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Volumn 54, Issue 3, 1997, Pages 325-339

Role of subunit diversity in signaling by heterotrimeric G proteins

Author keywords

Cell signaling; G protein; Isoforms; Physiological effects; Receptor; Subunits

Indexed keywords

GUANINE NUCLEOTIDE BINDING PROTEIN; PROTEIN SUBUNIT;

EID: 0030771361     PISSN: 00062952     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-2952(97)00269-4     Document Type: Note
Times cited : (129)

References (229)
  • 1
    • 0029282131 scopus 로고
    • G proteins and regulation of adenylyl cyclase
    • Gilman AG, G proteins and regulation of adenylyl cyclase. Biosci Rep 15: 65-97, 1995.
    • (1995) Biosci Rep , vol.15 , pp. 65-97
    • Gilman, A.G.1
  • 2
    • 0029320699 scopus 로고
    • Signal transduction: Evolution of an idea
    • Rodbell M, Signal transduction: Evolution of an idea. Biosci Rep 15: 117-133, 1995.
    • (1995) Biosci Rep , vol.15 , pp. 117-133
    • Rodbell, M.1
  • 4
    • 0028909714 scopus 로고
    • Receptors and G proteins as primary components of transmembrane signal transduction. Part I. G protein coupled receptors: Structure and function
    • Gudermann T, Nurnberg B and Schultz G, Receptors and G proteins as primary components of transmembrane signal transduction. Part I. G protein coupled receptors: Structure and function. J Mol Med 73: 51-63, 1995.
    • (1995) J Mol Med , vol.73 , pp. 51-63
    • Gudermann, T.1    Nurnberg, B.2    Schultz, G.3
  • 5
    • 0030034644 scopus 로고    scopus 로고
    • The G protein nanomachine
    • Clapham DE, The G protein nanomachine. Nature 379: 297-298, 1996.
    • (1996) Nature , vol.379 , pp. 297-298
    • Clapham, D.E.1
  • 9
    • 0023668192 scopus 로고
    • A novel complex from bovine visual cells of a 33,000-dalton phosphoprotein with β- and γ-transducin: Purification and subunit structure
    • Lee RH, Lieberman BS and Lolley RN, A novel complex from bovine visual cells of a 33,000-dalton phosphoprotein with β- and γ-transducin: Purification and subunit structure. Biochemistry 26: 3983-3990, 1987.
    • (1987) Biochemistry , vol.26 , pp. 3983-3990
    • Lee, R.H.1    Lieberman, B.S.2    Lolley, R.N.3
  • 11
    • 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 MR and Horvitz HR, EGL-10 regulates G protein signaling in the C. elegans nervous system and shares a conserved domain with many mammalian proteins. Cell 84: 115-125, 1996.
    • (1996) Cell , vol.84 , pp. 115-125
    • Koelle, M.R.1    Horvitz, H.R.2
  • 12
    • 0029808079 scopus 로고    scopus 로고
    • RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits
    • Watson N, Linder ME, Druey KM, Kehrl JH and Blumer KJ, RGS family members: GTPase-activating proteins for heterotrimeric G-protein α-subunits. Nature 383: 172-175, 1996.
    • (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
  • 14
    • 0031027064 scopus 로고    scopus 로고
    • There are GAPS and there are GAPS
    • Iyengar R, There are GAPS and there are GAPS. Science 275: 42-43, 1997.
    • (1997) Science , vol.275 , pp. 42-43
    • Iyengar, R.1
  • 15
    • 0031041306 scopus 로고    scopus 로고
    • RGS proteins and signaling by heterotrimeric G proteins
    • Dohlman HG and Thorner J, RGS proteins and signaling by heterotrimeric G proteins. J Biol Chem 272: 3871-3874, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 3871-3874
    • Dohlman, H.G.1    Thorner, J.2
  • 16
    • 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 JD and Lanier SM, Factors determining specificity of signal transduction by G-protein-coupled receptors. Regulation of signal transfer from receptor to G-protein. J Biol Chem 270: 15269-15276, 1995.
    • (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
  • 17
    • 0029860884 scopus 로고    scopus 로고
    • Characterization of a G protein activator in the neuroblastoma glioma cell hybrid NG108-15
    • Sato M, Ribas C, Hildebrandt JD and Lanier SM, Characterization of a G protein activator in the neuroblastoma glioma cell hybrid NG108-15. J Biol Chem 271: 30052-30060, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 30052-30060
    • Sato, M.1    Ribas, C.2    Hildebrandt, J.D.3    Lanier, S.M.4
  • 18
    • 0024709982 scopus 로고
    • Signal sorting and amplification through G protein-coupled receptors
    • Ross EM, Signal sorting and amplification through G protein-coupled receptors. Neuron 3: 141-152, 1989.
    • (1989) Neuron , vol.3 , pp. 141-152
    • Ross, E.M.1
  • 19
    • 0015239313 scopus 로고
    • The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanyl nucleotides in glucagon action
    • Rodbell M, Birnbaumer L, Pohl SL and Krans HMJ, The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. V. An obligatory role of guanyl nucleotides in glucagon action. J Biol Chem 246: 1877-1882, 1971.
    • (1971) J Biol Chem , vol.246 , pp. 1877-1882
    • Rodbell, M.1    Birnbaumer, L.2    Pohl, S.L.3    Krans, H.M.J.4
  • 20
    • 0014670359 scopus 로고
    • Adenyl cyclase in fat cells. II. Hormone receptors
    • Birnbaumer L and Rodbell M, Adenyl cyclase in fat cells. II. Hormone receptors. J Biol Chem 244: 3477-3482, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 3477-3482
    • Birnbaumer, L.1    Rodbell, M.2
  • 21
    • 0017795361 scopus 로고
    • Hormone-sensitive adenylate cyclase: Resolution and reconstitution of some components necessary for regulation of the enzyme
    • Ross EM, Haga T, Howlett AC, Schwarzmeier J, Schleifer LS and Gilman AG, Hormone-sensitive adenylate cyclase: Resolution and reconstitution of some components necessary for regulation of the enzyme. Adv Cyclic Nucleotide Res 9: 53-68, 1978.
    • (1978) Adv Cyclic Nucleotide Res , vol.9 , pp. 53-68
    • Ross, E.M.1    Haga, T.2    Howlett, A.C.3    Schwarzmeier, J.4    Schleifer, L.S.5    Gilman, A.G.6
  • 24
    • 0021111692 scopus 로고
    • Identification of the predominant substrate for ADP-ribosylation by islet activating protein
    • Bokoch GM, Katada T, Northup JK, Hewlett EL and Gilman AG, Identification of the predominant substrate for ADP-ribosylation by islet activating protein. J Biol Chem 258: 2072-2075, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 2072-2075
    • Bokoch, G.M.1    Katada, T.2    Northup, J.K.3    Hewlett, E.L.4    Gilman, A.G.5
  • 26
    • 0018901497 scopus 로고
    • Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes
    • Kuhn H, Light- and GTP-regulated interaction of GTPase and other proteins with bovine photoreceptor membranes. Nature 283: 587-589, 1980.
    • (1980) Nature , vol.283 , pp. 587-589
    • Kuhn, H.1
  • 27
    • 0005496920 scopus 로고
    • A light-activated GTPase in vertebrate photoreceptors: Regulation of light-activated cyclic GMP phosphodiesterase
    • Wheeler GL and Bitensky MW, A light-activated GTPase in vertebrate photoreceptors: Regulation of light-activated cyclic GMP phosphodiesterase. Proc Natl Acad Sci USA 74: 4238-4242, 1977.
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 4238-4242
    • Wheeler, G.L.1    Bitensky, M.W.2
  • 28
    • 0018715614 scopus 로고
    • Membrane-dependent guanine nucleotide binding and GTPase activities of soluble protein from bovine rod cell outer segments
    • Godchaux W and Zimmerman WF, Membrane-dependent guanine nucleotide binding and GTPase activities of soluble protein from bovine rod cell outer segments. J Biol Chem 254: 7874-7884, 1979.
