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Volumn 37, Issue , 1997, Pages 167-203

G protein βγ subunits

Author keywords

enzymes; guanine nucleotide binding proteins; ion channels; signal transduction

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); ADENYLATE CYCLASE; GUANINE NUCLEOTIDE BINDING PROTEIN; ION CHANNEL; PHOSPHOLIPASE A2; PHOSPHOLIPASE C; PHOSPHOTRANSFERASE; PROTEIN SUBUNIT;

EID: 0030957107     PISSN: 00664251     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.pharmtox.37.1.167     Document Type: Review
Times cited : (717)

References (238)
  • 1
    • 0023062991 scopus 로고
    • G proteins: Transducers of receptor-generated signals
    • Gilman AG. 1987. G proteins: Transducers of receptor-generated signals. Annu. Rev. Biochem. 56:615-49
    • (1987) Annu. Rev. Biochem. , vol.56 , pp. 615-649
    • Gilman, A.G.1
  • 3
    • 0024146522 scopus 로고
    • Function of the STE4 and STE18 genes in mating pheromone signal transduction in Saccharomyces cerevisae
    • Whiteway M, Hougan L, Dignard D, Bell L, Saari G, et al. 1988. Function of the STE4 and STE18 genes in mating pheromone signal transduction in Saccharomyces cerevisae. Cold Spring Harbor Symp. Quant. Biol. 53:585-90
    • (1988) Cold Spring Harbor Symp. Quant. Biol. , vol.53 , pp. 585-590
    • Whiteway, M.1    Hougan, L.2    Dignard, D.3    Bell, L.4    Saari, G.5
  • 4
    • 38249035983 scopus 로고
    • Which G protein subunits are the active mediators in signal transduction?
    • Birnbaumer L. 1987. Which G protein subunits are the active mediators in signal transduction? Trends Pharmacol. Sci. 8:209-11
    • (1987) Trends Pharmacol. Sci. , vol.8 , pp. 209-211
    • Birnbaumer, L.1
  • 6
    • 0023904958 scopus 로고
    • Direct G protein gating of ion channels
    • Brown AM, Birnbaumer L. 1988. Direct G protein gating of ion channels. Am. J. Physiol. 254:H401-10
    • (1988) Am. J. Physiol. , vol.254
    • Brown, A.M.1    Birnbaumer, L.2
  • 7
    • 0028076764 scopus 로고
    • WD repeat proteins: An ancient family of regulatory proteins
    • Neer EJ, Schmidt CJ, Nambudripad R, Smith TF. 1994. WD repeat proteins: an ancient family of regulatory proteins. Nature 371:297-300
    • (1994) Nature , vol.371 , pp. 297-300
    • Neer, E.J.1    Schmidt, C.J.2    Nambudripad, R.3    Smith, T.F.4
  • 10
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a GA protein βγ dimer at 2.1 Å resolution
    • Sondek J, Bohm A, Lambright DG, Hamm HE, Sigler PB. 1996. Crystal structure of a GA protein βγ dimer at 2.1 Å resolution. Nature 379:369-74
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 11
    • 0030034644 scopus 로고    scopus 로고
    • The G protein nanomachine
    • Clapham DE. 1996. The G protein nanomachine. Nature 379:297-99
    • (1996) Nature , vol.379 , pp. 297-299
    • Clapham, D.E.1
  • 12
    • 0030069667 scopus 로고    scopus 로고
    • G protein heterodimers: New structures propel new questions
    • Neer EJ, Smith TF. 1996. G protein heterodimers: New structures propel new questions. Cell 84:175-78
    • (1996) Cell , vol.84 , pp. 175-178
    • Neer, E.J.1    Smith, T.F.2
  • 13
    • 0027295485 scopus 로고
    • G protein βγ subunit: Physical and chemical characterization
    • Thomas TC, Sladek T, Yi F, Smith T, Neer EJ. 1993. G protein βγ subunit: physical and chemical characterization. Biochemistry 32:8628-35
    • (1993) Biochemistry , vol.32 , pp. 8628-8635
    • Thomas, T.C.1    Sladek, T.2    Yi, F.3    Smith, T.4    Neer, E.J.5
  • 14
    • 0030022001 scopus 로고    scopus 로고
    • βγ stimulation of rhodopsin phosphorylation by human β-adrenergic receptor kinase-1 but not for kinase binding
