activators of G-protein signaling
    • Blumer J.B., Smrcka A.V., and Lanier S.M. 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
  • 35
    • 19744364926 scopus 로고    scopus 로고
    • Dexras1 blocks receptor-mediated heterologous sensitization of adenylyl cyclase 1
    • Nguyen C.H., and Watts V.J. 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
  • 38
    • 77649180556 scopus 로고    scopus 로고
    • Mammalian blood loss-induced gene, kd312,
    • US Patent #6,462,177
    • K.M. Yen, Mammalian blood loss-induced gene, kd312, US Patent #6,462,177 (1998).
    • (1998)
    • Yen, K.M.1
  • 42
    • 0042809557 scopus 로고    scopus 로고
    • Altered atrial electrical restitution and heterogeneous sympathetic hyperinnervation in hearts with chronic left ventricular myocardial infarction: implications for atrial fibrillation
    • Miyauchi Y., Zhou S., Okuyama Y., Miyauchi M., Hayashi H., Hamabe A., Fishbein M.C., Mandel W.J., Chen L.S., Chen P.S., et al. Altered atrial electrical restitution and heterogeneous sympathetic hyperinnervation in hearts with chronic left ventricular myocardial infarction: implications for atrial fibrillation. Circulation 108 (2003) 360-366
    • (2003) Circulation , vol.108 , pp. 360-366
    • Miyauchi, Y.1    Zhou, S.2    Okuyama, Y.3    Miyauchi, M.4    Hayashi, H.5    Hamabe, A.6    Fishbein, M.C.7    Mandel, W.J.8    Chen, L.S.9    Chen, P.S.10
  • 44
    • 35348860241 scopus 로고    scopus 로고
    • Presenilin: running with scissors in the membrane
    • Selkoe D.J., and Wolfe M.S. Presenilin: running with scissors in the membrane. Cell 131 (2007) 215-221
    • (2007) Cell , vol.131 , pp. 215-221
    • Selkoe, D.J.1    Wolfe, M.S.2
  • 45
    • 3342889548 scopus 로고    scopus 로고
    • Presenilin 1 is essential for cardiac morphogenesis
    • Nakajima M., Moriizumi E., Koseki H., and Shirasawa T. Presenilin 1 is essential for cardiac morphogenesis. Dev. Dyn. 230 (2004) 795-799
    • (2004) Dev. Dyn. , vol.230 , pp. 795-799
    • Nakajima, M.1    Moriizumi, E.2    Koseki, H.3    Shirasawa, T.4
  • 47
    • 0027934665 scopus 로고
    • Tubulin-G protein association stabilizes GTP binding and activates GTPase: cytoskeletal participation in neuronal signal transduction
    • Roychowdhury S., and Rasenick M.M. Tubulin-G protein association stabilizes GTP binding and activates GTPase: cytoskeletal participation in neuronal signal transduction. Biochemistry 33 (1994) 9800-9805
    • (1994) Biochemistry , vol.33 , pp. 9800-9805
    • Roychowdhury, S.1    Rasenick, M.M.2
  • 48
    • 0027235428 scopus 로고
    • G protein binding and G protein activation by nucleotide transfer involve distinct domains on tubulin: regulation of signal transduction by cytoskeletal elements
    • Roychowdhury S., Wang N., and Rasenick M.M. G protein binding and G protein activation by nucleotide transfer involve distinct domains on tubulin: regulation of signal transduction by cytoskeletal elements. Biochemistry 32 (1993) 4955-4961
    • (1993) Biochemistry , vol.32 , pp. 4955-4961
    • Roychowdhury, S.1    Wang, N.2    Rasenick, M.M.3
  • 50
    • 0025176937 scopus 로고
    • Tubulin binds specifically to the signal-transducing proteins, Gs alpha and Gi alpha 1
    • Wang N., Yan K., and Rasenick M.M. Tubulin binds specifically to the signal-transducing proteins, Gs alpha and Gi alpha 1. J. Biol. Chem. 265 (1990) 1239-1242
    • (1990) J. Biol. Chem. , vol.265 , pp. 1239-1242
    • Wang, N.1    Yan, K.2    Rasenick, M.M.3
  • 51
    • 0023884769 scopus 로고
    • Exchange of guanine nucleotides between tubulin and GTP-binding proteins that regulate adenylate cyclase: cytoskeletal modification of neuronal signal transduction