    • (1979) J Biol Chem , vol.254 , pp. 7874-7884
    • Godchaux, W.1    Zimmerman, W.F.2
  • 29
    • 0000329823 scopus 로고
    • Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments
    • Fung BK and Stryer L, Photolyzed rhodopsin catalyzes the exchange of GTP for bound GDP in retinal rod outer segments. Proc Natl Acad Sci USA 77: 2500-2504, 1980.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2500-2504
    • Fung, B.K.1    Stryer, L.2
  • 30
    • 0020595220 scopus 로고
    • The regulatory components of adenylate cyclase and transducin. A family of structurally homologous guanine nucleotide-binding proteins
    • Manning DR and Gilman AG, The regulatory components of adenylate cyclase and transducin. A family of structurally homologous guanine nucleotide-binding proteins. J Biol Chem 258: 7059-7063, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 7059-7063
    • Manning, D.R.1    Gilman, A.G.2
  • 32
    • 0021325727 scopus 로고
    • Purification and properties of the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase
    • Bokoch GM, Katada T, Northup JK, Ui M and Gilman AG, Purification and properties of the inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. J Biol Chem 259: 3560-3567, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 3560-3567
    • Bokoch, G.M.1    Katada, T.2    Northup, J.K.3    Ui, M.4    Gilman, A.G.5
  • 33
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon MI, Strathmann MP and Gautam N, Diversity of G proteins in signal transduction. Science 252: 802-808, 1991.
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 34
    • 0025910365 scopus 로고
    • Structure and function of signal-transducing GTP-binding proteins
    • Kaziro Y, Itoh H, Kozasa T, Nakafuku M and Satoh T, Structure and function of signal-transducing GTP-binding proteins. Annu Rev Biochem 60: 349-400, 1991.
    • (1991) Annu Rev Biochem , vol.60 , pp. 349-400
    • Kaziro, Y.1    Itoh, H.2    Kozasa, T.3    Nakafuku, M.4    Satoh, T.5
  • 35
    • 0021194782 scopus 로고
    • i, by β-adrenergic receptors in reconstituted phospholipid vesicles
    • i, by β-adrenergic receptors in reconstituted phospholipid vesicles. J Biol Chem 259: 9351-9354, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 9351-9354
    • Asano, T.1    Katada, T.2    Gilman, A.G.3    Ross, E.M.4
  • 36
    • 0028168350 scopus 로고
    • 2A-adrenergic receptor to multiple G-proteins. A simple approach for estimating receptor-G-protein coupling efficiency in a transient expression system
    • 2A-adrenergic receptor to multiple G-proteins. A simple approach for estimating receptor-G-protein coupling efficiency in a transient expression system. J Biol Chem 269: 5730-5734, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 5730-5734
    • Chabre, O.1    Conklin, B.R.2    Brandon, S.3    Bourne, H.R.4    Limbird, L.E.5
  • 42
    • 0022002472 scopus 로고
    • Reconstitution of resolved muscarinic cholinergic receptors with purified GTP-binding proteins
    • Florio VA and Sternweis PC, Reconstitution of resolved muscarinic cholinergic receptors with purified GTP-binding proteins. J Biol Chem 260: 3477-3483, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 3477-3483
    • Florio, V.A.1    Sternweis, P.C.2
  • 43
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG, G proteins: Transducers of receptor-generated signals. Annu Rev Biochem 56: 615-649, 1987.
    • (1987) Annu Rev Biochem , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 44
    • 0022824304 scopus 로고
    • G proteins: A family of signal transducers
    • Stryer L and Bourne HR, G proteins: A family of signal transducers. Annu Rev Cell Biol 2: 391-419, 1986.
    • (1986) Annu Rev Cell Biol , vol.2 , pp. 391-419
    • Stryer, L.1    Bourne, H.R.2
  • 45
    • 0021342922 scopus 로고
    • The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Subunit dissociation and guanine nucleotide-dependent hormonal inhibition
    • Katada T, Northup JK, Bokoch GM, Ui M and Gilman AG, The inhibitory guanine nucleotide-binding regulatory component of adenylate cyclase. Subunit dissociation and guanine nucleotide-dependent hormonal inhibition. J Biol Chem 259: 3578-3585, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 3578-3585
    • Katada, T.1    Northup, J.K.2    Bokoch, G.M.3    Ui, M.4    Gilman, A.G.5
  • 47
    • 0342268914 scopus 로고
    • i and/or βγ
    • Eds. Dickey BF and Birnbaumer L. Springer, Berlin
    • i and/or βγ. In: GTPases in Biology II (Eds. Dickey BF and Birnbaumer L), pp. 417-428. Springer, Berlin, 1993.
    • (1993) GTPases in Biology II , pp. 417-428
    • Hildebrandt, J.D.1
  • 48
    • 0026418426 scopus 로고
    • Type-specific regulation of adenylyl cyclase by G protein βγ subunits
    • Tang W and Gilman AG, Type-specific regulation of adenylyl cyclase by G protein βγ subunits. Science 254: 1500-1503, 1991.
    • (1991) Science , vol.254 , pp. 1500-1503
    • Tang, W.1    Gilman, A.G.2
  • 50
    • 0027232606 scopus 로고
    • s-stimulated adenylyl cyclases
    • s-stimulated adenylyl cyclases. FASEB J 7: 768-775, 1993.
    • (1993) FASEB J , vol.7 , pp. 768-775
    • Iyengar, R.1
  • 51
    • 0028949133 scopus 로고
    • Adenylyl cyclases and the interaction between calcium and cAMP signalling
    • Cooper DMF, Mons N and Karpen JW, Adenylyl cyclases and the interaction between calcium and cAMP signalling. Nature 374: 421-424, 1995.
    • (1995) Nature , vol.374 , pp. 421-424
    • Cooper, D.M.F.1    Mons, N.2    Karpen, J.W.3
  • 52
    • 0028838122 scopus 로고
    • Mammalian membrane bound adenylyl cyclases
    • Taussig R and Gilman AG, Mammalian membrane bound adenylyl cyclases. J Biol Chem 270: 1-4, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 1-4
    • Taussig, R.1    Gilman, A.G.2
  • 55
    • 0020527915 scopus 로고
    • A nucleotide regulatory site for somatostatin inhibition of adenylate cyclase in S49 lymphoma cells
    • Jakobs KH, Aktories K and Schultz G, A nucleotide regulatory site for somatostatin inhibition of adenylate cyclase in S49 lymphoma cells. Nature 303: 177-178, 1983.
    • (1983) Nature , vol.303 , pp. 177-178
    • Jakobs, K.H.1    Aktories, K.2    Schultz, G.3
  • 57
    • 0025329903 scopus 로고
    • Hormone inhibition of adenylyl cyclase. Differences in the mechanisms for inhibition by hormones and G protein βγ
    • Hildebrandt JD and Kohnken RE, Hormone inhibition of adenylyl cyclase. Differences in the mechanisms for inhibition by hormones and G protein βγ. J Biol Chem 265: 9825-9830, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 9825-9830
    • Hildebrandt, J.D.1    Kohnken, R.E.2
  • 60
    • 0023645429 scopus 로고
    • A novel mechanism for the inhibition of adenylate cyclase via inhibitory GTP-binding proteins. Calmodulin-dependent inhibition of the cyclase catalyst by the βγ-subunits of GTP-binding proteins
    • Katada T, Kusakabe K, Oinuma M and Ui M, A novel mechanism for the inhibition of adenylate cyclase via inhibitory GTP-binding proteins. Calmodulin-dependent inhibition of the cyclase catalyst by the βγ-subunits of GTP-binding proteins. J Biol Chem 262: 11897-11900, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 11897-11900
    • Katada, T.1    Kusakabe, K.2    Oinuma, M.3    Ui, M.4
  • 61
    • 0023355659 scopus 로고
    • 2 activity in bovine rod outer segments by the βγ subunits of transducin and its inhibition by the α subunit
    • 2 activity in bovine rod outer segments by the βγ subunits of transducin and its inhibition by the α subunit. Proc Natl Acad Sci USA 84: 3623-3627, 1987.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3623-3627
    • Jelsema, C.L.1    Axelrod, J.2
  • 63
    • 0027068060 scopus 로고
    • Receptor-to-effector signalling through G proteins: Roles for βγ dimers as well as α subunits
    • Birnbaumer L, Receptor-to-effector signalling through G proteins: Roles for βγ dimers as well as α subunits. Cell 71: 1069-1072, 1992.