    • βγ stimulation of rhodopsin phosphorylation by human β-adrenergic receptor kinase-1 but not for kinase binding. J. Biol. Chem. 271:2941-48
    • (1996) J. Biol. Chem. , vol.271 , pp. 2941-2948
    • Haske, T.N.1    DeBlasi, A.2    LeVine, H.I.3
  • 15
    • 0026356891 scopus 로고
    • Predicting coiled coils from protein sequences
    • Lupas A, Van Dyke M, Stock J. 1991. Predicting coiled coils from protein sequences. Science 252:1162-64
    • (1991) Science , vol.252 , pp. 1162-1164
    • Lupas, A.1    Van Dyke, M.2    Stock, J.3
  • 17
    • 0025834532 scopus 로고
    • Diversity of G proteins in signal transduction
    • Simon MI, Strathmann MP, Gautam N. 1991. Diversity of G proteins in signal transduction. Science 252:802-8
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 20
    • 0026655342 scopus 로고
    • Interaction between G-protein β and γ subunit types is selective
    • Pronin AN, Gautam N. 1992. Interaction between G-protein β and γ subunit types is selective. Proc. Natl. Acad. Sci. USA 89:6220-24
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6220-6224
    • Pronin, A.N.1    Gautam, N.2
  • 22
    • 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, Gautam N. 1996. Differential ability to form the G protein βγ complex among members of the β and γ subunit families. J. Biol. Chem. 271:7141-46
    • (1996) J. Biol. Chem. , vol.271 , pp. 7141-7146
    • Yan, K.1    Kalyanaraman, V.2    Gautam, N.3
  • 23
    • 0028122359 scopus 로고
    • A 14-amino acid region of the G protein γ subunit is sufficient to confer selectivity of γ binding to the β subunit
    • Spring DJ, Neer EJ. 1994. A 14-amino acid region of the G protein γ subunit is sufficient to confer selectivity of γ binding to the β subunit. J. Biol. Chem. 269:22882-86
    • (1994) J. Biol. Chem. , vol.269 , pp. 22882-22886
    • Spring, D.J.1    Neer, E.J.2
  • 24
    • 0028933055 scopus 로고
    • Identification of a discrete region of the G protein γ subunit conferring selectivity in βγ complex formation
    • Lee C, Murakami T, Simonds WF. 1995. Identification of a discrete region of the G protein γ subunit conferring selectivity in βγ complex formation. J. Biol. Chem. 270:8779-84
    • (1995) J. Biol. Chem. , vol.270 , pp. 8779-8784
    • Lee, C.1    Murakami, T.2    Simonds, W.F.3
  • 26
    • 0025898422 scopus 로고
    • In vitro synthesis of G protein βγ dimers
    • Schmidt CJ, Neer EJ. 1991. In vitro synthesis of G protein βγ dimers. J. Biol. Chem. 266:4538-44
    • (1991) J. Biol. Chem. , vol.266 , pp. 4538-4544
    • Schmidt, C.J.1    Neer, E.J.2
  • 27
    • 0029074154 scopus 로고
    • The G protein γ subunit: Requirements for dimerization with β subunits
    • Mende U, Schmidt CJ, Yi F, Spring DJ, Neer EJ. 1995. The G protein γ subunit: requirements for dimerization with β subunits. J. Biol. Chem. 270:15892-98
    • (1995) J. Biol. Chem. , vol.270 , pp. 15892-15898
    • Mende, U.1    Schmidt, C.J.2    Yi, F.3    Spring, D.J.4    Neer, E.J.5
  • 28
    • 0028181755 scopus 로고
    • Association of the βγ subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90
    • Inanobe A, Takahashi K, Katada T. 1994. Association of the βγ subunits of trimeric GTP-binding proteins with 90-kDa heat shock protein, hsp90. J. Biochem. 115:486-92
    • (1994) J. Biochem. , vol.115 , pp. 486-492
    • Inanobe, A.1    Takahashi, K.2    Katada, T.3
  • 29
    • 0026691771 scopus 로고
    • Expression of functional G protein βγ dimers of defined subunit composition using a baculovirus expression system
    • Graber SG, Figler RA, Kalman-Maltese VK, Robishaw JD, Garrison JC. 1992. Expression of functional G protein βγ dimers of defined subunit composition using a baculovirus expression system. J. Biol. Chem. 267:13123-26