    • Rasenick M.M., and Wang N. Exchange of guanine nucleotides between tubulin and GTP-binding proteins that regulate adenylate cyclase: cytoskeletal modification of neuronal signal transduction. J. Neurochem. 51 (1988) 300-311
    • (1988) J. Neurochem. , vol.51 , pp. 300-311
    • Rasenick, M.M.1    Wang, N.2
  • 52
    • 0031282982 scopus 로고    scopus 로고
    • G protein beta1gamma2 subunits promote microtubule assembly
    • Roychowdhury S., and Rasenick M.M. G protein beta1gamma2 subunits promote microtubule assembly. J. Biol. Chem. 272 (1997) 31576-31581
    • (1997) J. Biol. Chem. , vol.272 , pp. 31576-31581
    • Roychowdhury, S.1    Rasenick, M.M.2
  • 54
    • 6944256893 scopus 로고    scopus 로고
    • Control of embryonic spindle positioning and Galpha activity by C. elegans RIC-8
    • Couwenbergs C., Spilker A.C., and Gotta M. 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
  • 55
    • 0035907344 scopus 로고    scopus 로고
    • Identification of a truncated form of the G-protein regulator AGS3 in heart that lacks the tetratricopeptide repeat domains
    • Pizzinat N., Takesono A., and Lanier S.M. Identification of a truncated form of the G-protein regulator AGS3 in heart that lacks the tetratricopeptide repeat domains. J. Biol. Chem. 276 (2001) 16601-16610
    • (2001) J. Biol. Chem. , vol.276 , pp. 16601-16610
    • Pizzinat, N.1    Takesono, A.2    Lanier, S.M.3
  • 56
    • 0029417219 scopus 로고
    • Adenylylcyclase supersensitization in mu-opioid receptor-transfected Chinese hamster ovary cells following chronic opioid treatment
    • Avidor-Reiss T., Bayewitch M., Levy R., Matus-Leibovitch N., Nevo I., and Vogel Z. Adenylylcyclase supersensitization in mu-opioid receptor-transfected Chinese hamster ovary cells following chronic opioid treatment. J. Biol. Chem. 270 (1995) 29732-29738
    • (1995) J. Biol. Chem. , vol.270 , pp. 29732-29738
    • Avidor-Reiss, T.1    Bayewitch, M.2    Levy, R.3    Matus-Leibovitch, N.4    Nevo, I.5    Vogel, Z.6
  • 57
    • 19444378697 scopus 로고    scopus 로고
    • Sensitization of adenylate cyclase by Galpha i/o-coupled receptors
    • Watts V.J., and Neve K.A. Sensitization of adenylate cyclase by Galpha i/o-coupled receptors. Pharmacol. Ther. 106 (2005) 405-421
    • (2005) Pharmacol. Ther. , vol.106 , pp. 405-421
    • Watts, V.J.1    Neve, K.A.2
  • 59
    • 20844436775 scopus 로고    scopus 로고
    • Activator of G protein signaling 3 regulates opiate activation of protein kinase A signaling and relapse of heroin-seeking behavior
    • Yao L., McFarland K., Fan P., Jiang Z., Inoue Y., and Diamond I. Activator of G protein signaling 3 regulates opiate activation of protein kinase A signaling and relapse of heroin-seeking behavior. Proc. Natl. Acad. Sci. U.S.A. 102 (2005) 8746-8751
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 8746-8751
    • Yao, L.1    McFarland, K.2    Fan, P.3    Jiang, Z.4    Inoue, Y.5    Diamond, I.6
  • 61
    • 0030576518 scopus 로고    scopus 로고
    • GAIP and RGS4 are GTPase-activating proteins for the Gi subfamily of G protein alpha 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 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
  • 62
    • 0029808079 scopus 로고    scopus 로고
    • RGS family members: GTPase-activating proteins for heterotrimeric G-protein alpha-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 alpha-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
  • 63
    • 14844343100 scopus 로고    scopus 로고
    • Multi-tasking RGS proteins in the heart: the next therapeutic target?