    • (1992) Cell , vol.71 , pp. 1069-1072
    • Birnbaumer, L.1
  • 65
    • 0027495684 scopus 로고
    • New roles for G protein βγ dimers in transmembrane signalling
    • Clapham DE and Neer EJ, New roles for G protein βγ dimers in transmembrane signalling. Nature 365: 403-406, 1993.
    • (1993) Nature , vol.365 , pp. 403-406
    • Clapham, D.E.1    Neer, E.J.2
  • 66
    • 0028177677 scopus 로고
    • The active role of βγ in signal transduction
    • Sternweis PC, The active role of βγ in signal transduction. Curr Opin Cell Biol 6: 198-203, 1994.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 198-203
    • Sternweis, P.C.1
  • 67
    • 0028912416 scopus 로고
    • The role of G protein βγ subunits in signal transduction
    • Muller S and Lohse MJ, The role of G protein βγ subunits in signal transduction. Biochem Soc Trans 23: 141-145, 1995.
    • (1995) Biochem Soc Trans , vol.23 , pp. 141-145
    • Muller, S.1    Lohse, M.J.2
  • 68
    • 0028176297 scopus 로고
    • cAMP and βγ subunits of heterotrimeric G proteins stimulate the mitogen activated protein kinase pathway in COS-7 cells
    • Faure M, Yoyno-Yasenetskaya TA and Bourne HR, cAMP and βγ subunits of heterotrimeric G proteins stimulate the mitogen activated protein kinase pathway in COS-7 cells. J Biol Chem 269: 7851-7854, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 7851-7854
    • Faure, M.1    Yoyno-Yasenetskaya, T.A.2    Bourne, H.R.3
  • 70
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits
    • Crespo P, Xu N, Simonds WF and Gutkind JS, Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits. Nature 369: 418-420, 1994.
    • (1994) Nature , vol.369 , pp. 418-420
    • Crespo, P.1    Xu, N.2    Simonds, W.F.3    Gutkind, J.S.4
  • 71
    • 0022497334 scopus 로고
    • Pertussis toxin alters the growth characteristics of Swiss 3T3 cells
    • Hildebrandt JD, Stolzenberg E and Graves J, Pertussis toxin alters the growth characteristics of Swiss 3T3 cells. FEBS Lett 203: 87-90, 1986.
    • (1986) FEBS Lett , vol.203 , pp. 87-90
    • Hildebrandt, J.D.1    Stolzenberg, E.2    Graves, J.3
  • 72
    • 0023010517 scopus 로고
    • Pertussis toxin-sensitive pathway in the stimulation of c-myc expression and DNA synthesis by bombesin
    • Letterio JJ, Coughlin SR and Williams LT, Pertussis toxin-sensitive pathway in the stimulation of c-myc expression and DNA synthesis by bombesin. Science 234: 1117-1119, 1986.
    • (1986) Science , vol.234 , pp. 1117-1119
    • Letterio, J.J.1    Coughlin, S.R.2    Williams, L.T.3
  • 73
    • 0023656163 scopus 로고
    • Possible involvement of a GTP-binding protein, the substrate of islet-activating protein, in receptor-mediated signaling responsible for cell proliferation
    • Murayama T and Ui M, Possible involvement of a GTP-binding protein, the substrate of islet-activating protein, in receptor-mediated signaling responsible for cell proliferation. J Biol Chem 262: 12463-12467, 1987.
    • (1987) J Biol Chem , vol.262 , pp. 12463-12467
    • Murayama, T.1    Ui, M.2
  • 74
    • 0027104056 scopus 로고
    • Mitogenic pathways regulated by G protein oncogenes
    • Gupta SK, Gallego C and Johnson GL, Mitogenic pathways regulated by G protein oncogenes. Mol Biol Cell 3: 123-128, 1992.
    • (1992) Mol Biol Cell , vol.3 , pp. 123-128
    • Gupta, S.K.1    Gallego, C.2    Johnson, G.L.3
  • 75
    • 0024614795 scopus 로고
    • The cyclic AMP-mediated stimulation of cell proliferation
    • Dumont JE, Jauniaux JC and Roger PP, The cyclic AMP-mediated stimulation of cell proliferation. Trends Biochem Sci 14: 67-71, 1989.
    • (1989) Trends Biochem Sci , vol.14 , pp. 67-71
    • Dumont, J.E.1    Jauniaux, J.C.2    Roger, P.P.3
  • 77
    • 0030047730 scopus 로고    scopus 로고
    • Gating by cyclic AMP: Expanded role for an old signalling pathway
    • Iyengar R, Gating by cyclic AMP: Expanded role for an old signalling pathway. Science 271: 461-463, 1996.
    • (1996) Science , vol.271 , pp. 461-463
    • Iyengar, R.1
  • 78
    • 0029815128 scopus 로고    scopus 로고
    • Interplay between Ras-related and heterotrimeric GTP binding proteins: Lifestyles of the BIG and little
    • Bokoch GM, Interplay between Ras-related and heterotrimeric GTP binding proteins: Lifestyles of the BIG and little. FASEB J 10: 1290-1295, 1996.
    • (1996) FASEB J , vol.10 , pp. 1290-1295
    • Bokoch, G.M.1
  • 79
    • 0029002493 scopus 로고
    • A direct interaction between G-protein βγ and the Raf-1 protein kinase
    • Pumiglia KM, LeVine H, Haske T, Habib T, Jove R and Decker SJ, A direct interaction between G-protein βγ and the Raf-1 protein kinase. J Biol Chem 270: 14251-14254, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 14251-14254
    • Pumiglia, K.M.1    LeVine, H.2    Haske, T.3    Habib, T.4    Jove, R.5    Decker, S.J.6
  • 80
    • 0028896344 scopus 로고
    • Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits
    • Langhans-Rajasekaran SA, Wan Y and Huang X-Y, Activation of Tsk and Btk tyrosine kinases by G protein βγ subunits. Proc Natl Acad Sci USA 92: 8601-8605, 1995.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 8601-8605
    • Langhans-Rajasekaran, S.A.1    Wan, Y.2    Huang, X.-Y.3
  • 81
    • 0028982925 scopus 로고
    • G βγ subunits mediate mitogen-activated protein kinase activation by the tyrosine kinase insulin-like growth factor 1 receptor
    • Luttrell LM, van Biesen T, Hawes BE, Koch WJ, Touhara K and Lefkowitz RJ, G βγ subunits mediate mitogen-activated protein kinase activation by the tyrosine kinase insulin-like growth factor 1 receptor. J Biol Chem 270: 16495-16498, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 16495-16498
    • Luttrell, L.M.1    Van Biesen, T.2    Hawes, B.E.3    Koch, W.J.4    Touhara, K.5    Lefkowitz, R.J.6
  • 83
    • 0030614911 scopus 로고    scopus 로고
    • Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation
    • Luttrell LM, Della Rocca GJ, van Biesen T, Luttrell DK and Lefkowitz RJ, Gβγ subunits mediate Src-dependent phosphorylation of the epidermal growth factor receptor. A scaffold for G protein-coupled receptor-mediated Ras activation. J Biol Chem 272: 4637-4644, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 4637-4644
    • Luttrell, L.M.1    Della Rocca, G.J.2    Van Biesen, T.3    Luttrell, D.K.4    Lefkowitz, R.J.5
  • 84
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI3 kinase-γ
    • Lopez-Ilasaca M, Crespo P, Pellici PP, Gutkind JS and Wetzker R, Linkage of G protein-coupled receptors to the MAPK signaling pathway through PI3 kinase-γ. Science 275: 394-397, 1997.
    • (1997) Science , vol.275 , pp. 394-397
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.P.3    Gutkind, J.S.4    Wetzker, R.5
  • 85
    • 0031031046 scopus 로고    scopus 로고
    • Integration hot-spot gets hotter
    • Dunlap K, Integration hot-spot gets hotter. Nature 385: 395-397, 1997.
    • (1997) Nature , vol.385 , pp. 395-397
    • Dunlap, K.1
  • 87
    • 0029921401 scopus 로고    scopus 로고
    • Voltage dependent modulation of B type calcium channels by G protein βγ subunits
    • Ikeda SR, Voltage dependent modulation of B type calcium channels by G protein βγ subunits. Nature 380: 255-258, 1996.