    • (1992) J. Biol. Chem. , vol.267 , pp. 13123-13126
    • Graber, S.G.1    Figler, R.A.2    Kalman-Maltese, V.K.3    Robishaw, J.D.4    Garrison, J.C.5
  • 30
    • 0029854139 scopus 로고    scopus 로고
    • Folding of proteins with WD-repeats: Comparison of six members of the WD-repeat superfamily to the G protein β subunit
    • In press
    • Garcia-Higuera I, Fenoglio J, Li Y, Lewis C, Panchenko MP, et al. 1996. Folding of proteins with WD-repeats: comparison of six members of the WD-repeat superfamily to the G protein β subunit. Biochemistry. In press
    • (1996) Biochemistry
    • Garcia-Higuera, I.1    Fenoglio, J.2    Li, Y.3    Lewis, C.4    Panchenko, M.P.5
  • 31
    • 0029966304 scopus 로고    scopus 로고
    • Protein prenyltransferases
    • Casey PJ, Seabra MC. 1996. Protein prenyltransferases. J. Biol. Chem. 271: 5289-92
    • (1996) J. Biol. Chem. , vol.271 , pp. 5289-5292
    • Casey, P.J.1    Seabra, M.C.2
  • 34
    • 0027932723 scopus 로고
    • Functional significance of G protein carboxymethylation
    • Parish CA, Rando RR. 1994. Functional significance of G protein carboxymethylation. Biochemistry 33:9986-91
    • (1994) Biochemistry , vol.33 , pp. 9986-9991
    • Parish, C.A.1    Rando, R.R.2
  • 35
    • 0027983602 scopus 로고
    • Effects of carboxyl methylation of photoreceptor G protein γ-subunit in visual transduction
    • Fukada Y, Matsuda T, Kokame K, Takao T, Shimonishi Y, et al. 1994. Effects of carboxyl methylation of photoreceptor G protein γ-subunit in visual transduction. J. Biol. Chem. 269:5163-70
    • (1994) J. Biol. Chem. , vol.269 , pp. 5163-5170
    • Fukada, Y.1    Matsuda, T.2    Kokame, K.3    Takao, T.4    Shimonishi, Y.5
  • 36
    • 0029940468 scopus 로고    scopus 로고
    • The role of G protein methylation in the function of a geranylgeranylated βγ isoform
    • Parish CA, Smrcka AV, Rando RR. 1996. The role of G protein methylation in the function of a geranylgeranylated βγ isoform. Biochemistry 35:7499-505
    • (1996) Biochemistry , vol.35 , pp. 7499-7505
    • Parish, C.A.1    Smrcka, A.V.2    Rando, R.R.3
  • 37
    • 0028363744 scopus 로고
    • In vitro processing of recombinant G protein γ subunits
    • Higgins JB, Casey PJ. 1994. In vitro processing of recombinant G protein γ subunits. J. Biol. Chem. 209:9067-73
    • (1994) J. Biol. Chem. , vol.209 , pp. 9067-9073
    • Higgins, J.B.1    Casey, P.J.2
  • 38
    • 0027090202 scopus 로고
    • Influence of γ subunit prenylation on association of guanine nucleotide-binding regulatory proteins with membranes
    • Muntz KH, Sternweis PC, Gilman AG, Mumby SM. 1992. Influence of γ subunit prenylation on association of guanine nucleotide-binding regulatory proteins with membranes. Mol. Biol. Cell 3:49-61
    • (1992) Mol. Biol. Cell , vol.3 , pp. 49-61
    • Muntz, K.H.1    Sternweis, P.C.2    Gilman, A.G.3    Mumby, S.M.4
  • 39
    • 0026009360 scopus 로고
    • G protein βγ dimers: Membrane targeting requires subunit coexpression and intact γ C-A-A-X domain
    • Simonds WF, Butrynski JE, Gautam N, Unson CB, Spiegel AM. 1991. G protein βγ dimers: Membrane targeting requires subunit coexpression and intact γ C-A-A-X domain. J. Biol. Chem. 266:5363-66
    • (1991) J. Biol. Chem. , vol.266 , pp. 5363-5366
    • Simonds, W.F.1    Butrynski, J.E.2    Gautam, N.3    Unson, C.B.4    Spiegel, A.M.5
  • 40
    • 0025992099 scopus 로고
    • Carboxyl methylation and farnesylation of transducin γ-subunit synergistically enhance its coupling with metarhodopsin II
    • Ohguro H, Fukada Y, Takao T, Shimonishi Y, Yoshizawa T, Akino T. 1991. Carboxyl methylation and farnesylation of transducin γ-subunit synergistically enhance its coupling with metarhodopsin II. EMBO J. 10:3669-74