    • Riddle E.L., Schwartzman R.A., Bond M., and Insel P.A. Multi-tasking RGS proteins in the heart: the next therapeutic target?. Circ. Res. 96 (2005) 401-411
    • (2005) Circ. Res. , vol.96 , pp. 401-411
    • Riddle, E.L.1    Schwartzman, R.A.2    Bond, M.3    Insel, P.A.4
  • 64
    • 43049122122 scopus 로고    scopus 로고
    • Regulation of G protein-coupled receptor signalling: focus on the cardiovascular system and regulator of G protein signalling proteins
    • Hendriks-Balk M.C., Peters S.L., Michel M.C., and Alewijnse A.E. Regulation of G protein-coupled receptor signalling: focus on the cardiovascular system and regulator of G protein signalling proteins. Eur. J. Pharmacol. 585 (2008) 278-291
    • (2008) Eur. J. Pharmacol. , vol.585 , pp. 278-291
    • Hendriks-Balk, M.C.1    Peters, S.L.2    Michel, M.C.3    Alewijnse, A.E.4
  • 67
    • 0034903134 scopus 로고    scopus 로고
    • Expression of RGS3, RGS4 and Gi alpha 2 in acutely failing donor hearts and end-stage heart failure
    • Owen V.J., Burton P.B., Mullen A.J., Birks E.J., Barton P., and Yacoub M.H. Expression of RGS3, RGS4 and Gi alpha 2 in acutely failing donor hearts and end-stage heart failure. Eur. Heart J. 22 (2001) 1015-1020
    • (2001) Eur. Heart J. , vol.22 , pp. 1015-1020
    • Owen, V.J.1    Burton, P.B.2    Mullen, A.J.3    Birks, E.J.4    Barton, P.5    Yacoub, M.H.6
  • 74
    • 0032917612 scopus 로고    scopus 로고
    • RGS4 inhibits G-protein signaling in cardiomyocytes
    • Tamirisa P., Blumer K.J., and Muslin A.J. RGS4 inhibits G-protein signaling in cardiomyocytes. Circulation 99 (1999) 441-447
    • (1999) Circulation , vol.99 , pp. 441-447
    • Tamirisa, P.1    Blumer, K.J.2    Muslin, A.J.3
  • 75
    • 0034967283 scopus 로고    scopus 로고
    • RGS4 reduces contractile dysfunction and hypertrophic gene induction in Galpha q overexpressing mice
    • Rogers J.H., Tsirka A., Kovacs A., Blumer K.J., Dorn II G.W., and Muslin A.J. RGS4 reduces contractile dysfunction and hypertrophic gene induction in Galpha q overexpressing mice. J. Mol. Cell. Cardiol. 33 (2001) 209-218
    • (2001) J. Mol. Cell. Cardiol. , vol.33 , pp. 209-218
    • Rogers, J.H.1    Tsirka, A.2    Kovacs, A.3    Blumer, K.J.4    Dorn II, G.W.5    Muslin, A.J.6
  • 77
    • 16344394786 scopus 로고    scopus 로고
    • Regulators of G protein signaling & drugs of abuse
    • Traynor J.R., and Neubig R.R. Regulators of G protein signaling & drugs of abuse. Mol. Interv. 5 (2005) 30-41
    • (2005) Mol. Interv. , vol.5 , pp. 30-41
    • Traynor, J.R.1    Neubig, R.R.2
  • 78
    • 0036765564 scopus 로고    scopus 로고
    • Characterization and comparison of RGS2 and RGS4 as GTPase-activating proteins for m2 muscarinic receptor-stimulated G(i)
    • Cladman W., and Chidiac P. 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
  • 81
    • 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
  • 82
    • 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., Gach A., Cui L., Liao R., and Mende U. 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    Gach, A.7    Cui, L.8    Liao, R.9    Mende, U.10
  • 83
    • 0033514516 scopus 로고    scopus 로고
    • Gbeta5 prevents the RGS7-Galphao interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins
    • Levay K., Cabrera J.L., Satpaev D.K., and Slepak V.Z. Gbeta5 prevents the RGS7-Galphao interaction through binding to a distinct Ggamma-like domain found in RGS7 and other RGS proteins. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 2503-2507
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 2503-2507
    • Levay, K.1    Cabrera, J.L.2    Satpaev, D.K.3    Slepak, V.Z.4