    • (1996) Nature , vol.380 , pp. 255-258
    • Ikeda, S.R.1
  • 89
    • 0031033757 scopus 로고    scopus 로고
    • Direct binding of G protein βγ complex to voltage dependent calcium channels
    • De Waard M, Liu H, Walker D, Scott VES, Gurnett CA and Campbell KP, Direct binding of G protein βγ complex to voltage dependent calcium channels. Nature 385: 446-450, 1997.
    • (1997) Nature , vol.385 , pp. 446-450
    • De Waard, M.1    Liu, H.2    Walker, D.3    Scott, V.E.S.4    Gurnett, C.A.5    Campbell, K.P.6
  • 92
    • 0026803223 scopus 로고
    • G protein-coupled mechanisms and nervous signaling
    • Hille B, G protein-coupled mechanisms and nervous signaling. Neuron 9: 187-195, 1992.
    • (1992) Neuron , vol.9 , pp. 187-195
    • Hille, B.1
  • 94
    • 0028133063 scopus 로고
    • Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases
    • Taussig R, Tang W-J, Hepler JR and Gilman AG, Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases. J Biol Chem 269: 6093-6100, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 6093-6100
    • Taussig, R.1    Tang, W.-J.2    Hepler, J.R.3    Gilman, A.G.4
  • 95
    • 0021748090 scopus 로고
    • Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain
    • Sternweis PC and Robishaw JD, Isolation of two proteins with high affinity for guanine nucleotides from membranes of bovine brain. J Biol Chem 259: 13806-13813, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 13806-13813
    • Sternweis, P.C.1    Robishaw, J.D.2
  • 96
    • 0021683990 scopus 로고
    • Purification and properties of the inhibitory guanine nucleotide regulatory unit of brain adenylate cyclase
    • Neer EJ, Lok JM and Wolf LG, Purification and properties of the inhibitory guanine nucleotide regulatory unit of brain adenylate cyclase. J Biol Chem 259: 14222-14229, 1984.
    • (1984) J Biol Chem , vol.259 , pp. 14222-14229
    • Neer, E.J.1    Lok, J.M.2    Wolf, L.G.3
  • 101
    • 0024966029 scopus 로고
    • The STE4 and STE18 genes of yeast encode potential β and γ subunits of the mating factor receptor-coupled G protein
    • Whiteway M, Hougan L, Dignard D, Thomas DY, Bell L, Saari GC, Grant FJ, O'Hara P and MacKay VL, The STE4 and STE18 genes of yeast encode potential β and γ subunits of the mating factor receptor-coupled G protein. Cell 56: 467-477, 1989.
    • (1989) Cell , vol.56 , pp. 467-477
    • Whiteway, M.1    Hougan, L.2    Dignard, D.3    Thomas, D.Y.4    Bell, L.5    Saari, G.C.6    Grant, F.J.7    O'Hara, P.8    MacKay, V.L.9
  • 102
    • 0025285275 scopus 로고
    • Pheromone response in yeast
    • Fields S, Pheromone response in yeast. Trends Biochem Sci 15: 270-273, 1990.
    • (1990) Trends Biochem Sci , vol.15 , pp. 270-273
    • Fields, S.1
  • 106
    • 0026676807 scopus 로고
    • 2 isoform of phospholipase C
    • 2 isoform of phospholipase C. Nature 360: 686-689, 1992.
    • (1992) Nature , vol.360 , pp. 686-689
    • Katz, A.1    Wu, D.2    Simon, M.I.3
  • 108
    • 0026497034 scopus 로고
    • βγ Subunit activation of G protein regulated phospholipase C
    • Boyer JL, Waldo GL and Harden TK, βγ Subunit activation of G protein regulated phospholipase C. J Biol Chem 267: 25451-25456, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 25451-25456
    • Boyer, J.L.1    Waldo, G.L.2    Harden, T.K.3
  • 112
    • 0028178715 scopus 로고
    • A G protein βγ subunit responsive phosphoinositide 3 kinase activity in human platelet cytosol
    • Thomason PA, James SR, Casey PJ and Downes CP, A G protein βγ subunit responsive phosphoinositide 3 kinase activity in human platelet cytosol. J Biol Chem 269: 16525-16528, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 16525-16528
    • Thomason, P.A.1    James, S.R.2    Casey, P.J.3    Downes, C.P.4
  • 113
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid derived cells is activated by G protein βγ subunits
    • Stephens L, Smrcka A, Cooke FT, Jackson TR, Sternweis PC and Hawkins PT, A novel phosphoinositide 3 kinase activity in myeloid derived cells is activated by G protein βγ subunits. Cell 77: 83-93, 1994.
    • (1994) Cell , vol.77 , pp. 83-93
    • Stephens, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.R.4    Sternweis, P.C.5    Hawkins, P.T.6
  • 114
    • 0025184011 scopus 로고
    • Differential regulation of G protein subunit expression in mouse oocytes, eggs, and early embryos
    • Allworth AE, Hildebrandt JD and Ziomek CA, Differential regulation of G protein subunit expression in mouse oocytes, eggs, and early embryos. Dev Biol 142: 129-137, 1990.
    • (1990) Dev Biol , vol.142 , pp. 129-137
    • Allworth, A.E.1    Hildebrandt, J.D.2    Ziomek, C.A.3
  • 115
    • 0024603356 scopus 로고
    • Pertussis toxin treatment in vivo is associated with a decline in G-protein β-subunits
    • Watkins DC, Northup JK and Malbon CC, Pertussis toxin treatment in vivo is associated with a decline in G-protein β-subunits. J Biol Chem 264: 4186-4194, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 4186-4194
    • Watkins, D.C.1    Northup, J.K.2    Malbon, C.C.3
  • 123
    • 0025924179 scopus 로고
    • oα mRNA arise by alternative splicing of transcripts from a single gene on human chromosome 16
    • oα mRNA arise by alternative splicing of transcripts from a single gene on human chromosome 16. Mol Cell Biol 11: 1146-1155, 1991.
    • (1991) Mol Cell Biol , vol.11 , pp. 1146-1155
    • Murtagh, J.J.1    Eddy, R.2    Shows, T.B.3    Moss, J.4    Vaughan, M.5
  • 125
    • 0023084055 scopus 로고
    • Progressive sequence alignment as a prerequisite to correct physiologic trees
    • Feng D-F and Doolittle RF, Progressive sequence alignment as a prerequisite to correct physiologic trees. J Mol Evol 25: 351-360, 1987.
    • (1987) J Mol Evol , vol.25 , pp. 351-360
    • Feng, D.-F.1    Doolittle, R.F.2
  • 126
    • 0024598146 scopus 로고
    • Fast and sensitive multiple sequence alignments on a microcomputer
    • Higgins DG and Sharp PM, Fast and sensitive multiple sequence alignments on a microcomputer. Comput Appl Biosci 5: 151-153, 1989.
    • (1989) Comput Appl Biosci , vol.5 , pp. 151-153
    • Higgins, D.G.1    Sharp, P.M.2
  • 127
    • 0021760092 scopus 로고
    • A comprehensive set of sequence analysis programs for the VAX
    • Devereux J, Haeberli P and Smithies O, A comprehensive set of sequence analysis programs for the VAX. Nucleic Acids Res 12: 387-395, 1984.
    • (1984) Nucleic Acids Res , vol.12 , pp. 387-395
    • Devereux, J.1    Haeberli, P.2    Smithies, O.3
  • 128
    • 0026699257 scopus 로고
    • Phylogeny and evolutionary rates of G protein α subunit genes
    • Yokoyama S and Starmer WT, Phylogeny and evolutionary rates of G protein α subunit genes. J Mol Evol 35: 230-238, 1992.
    • (1992) J Mol Evol , vol.35 , pp. 230-238
    • Yokoyama, S.1    Starmer, W.T.2
  • 130
    • 0024721654 scopus 로고
    • α Transducin is present in blue-, green-, and red-sensitive cone photoreceptors in the human retina
    • Lerea CL, Bunt Milam AH and Hurley JB, α Transducin is present in blue-, green-, and red-sensitive cone photoreceptors in the human retina. Neuron 3: 367-376, 1989.