    • (1991) EMBO J. , vol.10 , pp. 3669-3674
    • Ohguro, H.1    Fukada, Y.2    Takao, T.3    Shimonishi, Y.4    Yoshizawa, T.5    Akino, T.6
  • 41
    • 0342433181 scopus 로고    scopus 로고
    • Deleted in proof
    • Deleted in proof
  • 42
    • 0029908035 scopus 로고    scopus 로고
    • Isoprenylation of the G protein γ subunit is both necessary and sufficient for βγ dimer-mediated stimulation of phospholipase C
    • In press
    • Dietrich A, Brazil D, Meister M, Schrader M, Moomaw JF, et al. 1996. Isoprenylation of the G protein γ subunit is both necessary and sufficient for βγ dimer-mediated stimulation of phospholipase C. Biochemistry. In press
    • (1996) Biochemistry
    • Dietrich, A.1    Brazil, D.2    Meister, M.3    Schrader, M.4    Moomaw, J.F.5
  • 44
    • 0027198334 scopus 로고
    • Guanine nucleotide-specific phosphate transfer by guanine nucleotide-binding regulatory protein β-subunits: Characterization of the phosphorylated amino acid
    • Wieland T, Nurnberg B, Ulibarri I, Kaldenberg-Stash S, Schultz G, Jakobs KH. 1993. Guanine nucleotide-specific phosphate transfer by guanine nucleotide-binding regulatory protein β-subunits: characterization of the phosphorylated amino acid. J. Biol. Chem. 268:18111-18
    • (1993) J. Biol. Chem. , vol.268 , pp. 18111-18118
    • Wieland, T.1    Nurnberg, B.2    Ulibarri, I.3    Kaldenberg-Stash, S.4    Schultz, G.5    Jakobs, K.H.6
  • 45
    • 0026730811 scopus 로고
    • Stimulation and inhibition of human platelet adenylylcyclase by thiophosphorylated transducin βγ-subunits
    • Wieland T, Ronzani M, Jakobs KH. 1992. Stimulation and inhibition of human platelet adenylylcyclase by thiophosphorylated transducin βγ-subunits. J. Biol. Chem. 267:20791-97
    • (1992) J. Biol. Chem. , vol.267 , pp. 20791-20797
    • Wieland, T.1    Ronzani, M.2    Jakobs, K.H.3
  • 46
    • 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, Metz SA. 1996. 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) Biochem. J. , vol.313 , pp. 97-107
    • Kowluru, A.1    Seavey, S.E.2    Rhodes, C.J.3    Metz, S.A.4
  • 48
    • 0028228109 scopus 로고
    • A two-component system that regulates an osmosensing MAP kinase cascade in yeast
    • Maeda T, Wurgler-Murphy SM, Saito H. 1994. A two-component system that regulates an osmosensing MAP kinase cascade in yeast. Nature 369:242-45
    • (1994) Nature , vol.369 , pp. 242-245
    • Maeda, T.1    Wurgler-Murphy, S.M.2    Saito, H.3
  • 49
    • 0028981362 scopus 로고
    • zα by protein kinase C blocks interaction with the βγ complex
    • zα by protein kinase C blocks interaction with the βγ complex. J. Biol. Chem. 270:23119-25
    • (1995) J. Biol. Chem. , vol.270 , pp. 23119-23125
    • Fields, T.A.1    Casey, P.J.2
  • 51
    • 0025969447 scopus 로고
    • Pheromone-induced phosphorylation of a G protein β subunit in S. cerevisiae is associated with an adaptive response to mating pheromone
    • Cole GM, Reed SI. 1991. Pheromone-induced phosphorylation of a G protein β subunit in S. cerevisiae is associated with an adaptive response to mating pheromone. Cell 64:703-6
    • (1991) Cell , vol.64 , pp. 703-706
    • Cole, G.M.1    Reed, S.I.2
  • 52
    • 0017842904 scopus 로고
    • Actions of choleragen and gonadotropin in isolated Leydig cells: Functional compartmentalization of the hormone-activated cyclic AMP response
    • Dufau ML, Horner KA, Hayashi K, Tsuruhara T, Conn PM, Catt KJ. 1978. Actions of choleragen and gonadotropin in isolated Leydig cells: functional compartmentalization of the hormone-activated cyclic AMP response. J. Biol. Chem. 253:3721-29