  • 84
    • 0033515040 scopus 로고    scopus 로고
    • The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit
    • Makino E.R., Handy J.W., Li T., and Arshavsky V.Y. The GTPase activating factor for transducin in rod photoreceptors is the complex between RGS9 and type 5 G protein beta subunit. Proc. Natl. Acad. Sci. U.S.A. 96 (1999) 1947-1952
    • (1999) Proc. Natl. Acad. Sci. U.S.A. , vol.96 , pp. 1947-1952
    • Makino, E.R.1    Handy, J.W.2    Li, T.3    Arshavsky, V.Y.4
  • 86
    • 0032562743 scopus 로고    scopus 로고
    • Cloning and tissue distribution of the human G protein beta 5 cDNA
    • Jones P.G., Lombardi S.J., and Cockett M.I. Cloning and tissue distribution of the human G protein beta 5 cDNA. Biochim. Biophys. Acta 1402 (1998) 288-291
    • (1998) Biochim. Biophys. Acta , vol.1402 , pp. 288-291
    • Jones, P.G.1    Lombardi, S.J.2    Cockett, M.I.3
  • 90
    • 34547129113 scopus 로고    scopus 로고
    • Signaling by a non-dissociated complex of G Protein betagamma and alpha subunits stimulated by a receptor-independent activator of G protein signaling, AGS8
    • Yuan C., Sato M., Lanier S.M., and Smrcka A.V. Signaling by a non-dissociated complex of G Protein betagamma and alpha subunits stimulated by a receptor-independent activator of G protein signaling, AGS8. J. Biol. Chem. 282 (2007) 19938-19947
    • (2007) J. Biol. Chem. , vol.282 , pp. 19938-19947
    • Yuan, C.1    Sato, M.2    Lanier, S.M.3    Smrcka, A.V.4
  • 92
    • 0037146552 scopus 로고    scopus 로고
    • The betagamma subunit of heterotrimeric G proteins interacts with RACK1 and two other WD repeat proteins
    • Dell E.J., Connor J., Chen S., Stebbins E.G., Skiba N.P., Mochly-Rosen D., and Hamm H.E. The betagamma subunit of heterotrimeric G proteins interacts with RACK1 and two other WD repeat proteins. J. Biol. Chem. 277 (2002) 49888-49895
    • (2002) J. Biol. Chem. , vol.277 , pp. 49888-49895
    • Dell, E.J.1    Connor, J.2    Chen, S.3    Stebbins, E.G.4    Skiba, N.P.5    Mochly-Rosen, D.6    Hamm, H.E.7
  • 94
    • 2342444943 scopus 로고    scopus 로고
    • RACK1 regulates specific functions of Gbetagamma
    • Chen S., Dell E.J., Lin F., Sai J., and Hamm H.E. RACK1 regulates specific functions of Gbetagamma. J. Biol. Chem. 279 (2004) 17861-17868
    • (2004) J. Biol. Chem. , vol.279 , pp. 17861-17868
    • Chen, S.1    Dell, E.J.2    Lin, F.3    Sai, J.4    Hamm, H.E.5
  • 96
    • 34948880732 scopus 로고    scopus 로고
    • Effects of RACK1 on cell migration and IGF-I signalling in cardiomyoctes are not dependent on an association with the IGF-IR
    • O'Donovan H.C., Kiely P.A., and O'Connor R. Effects of RACK1 on cell migration and IGF-I signalling in cardiomyoctes are not dependent on an association with the IGF-IR. Cell Signal. 19 (2007) 2588-2595
    • (2007) Cell Signal. , vol.19 , pp. 2588-2595
    • O'Donovan, H.C.1    Kiely, P.A.2    O'Connor, R.3
  • 97
    • 0034054672 scopus 로고    scopus 로고
    • G protein modulation of N-type calcium channels is facilitated by physical interactions between syntaxin 1A and Gbetagamma
    • Jarvis S.E., Magga J.M., Beedle A.M., Braun J.E., and Zamponi G.W. G protein modulation of N-type calcium channels is facilitated by physical interactions between syntaxin 1A and Gbetagamma. J. Biol. Chem. 275 (2000) 6388-6394
    • (2000) J. Biol. Chem. , vol.275 , pp. 6388-6394
    • Jarvis, S.E.1    Magga, J.M.2    Beedle, A.M.3    Braun, J.E.4    Zamponi, G.W.5
  • 98
    • 0037113926 scopus 로고    scopus 로고
    • Molecular determinants of syntaxin 1 modulation of N-type calcium channels