    • (1989) Neuron , vol.3 , pp. 367-376
    • Lerea, C.L.1    Bunt Milam, A.H.2    Hurley, J.B.3
  • 133
    • 0022996122 scopus 로고
    • Molecular basis for two forms of the G protein that stimulates adenylate cyclase
    • Robishaw JD, Smigel MD and Gilman AG, Molecular basis for two forms of the G protein that stimulates adenylate cyclase. J Biol Chem 261: 9587-9590, 1986.
    • (1986) J Biol Chem , vol.261 , pp. 9587-9590
    • Robishaw, J.D.1    Smigel, M.D.2    Gilman, A.G.3
  • 136
    • 0028177082 scopus 로고
    • i2 to the Golgi by alternative spliced carboxyl-terminal region
    • i2 to the Golgi by alternative spliced carboxyl-terminal region. Science 263: 95-98, 1994.
    • (1994) Science , vol.263 , pp. 95-98
    • Montmayeur, J.-P.1    Borrelli, E.2
  • 138
    • 0027056925 scopus 로고
    • Selective tissue distribution of G protein γ subunits, including a new form of γ subunit identified by cDNA cloning
    • Cali JJ, Balcueva EA, Rybalkin I and Robishaw JD, Selective tissue distribution of G protein γ subunits, including a new form of γ subunit identified by cDNA cloning. J Biol Chem 267: 24023-24027, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 24023-24027
    • Cali, J.J.1    Balcueva, E.A.2    Rybalkin, I.3    Robishaw, J.D.4
  • 139
    • 0024475378 scopus 로고
    • olf: An olfactory neuron specific-G protein involved in odorant signal transduction
    • olf: An olfactory neuron specific-G protein involved in odorant signal transduction. Science 244: 790-795, 1989.
    • (1989) Science , vol.244 , pp. 790-795
    • Jones, D.T.1    Reed, R.R.2
  • 140
    • 0022993799 scopus 로고
    • Identification of specific transducin α subunits in retinal rod and cone photoreceptors
    • Lerea CL, Somers DE, Hurley JB, Klock IB and Bunt Milam AH, Identification of specific transducin α subunits in retinal rod and cone photoreceptors. Science 234: 77-80, 1986.
    • (1986) Science , vol.234 , pp. 77-80
    • Lerea, C.L.1    Somers, D.E.2    Hurley, J.B.3    Klock, I.B.4    Bunt Milam, A.H.5
  • 141
    • 0026718951 scopus 로고
    • Gustducin is a taste-cell-specific G protein closely related to the transducins
    • McLaughlin SK, McKinnon PJ and Margolskee RF, Gustducin is a taste-cell-specific G protein closely related to the transducins. Nature 357: 563-569, 1992.
    • (1992) Nature , vol.357 , pp. 563-569
    • McLaughlin, S.K.1    McKinnon, P.J.2    Margolskee, R.F.3
  • 142
    • 0026472131 scopus 로고
    • Retinal rods and cones have distinct G protein β and γ subunits
    • Peng YY, Robishaw JD, Levine MA and Yau KW, Retinal rods and cones have distinct G protein β and γ subunits. Proc Natl Acad Sci USA 89: 10882-10886, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 10882-10886
    • Peng, Y.Y.1    Robishaw, J.D.2    Levine, M.A.3    Yau, K.W.4
  • 143
    • 0028932506 scopus 로고
    • Molecular cloning and characterization of the G protein γ subunit of cone photoreceptors
    • Ong O, Yamane HK, Phan KB, Fong HKW, Bok D, Lee RH and Fung BK, Molecular cloning and characterization of the G protein γ subunit of cone photoreceptors. J Biol Chem 270: 8495-8500, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 8495-8500
    • Ong, O.1    Yamane, H.K.2    Phan, K.B.3    Fong, H.K.W.4    Bok, D.5    Lee, R.H.6    Fung, B.K.7
  • 144
    • 0028939993 scopus 로고
    • A novel GTP-binding protein γ-subunit, Gγ8, is expressed during neurogenesis in the olfactory and vomeronasal neuroepithelia
    • Ryba NJP and Tirindelli R, A novel GTP-binding protein γ-subunit, Gγ8, is expressed during neurogenesis in the olfactory and vomeronasal neuroepithelia. J Biol Chem 270: 6757-6767, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 6757-6767
    • Ryba, N.J.P.1    Tirindelli, R.2
  • 145
    • 0026655342 scopus 로고
    • Interaction between G protein β and γ subunit types is selective
    • Pronin AN and Gautam N, Interaction between G protein β and γ subunit types is selective. Proc Natl Acad Sci USA 89: 6220-6224, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 6220-6224
    • Pronin, A.N.1    Gautam, N.2
  • 146
    • 0026655036 scopus 로고
    • Specificity of G protein β and γ subunit interactions
    • Schmidt CJ, Thomas TC, Levine MA and Neer EJ, Specificity of G protein β and γ subunit interactions. J Biol Chem 267: 13807-13810, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 13807-13810
    • Schmidt, C.J.1    Thomas, T.C.2    Levine, M.A.3    Neer, E.J.4
  • 147
    • 0030002944 scopus 로고    scopus 로고
    • Differential ability to form the G protein βγ complex among members of the β and γ subunit families
    • Yan K, Kalyanaraman V and Gautam N, Differential ability to form the G protein βγ complex among members of the β and γ subunit families. J Biol Chem 271: 7141-7146, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 7141-7146
    • Yan, K.1    Kalyanaraman, V.2    Gautam, N.3
  • 150
    • 0027085772 scopus 로고
    • Identification and isolation of common and tissue-specific geranylgeranylated γ subunits of guanine-nucleotide-binding proteins in various tissues
    • Morishita R, Fukada Y, Kokame K, Yoshizawa T, Masuda K, Niwa M, Kato K and Asano T, Identification and isolation of common and tissue-specific geranylgeranylated γ subunits of guanine-nucleotide-binding proteins in various tissues. Eur J Biochem 210: 1061-1069, 1992.
    • (1992) Eur J Biochem , vol.210 , pp. 1061-1069
    • Morishita, R.1    Fukada, Y.2    Kokame, K.3    Yoshizawa, T.4    Masuda, K.5    Niwa, M.6    Kato, K.7    Asano, T.8
  • 151
    • 0026740811 scopus 로고
    • Molecular heterogeneity of the βγ subunits of GTP binding proteins in bovine brain membranes
    • Kontani K, Taksunobu K, Inanobe A, Ui M and Katada T, Molecular heterogeneity of the βγ subunits of GTP binding proteins in bovine brain membranes. Arch Biochem Biophys 294: 527-533, 1992.
    • (1992) Arch Biochem Biophys , vol.294 , pp. 527-533
    • Kontani, K.1    Taksunobu, K.2    Inanobe, A.3    Ui, M.4    Katada, T.5
  • 152
    • 0028031159 scopus 로고
    • Direct interaction of the α and γ subunits of the G proteins. Purification and analysis by limited proteolysis
    • Rahmatullah M and Robishaw JD, Direct interaction of the α and γ subunits of the G proteins. Purification and analysis by limited proteolysis. J Biol Chem 269: 3574-3580, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 3574-3580
    • Rahmatullah, M.1    Robishaw, J.D.2
  • 153
    • 0028870405 scopus 로고
    • Specificity of G protein α-γ subunit interactions: N-terminal 15 amino acids of γ subunit specifies interaction with α subunit
    • Rahmatullah M, Ginnan R and Robishaw JD, Specificity of G protein α-γ subunit interactions: N-terminal 15 amino acids of γ subunit specifies interaction with α subunit. J Biol Chem 270: 2946-2951, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 2946-2951
    • Rahmatullah, M.1    Ginnan, R.2    Robishaw, J.D.3
  • 157
    • 0021079937 scopus 로고
    • Characterization of transducin from bovine retinal rod outer segments. I. Separation and reconstitution of the subunits
    • Fung BK, Characterization of transducin from bovine retinal rod outer segments. I. Separation and reconstitution of the subunits. J Biol Chem 258: 10495-10502, 1983.