    • (1978) J. Biol. Chem. , vol.253 , pp. 3721-3729
    • Dufau, M.L.1    Horner, K.A.2    Hayashi, K.3    Tsuruhara, T.4    Conn, P.M.5    Catt, K.J.6
  • 53
    • 0021023294 scopus 로고
    • Compartments of cyclic AMP and protein kinase in mammalian cardiomyocytes
    • Buxton IL, Brunton LL. 1983. Compartments of cyclic AMP and protein kinase in mammalian cardiomyocytes. J. Biol. Chem. 258:10233-39
    • (1983) J. Biol. Chem. , vol.258 , pp. 10233-10239
    • Buxton, I.L.1    Brunton, L.L.2
  • 55
    • 0025730818 scopus 로고
    • Subcellular patterns of calcium release determined by G protein-specific residues of muscarinic receptors
    • Lechleiter J, Girard S, Clapham D, Peralta E. 1991. Subcellular patterns of calcium release determined by G protein-specific residues of muscarinic receptors. Nature 350:505-8
    • (1991) Nature , vol.350 , pp. 505-508
    • Lechleiter, J.1    Girard, S.2    Clapham, D.3    Peralta, E.4
  • 56
    • 0027936892 scopus 로고
    • Membrane organization in G-protein mechanisms
    • Neubig RR. 1994. Membrane organization in G-protein mechanisms. FASEB J. 8:939-46
    • (1994) FASEB J. , vol.8 , pp. 939-946
    • Neubig, R.R.1
  • 57
    • 0027275642 scopus 로고
    • Signal transducing molecules and GPI-linked proteins form a caveolinrich insoluble complex in MDCK cells
    • Sargiacomo M, Sudol M, Tang Z, Lisanti MP. 1993. Signal transducing molecules and GPI-linked proteins form a caveolinrich insoluble complex in MDCK cells. J. Cell Biol. 122:789-808
    • (1993) J. Cell Biol. , vol.122 , pp. 789-808
    • Sargiacomo, M.1    Sudol, M.2    Tang, Z.3    Lisanti, M.P.4
  • 61
    • 0023036853 scopus 로고
    • Fractionation of the β subunit common to guanine nucleotide-binding regulatory proteins with the cytoskeleton
    • Carlson KE, Woolkalis MJ, Newhouse MG, Manning DR. 1986. Fractionation of the β subunit common to guanine nucleotide-binding regulatory proteins with the cytoskeleton. Mol. Pharmacol. 30:463-68
    • (1986) Mol. Pharmacol. , vol.30 , pp. 463-468
    • Carlson, K.E.1    Woolkalis, M.J.2    Newhouse, M.G.3    Manning, D.R.4
  • 62
    • 0027998469 scopus 로고
    • Localization of a heterotrimeric G protein γ subunit to focal adhesions and associated stress fibers
    • Hansen CA, Schroering AG, Carey DJ, Robishaw JD. 1994. Localization of a heterotrimeric G protein γ subunit to focal adhesions and associated stress fibers. J. Cell Biol. 126:811-19
    • (1994) J. Cell Biol. , vol.126 , pp. 811-819
    • Hansen, C.A.1    Schroering, A.G.2    Carey, D.J.3    Robishaw, J.D.4
  • 63
    • 0029060381 scopus 로고
    • A periodic network of G protein βγ subunit coexisting with cytokeratin filament in starfish oocytes
    • Chiba K, Longo FJ, Kontani K, Katada T, Hoshi M. 1995. A periodic network of G protein βγ subunit coexisting with cytokeratin filament in starfish oocytes. Dev. Biol. 169:415-20
    • (1995) Dev. Biol. , vol.169 , pp. 415-420
    • Chiba, K.1    Longo, F.J.2    Kontani, K.3    Katada, T.4    Hoshi, M.5
  • 64
    • 0029929903 scopus 로고    scopus 로고
    • Differential distribution of a subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas
    • Denker SP, McCaffery JM, Palade GE, Insel PA, Farquhar MG. 1996. Differential distribution of a subunits and βγ subunits of heterotrimeric G proteins on Golgi membranes of the exocrine pancreas. J. Cell Biol. 133:1027-40
    • (1996) J. Cell Biol. , vol.133 , pp. 1027-1040
    • Denker, S.P.1    McCaffery, J.M.2    Palade, G.E.3    Insel, P.A.4    Farquhar, M.G.5
  • 67
    • 0028237708 scopus 로고
    • Structural determinants for activation of the α-subunit of a heterotrimeric G protein