    • Jarvis S.E., Barr W., Feng Z.P., Hamid J., and Zamponi G.W. Molecular determinants of syntaxin 1 modulation of N-type calcium channels. J. Biol. Chem. 277 (2002) 44399-44407
    • (2002) J. Biol. Chem. , vol.277 , pp. 44399-44407
    • Jarvis, S.E.1    Barr, W.2    Feng, Z.P.3    Hamid, J.4    Zamponi, G.W.5
  • 100
    • 35548980544 scopus 로고    scopus 로고
    • 2+-dependent binding of synaptotagmin to the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex
    • 2+-dependent binding of synaptotagmin to the soluble N-ethylmaleimide-sensitive factor attachment protein receptor (SNARE) complex. Mol. Pharmacol. 72 (2007) 1210-1219
    • (2007) Mol. Pharmacol. , vol.72 , pp. 1210-1219
    • Yoon, E.J.1    Gerachshenko, T.2    Spiegelberg, B.D.3    Alford, S.4    Hamm, H.E.5
  • 101
    • 33244488029 scopus 로고    scopus 로고
    • Identification, localization and interaction of SNARE proteins in atrial cardiac myocytes
    • Peters C.G., Miller D.F., and Giovannucci D.R. Identification, localization and interaction of SNARE proteins in atrial cardiac myocytes. J. Mol. Cell. Cardiol. 40 (2006) 361-374
    • (2006) J. Mol. Cell. Cardiol. , vol.40 , pp. 361-374
    • Peters, C.G.1    Miller, D.F.2    Giovannucci, D.R.3
  • 102
    • 0023668192 scopus 로고
    • A novel complex from bovine visual cells of a 33,000-dalton phosphoprotein with beta- and gamma-transducin: purification and subunit structure
    • Lee R.H., Lieberman B.S., and Lolley R.N. A novel complex from bovine visual cells of a 33,000-dalton phosphoprotein with beta- and gamma-transducin: purification and subunit structure. Biochemistry 26 (1987) 3983-3990
    • (1987) Biochemistry , vol.26 , pp. 3983-3990
    • Lee, R.H.1    Lieberman, B.S.2    Lolley, R.N.3
  • 103
    • 0029814150 scopus 로고    scopus 로고
    • Phosducin is a ubiquitous G-protein regulator
    • Danner S., and Lohse M.J. Phosducin is a ubiquitous G-protein regulator. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 10145-10150
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 10145-10150
    • Danner, S.1    Lohse, M.J.2
  • 104
    • 33646827339 scopus 로고    scopus 로고
    • SUMO-1 controls the protein stability and the biological function of phosducin
    • Klenk C., Humrich J., Quitterer U., and Lohse M.J. SUMO-1 controls the protein stability and the biological function of phosducin. J. Biol. Chem. 281 (2006) 8357-8364
    • (2006) J. Biol. Chem. , vol.281 , pp. 8357-8364
    • Klenk, C.1    Humrich, J.2    Quitterer, U.3    Lohse, M.J.4
  • 105
    • 0344075958 scopus 로고    scopus 로고
    • Cloning and characterization of the rat and human phosducin-like protein genes: structure, expression and chromosomal localization
    • Thibault C., Feng Wang J., Charnas R., Mirel D., Barhite S., and Miles M.F. Cloning and characterization of the rat and human phosducin-like protein genes: structure, expression and chromosomal localization. Biochim. Biophys. Acta 1444 (1999) 346-354
    • (1999) Biochim. Biophys. Acta , vol.1444 , pp. 346-354
    • Thibault, C.1    Feng Wang, J.2    Charnas, R.3    Mirel, D.4    Barhite, S.5    Miles, M.F.6
  • 106
    • 0033762303 scopus 로고    scopus 로고
    • Quantification of the tissue levels and function of the G-protein regulator phosducin-like protein (PhlP)
    • Schroder S., and Lohse M.J. Quantification of the tissue levels and function of the G-protein regulator phosducin-like protein (PhlP). Naunyn Schmiedebergs Arch. Pharmacol. 362 (2000) 435-439
    • (2000) Naunyn Schmiedebergs Arch. Pharmacol. , vol.362 , pp. 435-439
    • Schroder, S.1    Lohse, M.J.2
  • 107
    • 0030924690 scopus 로고    scopus 로고