    • (1983) J Biol Chem , vol.258 , pp. 10495-10502
    • Fung, B.K.1
  • 158
    • 0024603349 scopus 로고
    • o in reconstituted phospholipid vesicles
    • o in reconstituted phospholipid vesicles. J Biol Chem 264: 3909-3915, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 3909-3915
    • Florio, V.A.1    Sternweis, P.C.2
  • 159
    • 0023697285 scopus 로고
    • Transducin inhibition of light-dependent rhodopsin phosphorylation: Evidence for βγ subunit interaction with rhodopsin
    • Kelleher DJ and Johnson GL, Transducin inhibition of light-dependent rhodopsin phosphorylation: Evidence for βγ subunit interaction with rhodopsin. Mol Pharmacol 34: 452-460, 1988.
    • (1988) Mol Pharmacol , vol.34 , pp. 452-460
    • Kelleher, D.J.1    Johnson, G.L.2
  • 160
    • 0025779113 scopus 로고
    • Rhodopsin and the retinal G-protein distinguish among G-protein βγ subunit forms
    • Fawzi AB, Fay DS, Murphy EA, Tamir H, Erdos JJ and Northup JK, Rhodopsin and the retinal G-protein distinguish among G-protein βγ subunit forms. J Biol Chem 266: 12194-12200, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 12194-12200
    • Fawzi, A.B.1    Fay, D.S.2    Murphy, E.A.3    Tamir, H.4    Erdos, J.J.5    Northup, J.K.6
  • 161
    • 0027435265 scopus 로고
    • Specific interaction with rhodopsin is dependent on the γ subunit type in a G protein
    • Kisselev O and Gautam N, Specific interaction with rhodopsin is dependent on the γ subunit type in a G protein. J Biol Chem 268: 24519-24522, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 24519-24522
    • Kisselev, O.1    Gautam, N.2
  • 162
    • 0029746261 scopus 로고    scopus 로고
    • Role of the prenyl group on the G protein γ subunit in coupling trimeric G proteins to A1 adenosine receptors
    • Yasuda H, Lindorfer MA, Woodfork KA, Fletcher JE and Garrison JC, Role of the prenyl group on the G protein γ subunit in coupling trimeric G proteins to A1 adenosine receptors. J Biol Chem 271: 18588-18595, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 18588-18595
    • Yasuda, H.1    Lindorfer, M.A.2    Woodfork, K.A.3    Fletcher, J.E.4    Garrison, J.C.5
  • 164
    • 0025441553 scopus 로고
    • β and γ subunits of a yeast guanine nucleotide binding protein are not essential for membrane association of the α subunit but are required for receptor coupling
    • Blumer KJ and Thorner J, β and γ Subunits of a yeast guanine nucleotide binding protein are not essential for membrane association of the α subunit but are required for receptor coupling. Proc Natl Acad Sci USA 87: 4363-4367, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4363-4367
    • Blumer, K.J.1    Thorner, J.2
  • 165
    • 0026319547 scopus 로고
    • o: Assay using recombinant α subunits in reconstituted phospholipid vesicles
    • o: Assay using recombinant α subunits in reconstituted phospholipid vesicles. Biochemistry 30: 10769-10777, 1991.
    • (1991) Biochemistry , vol.30 , pp. 10769-10777
    • Rubenstein, R.C.1    Linder, M.E.2    Ross, E.M.3
  • 166
    • 0026786080 scopus 로고
    • Rhodopsin/transducin interactions: I. Characterization of the binding of the transducin βγ complex to rhodopsin using fluorescence spectrometry
    • Phillips WJ and Cerione RA, Rhodopsin/transducin interactions: I. Characterization of the binding of the transducin βγ complex to rhodopsin using fluorescence spectrometry. J Biol Chem 267: 17032-17039, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 17032-17039
    • Phillips, W.J.1    Cerione, R.A.2
  • 169
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites on Gβ. A receptor-derived peptide binds to the carboxyl terminus
    • Taylor JM, Jacoh-Mosier GG, Lawton RG, VanDort M and Neubig RR, Receptor and membrane interaction sites on Gβ. A receptor-derived peptide binds to the carboxyl terminus. J Biol Chem 271: 3336-3339, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 3336-3339
    • Taylor, J.M.1    Jacoh-Mosier, G.G.2    Lawton, R.G.3    VanDort, M.4    Neubig, R.R.5
  • 170
    • 0026005355 scopus 로고
    • Identification of the subunits of GTP binding proteins coupled to somatostatin receptors
    • Law SF, Manning D and Reisine T, Identification of the subunits of GTP binding proteins coupled to somatostatin receptors. J Biol Chem 266: 17885-17897, 1991.
    • (1991) J Biol Chem , vol.266 , pp. 17885-17897
    • Law, S.F.1    Manning, D.2    Reisine, T.3
  • 171
    • 0023100824 scopus 로고
    • Production of antibodies against rhodopsin after immunization with βγ-subunits of transducin: Evidence for interaction of βγ-subunits of guanosine 5′-triphosphate binding proteins with receptor
    • Halpern JL, Chang PP, Tsai SC, Adamik R, Kanaho Y, Sohn R, Moss J and Vaughan M, Production of antibodies against rhodopsin after immunization with βγ-subunits of transducin: Evidence for interaction of βγ-subunits of guanosine 5′-triphosphate binding proteins with receptor. Biochemistry 26: 1655-1658, 1987.
    • (1987) Biochemistry , vol.26 , pp. 1655-1658
    • Halpern, J.L.1    Chang, P.P.2    Tsai, S.C.3    Adamik, R.4    Kanaho, Y.5    Sohn, R.6    Moss, J.7    Vaughan, M.8
  • 172
    • 0025880464 scopus 로고
    • Assignment of G protein subtypes to specific receptors inducing inhibition of calcium currents
    • Kleuss C, Hescheler J, Ewel C, Rosenthal W, Schultz G and Wittig B, Assignment of G protein subtypes to specific receptors inducing inhibition of calcium currents. Nature 353: 43-48, 1991.
    • (1991) Nature , vol.353 , pp. 43-48
    • Kleuss, C.1    Hescheler, J.2    Ewel, C.3    Rosenthal, W.4    Schultz, G.5    Wittig, B.6
  • 173
    • 0026752495 scopus 로고
    • Different β-subunits determine G protein interaction with transmembrane receptors
    • Kleuss C, Scherubl H, Herscheler J, Schultz G and Wittig B, Different β-subunits determine G protein interaction with transmembrane receptors. Nature 358: 424-426, 1992.
    • (1992) Nature , vol.358 , pp. 424-426
    • Kleuss, C.1    Scherubl, H.2    Herscheler, J.3    Schultz, G.4    Wittig, B.5
  • 174
    • 0027530916 scopus 로고
    • Selectivity in signal transduction determined by γ subunits of heterotrimeric G proteins
    • Kleuss C, Scherubl H, Hescheler J, Schultz G and Wittig B, Selectivity in signal transduction determined by γ subunits of heterotrimeric G proteins. Science 259: 832-834, 1993.
    • (1993) Science , vol.259 , pp. 832-834
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 175
    • 0030575941 scopus 로고    scopus 로고
    • Specificity of interaction between receptor and G protein: Use of antisense techniques to relate G protein subunits to function
    • Kalkbrenner F, Dippel E, Wittig B and Schultz G, Specificity of interaction between receptor and G protein: Use of antisense techniques to relate G protein subunits to function. Biochim Biophys Acta 1314: 125-139, 1996.
    • (1996) Biochim Biophys Acta , vol.1314 , pp. 125-139
    • Kalkbrenner, F.1    Dippel, E.2    Wittig, B.3    Schultz, G.4
  • 177
    • 0029670735 scopus 로고    scopus 로고
    • 2+ currents by somatostatin in cultured ovine somatotrophs
    • 2+ currents by somatostatin in cultured ovine somatotrophs. J Physiol (Lond) 491: 21-29, 1996.
    • (1996) J Physiol (Lond) , vol.491 , pp. 21-29
    • Chen, C.1    Clarke, I.J.2
  • 180
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig RR, Membrane organization in G-protein mechanisms. FASEB J 8: 939-946, 1994.