    • Lambright DG, Noel JP, Hamm HE, Sigler PB. 1994. Structural determinants for activation of the α-subunit of a heterotrimeric G protein. Nature 369:621-28
    • (1994) Nature , vol.369 , pp. 621-628
    • Lambright, D.G.1    Noel, J.P.2    Hamm, H.E.3    Sigler, P.B.4
  • 68
    • 0020975121 scopus 로고
    • Characterization of transducin from bovine retinal rod outer segments. II. Evidence for distinct binding sites and conformational changes revealed by limited proteolysis with trypsin
    • Fung BK-K, Nash CR. 1983. Characterization of transducin from bovine retinal rod outer segments. II. Evidence for distinct binding sites and conformational changes revealed by limited proteolysis with trypsin. J. Biol. Chem. 258: 10503-10
    • (1983) J. Biol. Chem. , vol.258 , pp. 10503-10510
    • Fung, B.K.-K.1    Nash, C.R.2
  • 69
    • 0023879691 scopus 로고
    • The amino terminus of G protein α subunits is required for interaction with βγ
    • Neer EJ, Pulsifer L, Wolf L. 1988. The amino terminus of G protein α subunits is required for interaction with βγ. J. Biol. Chem. 263:8996-9000
    • (1988) J. Biol. Chem. , vol.263 , pp. 8996-9000
    • Neer, E.J.1    Pulsifer, L.2    Wolf, L.3
  • 71
    • 0021683990 scopus 로고
    • Purification and properties of the inhibitory guanine nucleotide regulatory unit of brain adenylate cyclase
    • Neer EJ, Lok JM, Wolf LG. 1984. Purification and properties of the inhibitory guanine nucleotide regulatory unit of brain adenylate cyclase. J. Biol. Chem. 259:14222-29
    • (1984) J. Biol. Chem. , vol.259 , pp. 14222-14229
    • Neer, E.J.1    Lok, J.M.2    Wolf, L.G.3
  • 72
    • 0021751510 scopus 로고
    • Effects of guanyl nucleotides and rhodopsin on ADP-ribosylation of the inhibitory GTP-binding component of adenylate cyclase by pertussis toxin
    • Tsai SC, Adamik R, Kanaho Y, Hewlett EL, Moss J. 1984. Effects of guanyl nucleotides and rhodopsin on ADP-ribosylation of the inhibitory GTP-binding component of adenylate cyclase by pertussis toxin. J. Biol. Chem. 259:15320-23
    • (1984) J. Biol. Chem. , vol.259 , pp. 15320-15323
    • Tsai, S.C.1    Adamik, R.2    Kanaho, Y.3    Hewlett, E.L.4    Moss, J.5
  • 73
    • 0022347238 scopus 로고
    • Pertussis toxin-catalyzed ADPribosylation of transducin: Cysteine 347 is the ADP-ribose acceptor site
    • West REJ, Moss J, Vaughan M, Liu T, Liu TY. 1985. Pertussis toxin-catalyzed ADPribosylation of transducin: Cysteine 347 is the ADP-ribose acceptor site. J. Biol. Chem. 260:14428-30
    • (1985) J. Biol. Chem. , vol.260 , pp. 14428-14430
    • West, R.E.J.1    Moss, J.2    Vaughan, M.3    Liu, T.4    Liu, T.Y.5
  • 74
    • 0019512472 scopus 로고
    • Conformational changes of adenylyl cyclase regulatory proteins mediated by guanine nucleotides
    • Hudson TH, Roeber JF, Johnson GL. 1981. Conformational changes of adenylyl cyclase regulatory proteins mediated by guanine nucleotides. J. Biol. Chem. 256:1459-65
    • (1981) J. Biol. Chem. , vol.256 , pp. 1459-1465
    • Hudson, T.H.1    Roeber, J.F.2    Johnson, G.L.3
  • 76
    • 0021993452 scopus 로고
    • s: Accumulation of turnover of enzyme-nucleotide intermediates
    • s: accumulation of turnover of enzyme-nucleotide intermediates. J. Biol. Chem. 260:266-72
    • (1985) J. Biol. Chem. , vol.260 , pp. 266-272
    • Brandt, D.R.1    Ross, E.M.2
  • 79
    • 0026786080 scopus 로고
    • Rhodopsin/transducin interactions. I. Characterization of the binding of the transducinβγ subunit complex to rhodopsin using fluorescence spectroscopy
    • Phillips WJ, Cerione RA. 1992. Rhodopsin/transducin interactions. I. Characterization of the binding of the transducinβγ subunit complex to rhodopsin using fluorescence spectroscopy. J. Biol. Chem. 267:17032-39