    • Interaction of phosducin-like protein with G protein betagamma subunits
    • Thibault C., Sganga M.W., and Miles M.F. Interaction of phosducin-like protein with G protein betagamma subunits. J. Biol. Chem. 272 (1997) 12253-12256
    • (1997) J. Biol. Chem. , vol.272 , pp. 12253-12256
    • Thibault, C.1    Sganga, M.W.2    Miles, M.F.3
  • 108
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin
    • Gaudet R., Bohm A., and Sigler P.B. Crystal structure at 2.4 angstroms resolution of the complex of transducin betagamma and its regulator, phosducin. Cell 87 (1996) 577-588
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 109
    • 0029935648 scopus 로고    scopus 로고
    • Inhibition of G-protein betagamma-subunit functions by phosducin-like protein
    • Schroder S., and Lohse M.J. Inhibition of G-protein betagamma-subunit functions by phosducin-like protein. Proc. Natl. Acad. Sci. U.S.A. 93 (1996) 2100-2104
    • (1996) Proc. Natl. Acad. Sci. U.S.A. , vol.93 , pp. 2100-2104
    • Schroder, S.1    Lohse, M.J.2
  • 112
    • 0035164003 scopus 로고    scopus 로고
    • Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default
    • Oh P., and Schnitzer J.E. Segregation of heterotrimeric G proteins in cell surface microdomains. G(q) binds caveolin to concentrate in caveolae, whereas G(i) and G(s) target lipid rafts by default. Mol. Biol. Cell 12 (2001) 685-698
    • (2001) Mol. Biol. Cell , vol.12 , pp. 685-698
    • Oh, P.1    Schnitzer, J.E.2
  • 113
    • 0037710123 scopus 로고    scopus 로고
    • Cholesterol-dependent association of caveolin-1 with the transducin alpha subunit in bovine photoreceptor rod outer segments: disruption by cyclodextrin and guanosine 5′-O-(3-thiotriphosphate)
    • Elliott M.H., Fliesler S.J., and Ghalayini A.J. Cholesterol-dependent association of caveolin-1 with the transducin alpha subunit in bovine photoreceptor rod outer segments: disruption by cyclodextrin and guanosine 5′-O-(3-thiotriphosphate). Biochemistry 42 (2003) 7892-7903
    • (2003) Biochemistry , vol.42 , pp. 7892-7903
    • Elliott, M.H.1    Fliesler, S.J.2    Ghalayini, A.J.3
  • 114
    • 41149124594 scopus 로고    scopus 로고
    • Caveolae as organizers of pharmacologically relevant signal transduction molecules
    • Patel H.H., Murray F., and Insel P.A. Caveolae as organizers of pharmacologically relevant signal transduction molecules. Annu. Rev. Pharmacol. Toxicol. 48 (2008) 359-391
    • (2008) Annu. Rev. Pharmacol. Toxicol. , vol.48 , pp. 359-391
    • Patel, H.H.1    Murray, F.2    Insel, P.A.3
  • 115
    • 33747396191 scopus 로고    scopus 로고
    • Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition
    • Han Y., Chen Y.S., Liu Z., Bodyak N., Rigor D., Bisping E., Pu W.T., and Kang P.M. Overexpression of HAX-1 protects cardiac myocytes from apoptosis through caspase-9 inhibition. Circ. Res. 99 (2006) 415-423
    • (2006) Circ. Res. , vol.99 , pp. 415-423
    • Han, Y.1    Chen, Y.S.2    Liu, Z.3    Bodyak, N.4    Rigor, D.5    Bisping, E.6    Pu, W.T.7    Kang, P.M.8
  • 118
    • 0035824512 scopus 로고    scopus 로고
    • Interaction between the G alpha subunit of heterotrimeric G(12) protein and Hsp90 is required for G alpha(12) signaling
    • Vaiskunaite R., Kozasa T., and Voyno-Yasenetskaya T.A. Interaction between the G alpha subunit of heterotrimeric G(12) protein and Hsp90 is required for G alpha(12) signaling. J. Biol. Chem. 276 (2001) 46088-46093
    • (2001) J. Biol. Chem. , vol.276 , pp. 46088-46093
    • Vaiskunaite, R.1    Kozasa, T.2    Voyno-Yasenetskaya, T.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.