    • (1994) FASEB J , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 181
    • 0024986794 scopus 로고
    • Specific associations between tubulin and G proteins: Participation of cytoskeletal elements in cellular signal transduction
    • Rasenick MM, Wang N and Yan K, Specific associations between tubulin and G proteins: Participation of cytoskeletal elements in cellular signal transduction. Adv Second Messenger Phosphoprotein Res 24: 381-386, 1990.
    • (1990) Adv Second Messenger Phosphoprotein Res , vol.24 , pp. 381-386
    • Rasenick, M.M.1    Wang, N.2    Yan, K.3
  • 182
    • 0030265643 scopus 로고    scopus 로고
    • G proteins: Out of the cytoskeletal closet
    • Rodbell M, G proteins: Out of the cytoskeletal closet. Mt Sinai J Med 63: 381-386, 1996.
    • (1996) Mt Sinai J Med , vol.63 , pp. 381-386
    • Rodbell, M.1
  • 183
    • 0026095719 scopus 로고
    • The regulation of adenylyl cyclase by receptor-operated G proteins
    • Levitzki A and Bar-Sinai A, The regulation of adenylyl cyclase by receptor-operated G proteins. Pharmacol Ther 50: 271-283, 1991.
    • (1991) Pharmacol Ther , vol.50 , pp. 271-283
    • Levitzki, A.1    Bar-Sinai, A.2
  • 184
    • 0028792376 scopus 로고
    • Identification of structural elements involved in G protein gating of the GIRK1 potassium channel
    • Slesinger PA, Reuveny E, Jan YN and Jan LY, Identification of structural elements involved in G protein gating of the GIRK1 potassium channel. Neuron 15: 1145-1156, 1995.
    • (1995) Neuron , vol.15 , pp. 1145-1156
    • Slesinger, P.A.1    Reuveny, E.2    Jan, Y.N.3    Jan, L.Y.4
  • 185
    • 0028093624 scopus 로고
    • A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling
    • Kisselev OG, Ermolaeva MV and Gautam N, A farnesylated domain in the G protein γ subunit is a specific determinant of receptor coupling. J Biol Chem 269: 21399-21402, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 21399-21402
    • Kisselev, O.G.1    Ermolaeva, M.V.2    Gautam, N.3
  • 189
    • 0028351930 scopus 로고
    • Lipid modifications of G proteins
    • Casey PJ, Lipid modifications of G proteins. Curr Opin Cell Biol 6: 219-225, 1994.
    • (1994) Curr Opin Cell Biol , vol.6 , pp. 219-225
    • Casey, P.J.1
  • 190
    • 0028935780 scopus 로고
    • Protein lipidation in cell signaling
    • Casey PJ, Protein lipidation in cell signaling. Science 268: 221-225, 1995.
    • (1995) Science , vol.268 , pp. 221-225
    • Casey, P.J.1
  • 192
  • 194
    • 0027340389 scopus 로고
    • s protein α subunit after activation by the β-adrenergic receptor or cholera toxin
    • s protein α subunit after activation by the β-adrenergic receptor or cholera toxin. J Biol Chem 268: 23769-23772, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 23769-23772
    • Degtyarev, M.Y.1    Spiegel, A.M.2    Jones, T.L.Z.3
  • 195
    • 0026735063 scopus 로고
    • Protein isoprenylation and methylation at carboxyl-terminal cysteine residues
    • Clarke S, Protein isoprenylation and methylation at carboxyl-terminal cysteine residues. Annu Rev Biochem 61: 355-386, 1992.
    • (1992) Annu Rev Biochem , vol.61 , pp. 355-386
    • Clarke, S.1
  • 197
    • 0025090885 scopus 로고
    • Carboxyl methylation and COOH-terminal processing of the brain G protein γ subunit
    • Backlund PS Jr, Simonds WF and Spiegel AM, Carboxyl methylation and COOH-terminal processing of the brain G protein γ subunit. J Biol Chem 265: 15572-15576, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 15572-15576
    • Backlund P.S., Jr.1    Simonds, W.F.2    Spiegel, A.M.3
  • 198
    • 0025992099 scopus 로고
    • Carboxyl methylation and farnesylation of transducin γ subunit synergistically enhance its coupling with metarhodopsin II
    • Ohguro H, Fulada Y, Takao T, Shimonishi Y, Yoshizawa T and Akino T, Carboxyl methylation and farnesylation of transducin γ subunit synergistically enhance its coupling with metarhodopsin II. EMBO J 10: 3669-3674, 1991.
    • (1991) EMBO J , vol.10 , pp. 3669-3674
    • Ohguro, H.1    Fulada, Y.2    Takao, T.3    Shimonishi, Y.4    Yoshizawa, T.5    Akino, T.6
  • 199
    • 0027249015 scopus 로고
    • Purification of four forms of the βγ subunit complex of G proteins containing different γ subunits
    • Asano T, Morishita R, Fukada Y, Yoshizawa T and Kato K, Purification of four forms of the βγ subunit complex of G proteins containing different γ subunits. J Biol Chem 268: 20512-20519, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 20512-20519
    • Asano, T.1    Morishita, R.2    Fukada, Y.3    Yoshizawa, T.4    Kato, K.5
  • 200
    • 0028845341 scopus 로고
    • Efficient interaction with a receptor requires a specific type of prenyl group on the G protein γ subunit
    • Kisselev O, Ermolaeva M and Gautam N, Efficient interaction with a receptor requires a specific type of prenyl group on the G protein γ subunit. J Biol Chem 270: 25356-25358, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 25356-25358
    • Kisselev, O.1    Ermolaeva, M.2    Gautam, N.3
  • 202
    • 0026648586 scopus 로고
    • The rod transducin α subunit amino terminus is heterogeneously fatty acylated
    • Neubert TA, Johnson RS, Hurley JB and Walsh KA, The rod transducin α subunit amino terminus is heterogeneously fatty acylated. J Biol Chem 267: 18274-18277, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 18274-18277
    • Neubert, T.A.1    Johnson, R.S.2    Hurley, J.B.3    Walsh, K.A.4
  • 203
    • 0026786031 scopus 로고
    • Lipid modification at the N terminus of photoreceptor G protein α subunit
    • Kokame K, Fukada Y, Yoshizawa T, Takao T and Shimonishi Y, Lipid modification at the N terminus of photoreceptor G protein α subunit. Nature 359: 749-752, 1992.
    • (1992) Nature , vol.359 , pp. 749-752
    • Kokame, K.1    Fukada, Y.2    Yoshizawa, T.3    Takao, T.4    Shimonishi, Y.5
  • 205
    • 0029037647 scopus 로고
    • Role of heterogeneous N-terminal acylation of recoverin in rhodopsin phosphorylation
    • Sanada K, Kokame K, Yoshizawa T, Takao T, Shimonishi Y and Fukada Y, Role of heterogeneous N-terminal acylation of recoverin in rhodopsin phosphorylation. J Biol Chem 270: 15459-15462, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 15459-15462
    • Sanada, K.1    Kokame, K.2    Yoshizawa, T.3    Takao, T.4    Shimonishi, Y.5    Fukada, Y.6
  • 206
    • 0028900550 scopus 로고
    • Involvement of N-myristoylation in monoclonal antibody recognition sites on chimeric G protein α subunits
    • Justice JM, Bliziotes MM, Stevens LA, Moss J and Vaughan M, Involvement of N-myristoylation in monoclonal antibody recognition sites on chimeric G protein α subunits. J Biol Chem 270: 6436-6439, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 6436-6439
    • Justice, J.M.1    Bliziotes, M.M.2    Stevens, L.A.3    Moss, J.4    Vaughan, M.5
  • 207
    • 0030248856 scopus 로고    scopus 로고
    • The role of prenylation in G protein assembly and function
    • Higgins JB and Casey PJ, The role of prenylation in G protein assembly and function. Cell Signal 8: 433-437, 1996.