    • (1992) J. Biol. Chem. , vol.267 , pp. 17032-17039
    • Phillips, W.J.1    Cerione, R.A.2
  • 80
    • 0026788155 scopus 로고
    • Rhodopsin/transducin interactions. II. Influence of the transducinβγ subunit complex on the coupling of the transducin-α subunit to rhodopsin
    • Phillips WJ, Wong SC, Cerione RA. 1992. Rhodopsin/transducin interactions. II. Influence of the transducinβγ subunit complex on the coupling of the transducin-α subunit to rhodopsin. J. Biol. Chem. 267:17040-46
    • (1992) J. Biol. Chem. , vol.267 , pp. 17040-17046
    • Phillips, W.J.1    Wong, S.C.2    Cerione, R.A.3
  • 81
    • 0023697285 scopus 로고
    • Transducin inhibition of light-dependent rhodopsin phosphorylation: Evidence for βγ subunit interaction with rhodopsin
    • Kelleher DJ, Johnson GL. 1988. Transducin inhibition of light-dependent rhodopsin phosphorylation: evidence for βγ subunit interaction with rhodopsin. Mol. Pharmacol. 34:452-60
    • (1988) Mol. Pharmacol. , vol.34 , pp. 452-460
    • Kelleher, D.J.1    Johnson, G.L.2
  • 82
    • 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, Gautam N. 1995. Efficient interaction with a receptor requires a specific type of prenyl group on the G protein γ subunit. J. Biol. Chem. 270:25356-58
    • (1995) J. Biol. Chem. , vol.270 , pp. 25356-25358
    • Kisselev, O.1    Ermolaeva, M.2    Gautam, N.3
  • 83
    • 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, Thorner J. 1990. 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 87:4363-67
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 4363-4367
    • Blumer, K.J.1    Thorner, J.2
  • 84
    • 0029020634 scopus 로고
    • The G protein βγ subunit is essential for multiple responses to chemoattractants in Dictyostelium
    • Wu L, Valkema R, Van Haastert PJ, Devreotes PN. 1995. The G protein βγ subunit is essential for multiple responses to chemoattractants in Dictyostelium. J. Cell Biol. 129:1667-75
    • (1995) J. Cell Biol. , vol.129 , pp. 1667-1675
    • Wu, L.1    Valkema, R.2    Van Haastert, P.J.3    Devreotes, P.N.4
  • 85
    • 0028923803 scopus 로고
    • S-prenylated cysteine analogues inhibit receptor-mediated G protein activation in native human granulocyte and reconstituted bovine retinal rod out segment membranes
    • Scheer A, Gierschik P. 1995. S-prenylated cysteine analogues inhibit receptor-mediated G protein activation in native human granulocyte and reconstituted bovine retinal rod out segment membranes. Biochemistry 34:4952-61
    • (1995) Biochemistry , vol.34 , pp. 4952-4961
    • Scheer, A.1    Gierschik, P.2
  • 86
    • 0029026880 scopus 로고
    • Receptor-G protein coupling is established by a potential conformational switch in the βγ complex
    • Kisselev O, Pronin A, Ermolaeva M, Gautam N. 1995. Receptor-G protein coupling is established by a potential conformational switch in the βγ complex. Proc. Natl. Acad. Sci. USA 92:9102-6
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9102-9106
    • Kisselev, O.1    Pronin, A.2    Ermolaeva, M.3    Gautam, N.4
  • 87
    • 0030064529 scopus 로고    scopus 로고
    • Receptor and membrane interaction sites of Gβ: A receptor-derived peptide binds to the carboxyl terminus
    • Taylor JM, Jacob-Mosier GG, Lawton RG, VanDort M, Neubig RR. 1996. Receptor and membrane interaction sites of Gβ: A receptor-derived peptide binds to the carboxyl terminus. J. Biol. Chem. 271:3336-39
    • (1996) J. Biol. Chem. , vol.271 , pp. 3336-3339
    • Taylor, J.M.1    Jacob-Mosier, G.G.2    Lawton, R.G.3    VanDort, M.4    Neubig, R.R.5
  • 89
    • 0026752495 scopus 로고