    • (1996) Cell Signal , vol.8 , pp. 433-437
    • Higgins, J.B.1    Casey, P.J.2
  • 209
    • 0026452219 scopus 로고
    • G protein βγ subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of γ
    • Iñiguez-Lluhi JA, Simon MI, Robishaw JD and Gilman AG, G protein βγ subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of γ. J Biol Chem 267: 23409-23417, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 23409-23417
    • Iñiguez-Lluhi, J.A.1    Simon, M.I.2    Robishaw, J.D.3    Gilman, A.G.4
  • 211
    • 0038409097 scopus 로고    scopus 로고
    • Interactions of phosducin with defined G protein βγ subunits
    • Muller S, Straub A, Schroder S, Bauer PH and Lohse MJ, Interactions of phosducin with defined G protein βγ subunits. J Biol Chem 271: 11781-11786, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 11781-11786
    • Muller, S.1    Straub, A.2    Schroder, S.3    Bauer, P.H.4    Lohse, M.J.5
  • 212
    • 0030597983 scopus 로고    scopus 로고
    • Activation of G protein coupled inward rectifier channels in brain neurons requires association of G protein βγ subunits with cell membranes
    • Nakajima Y, Nakajima S and Kozasa T, Activation of G protein coupled inward rectifier channels in brain neurons requires association of G protein βγ subunits with cell membranes. FEBS Lett 390: 217-220, 1996.
    • (1996) FEBS Lett , vol.390 , pp. 217-220
    • Nakajima, Y.1    Nakajima, S.2    Kozasa, T.3
  • 213
    • 0028179876 scopus 로고
    • 2 by recombinant guanine nucleotide binding protein βγ dimers produced in a baculovirus insect cell expression system. Requirement of γ subunit isoprenylation for stimulation of phospholipase C
    • 2 by recombinant guanine nucleotide binding protein βγ dimers produced in a baculovirus insect cell expression system. Requirement of γ subunit isoprenylation for stimulation of phospholipase C. Eur J Biochem 219: 171-178, 1994.
    • (1994) Eur J Biochem , vol.219 , pp. 171-178
    • Dietrich, A.1    Meister, M.2    Brazil, D.3    Camps, M.4    Gierschik, P.5
  • 214
    • 0030065070 scopus 로고    scopus 로고
    • A novel regulatory mechanism for trimeric GTP-binding proteins in the membrane and secretory granule fractions of human and rodent β cells
    • Kowluru A, Seavey SE, Rhodes CJ and Metz SA, A novel regulatory mechanism for trimeric GTP-binding proteins in the membrane and secretory granule fractions of human and rodent β cells. Biochem J 313: 97-107, 1996.
    • (1996) Biochem J , vol.313 , pp. 97-107
    • Kowluru, A.1    Seavey, S.E.2    Rhodes, C.J.3    Metz, S.A.4
  • 216
    • 0027198334 scopus 로고
    • Guanine nucleotide specific phosphate transfer by guanine nucleotide binding regulatory protein β subunits. Characterization of the phosphorylated amino acid
    • Wieland T, Nurnbeerg B, Ulibarri I, Kaldenverg-Stasch S, Schultz G and Jakobs KH, Guanine nucleotide specific phosphate transfer by guanine nucleotide binding regulatory protein β subunits. Characterization of the phosphorylated amino acid. J Biol Chem 268: 18111-18118, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 18111-18118
    • Wieland, T.1    Nurnbeerg, B.2    Ulibarri, I.3    Kaldenverg-Stasch, S.4    Schultz, G.5    Jakobs, K.H.6
  • 217
    • 0029863008 scopus 로고    scopus 로고
    • 16 and evidence for a synergic interaction between gβγ and the β subunit of a receptor-activated G protein
    • 16 and evidence for a synergic interaction between Gβγ and the β subunit of a receptor-activated G protein. Proc Natl Acad Sci USA 93: 2827-2831, 1996.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 2827-2831
    • Zhu, X.1    Birnbaumer, L.2
  • 218
    • 0029982561 scopus 로고    scopus 로고
    • A domain on the G protein β subunit interacts with both adenylyl cyclase 2 and the muscarinic atrial potassium channel
    • Yan K and Gautam N, A domain on the G protein β subunit interacts with both adenylyl cyclase 2 and the muscarinic atrial potassium channel. J Biol Chem 271: 17597-17600, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 17597-17600
    • Yan, K.1    Gautam, N.2
  • 219
    • 0345610501 scopus 로고    scopus 로고
    • Structural determinants for the interaction with three different effectors on the G protein β subunit
    • Yan K and Gautam N, Structural determinants for the interaction with three different effectors on the G protein β subunit. J Biol Chem 272: 2056-2059, 1997.
    • (1997) J Biol Chem , vol.272 , pp. 2056-2059
    • Yan, K.1    Gautam, N.2
  • 221
    • 0029662023 scopus 로고    scopus 로고
    • Gβ subunit interacts with a peptide encoding region 956-982 of adenylyl cyclase 2. Cross-linking of the peptide to free Gβγ but not the heterotrimer
    • Weng G, Li J, Dingus J, Hildebrandt JD, Weinstein H and Iyengar R, Gβ Subunit interacts with a peptide encoding region 956-982 of adenylyl cyclase 2. Cross-linking of the peptide to free Gβγ but not the heterotrimer. J Biol Chem 271: 26445-26448, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 26445-26448
    • Weng, G.1    Li, J.2    Dingus, J.3    Hildebrandt, J.D.4    Weinstein, H.5    Iyengar, R.6
  • 222
    • 0027091999 scopus 로고
    • Dominant negative mutants of a yeast G protein β subunit identify two functional regions involved in pheromone signalling
    • Leberer E, Dignard D, Hougan L, Thomas DY and Whiteway M, Dominant negative mutants of a yeast G protein β subunit identify two functional regions involved in pheromone signalling. EMBO J 11: 4805-4813, 1992.
    • (1992) EMBO J , vol.11 , pp. 4805-4813
    • Leberer, E.1    Dignard, D.2    Hougan, L.3    Thomas, D.Y.4    Whiteway, M.5
  • 223
    • 0030297912 scopus 로고    scopus 로고
    • Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin
    • Gaudet R, Bohm A and Sigler PB, Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin. Cell 87: 577-588, 1996.
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 224
    • 0028826886 scopus 로고
    • Identification of domains conferring G protein regulation on inward rectifier channels
    • Kunkel MT and Peralta EG, Identification of domains conferring G protein regulation on inward rectifier channels. Cell 83: 443-449, 1995.
    • (1995) Cell , vol.83 , pp. 443-449
    • Kunkel, M.T.1    Peralta, E.G.2
  • 225
    • 0028792375 scopus 로고
    • Evidence that direct binding of G βγ to the GIRK1 G protein gated inwardly rectifying potassium channel is important for channel activation
    • Huang C-L, Slesinger PA, Casey PJ, Jan YN and Jan LY, Evidence that direct binding of G βγ to the GIRK1 G protein gated inwardly rectifying potassium channel is important for channel activation. Neuron 15: 1133-1143, 1995.
    • (1995) Neuron , vol.15 , pp. 1133-1143
    • Huang, C.-L.1    Slesinger, P.A.2    Casey, P.J.3    Jan, Y.N.4    Jan, L.Y.5
  • 227
    • 0027983609 scopus 로고
    • A region of the muscarinic gated atrial potassium channel critical for activation by G protein βγ subunits
    • Takao K, Yoshii M, Kanda A, Kokubun S and Nukada T, A region of the muscarinic gated atrial potassium channel critical for activation by G protein βγ subunits. Neuron 13: 747-755, 1994.
    • (1994) Neuron , vol.13 , pp. 747-755
    • Takao, K.1    Yoshii, M.2    Kanda, A.3    Kokubun, S.4    Nukada, T.5
  • 228
    • 0028284596 scopus 로고
    • Biochemical and genetic analysis of dominant negative mutations affecting a yeast G protein γ subunit
    • Grishin AV, Weiner JL and Blumer KJ, Biochemical and genetic analysis of dominant negative mutations affecting a yeast G protein γ subunit. Mol Cell Biol 14: 4571-4578, 1994.
    • (1994) Mol Cell Biol , vol.14 , pp. 4571-4578
    • Grishin, A.V.1    Weiner, J.L.2    Blumer, K.J.3
  • 229
    • 0024319210 scopus 로고
    • G proteins control diverse pathways of transmembrane signaling
    • Freissmuth M, Casey PJ and Gilman AG, G proteins control diverse pathways of transmembrane signaling. FASEB J 3: 2125-2131, 1989.
    • (1989) FASEB J , vol.3 , pp. 2125-2131
    • Freissmuth, M.1    Casey, P.J.2    Gilman, A.G.3


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