    • Different β-subunits determine G-protein interaction with transmembrane receptors
    • Kleuss C, Scherubl H, Hescheler J, Schultz G, Wittig B. 1992. Different β-subunits determine G-protein interaction with transmembrane receptors. Nature 358:424-26
    • (1992) Nature , vol.358 , pp. 424-426
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5
  • 92
    • 0029982561 scopus 로고    scopus 로고
    • A domain on the G protein β subunit interacts with both adeylyl cyclase 2 and the muscarinic atrial potassium channel
    • Yan K, Gautam N. 1996. A domain on the G protein β subunit interacts with both adeylyl cyclase 2 and the muscarinic atrial potassium channel. J. Biol. Chem. 271:17597-600
    • (1996) J. Biol. Chem. , vol.271 , pp. 17597-17600
    • Yan, K.1    Gautam, N.2
  • 93
    • 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, Whiteway M. 1992. Dominant-negative mutants of a yeast G-protein β subunit identify two functional regions involved in pheromone signalling. EMBO J. 11:4805-13
    • (1992) EMBO J. , vol.11 , pp. 4805-4813
    • Leberer, E.1    Dignard, D.2    Hougan, L.3    Thomas, D.Y.4    Whiteway, M.5
  • 94
    • 0028348035 scopus 로고
    • Direct G protein gating of ion channels?
    • Clapham DE. 1994. Direct G protein gating of ion channels? Annu. Rev. Neurosci. 17:441-64
    • (1994) Annu. Rev. Neurosci. , vol.17 , pp. 441-464
    • Clapham, D.E.1
  • 100
    • 0022350208 scopus 로고
    • Uncoupling of cardiac muscarinic and β-adrenergic receptors from ion channels by a guanine nucleotide analogue
    • Breitwieser GE, Szabo G. 1985. Uncoupling of cardiac muscarinic and β-adrenergic receptors from ion channels by a guanine nucleotide analogue. Naturel 317:538-40
    • (1985) Naturel , vol.317 , pp. 538-540
    • Breitwieser, G.E.1    Szabo, G.2
  • 105
    • 0028180952 scopus 로고
    • Recombinant G protein βγ-subunits activate the muscarinicgated atrial potassium channel
    • Wickman KD, Iñiguez-Lluhi JA, Davenport PA, Taussig R, Krapivinsky GB, et al. 1994. Recombinant G protein βγ-subunits activate the muscarinicgated atrial potassium channel. Nature 368:255-57
    • (1994) Nature , vol.368 , pp. 255-257
    • Wickman, K.D.1    Iñiguez-Lluhi, J.A.2    Davenport, P.A.3    Taussig, R.4    Krapivinsky, G.B.5
  • 106
    • 0028322077 scopus 로고
    • Activation of the cloned muscarinic potassium channel by G protein βγ subunits
    • Reuveny E, Slesinger PA, Inglese J, Morales JM, Iñiguez-Lluhi JA, et al. 1994. Activation of the cloned muscarinic potassium channel by G protein βγ subunits. Nature 370:143-46
    • (1994) Nature , vol.370 , pp. 143-146
    • Reuveny, E.1    Slesinger, P.A.2    Inglese, J.3    Morales, J.M.4    Iñiguez-Lluhi, J.A.5
  • 107
    • 0029083582 scopus 로고
    • Inhibition of function in Xenopus oocytes of the inwardly rectifying G-protein-activated atrial K channel (GIRK1) by overexpression of a membrane-attached form of the C-terminal tail
    • Dascal N. Doupnik CA, Ivanina T, Bausch S, Wang W. et al. 1995. Inhibition of function in Xenopus oocytes of the inwardly rectifying G-protein-activated atrial K channel (GIRK1) by overexpression of a membrane-attached form of the C-terminal tail. Proc. Natl. Acacl. Sci. USA 92:6758-62
    • (1995) Proc. Natl. Acacl. Sci. USA , vol.92 , pp. 6758-6762
    • Dascal, N.1    Doupnik, C.A.2    Ivanina, T.3    Bausch, S.4    Wang, W.5
  • 110
    • 0028144742 scopus 로고
    • Cloning and functional expression of a rat heart KATP channel
    • Ashford MLJ, Bond CT, Blair TA, Adelman JP. 1994. Cloning and functional expression of a rat heart KATP channel. Nature 370:456-59
    • (1994) Nature , vol.370 , pp. 456-459
    • Ashford, M.L.J.1    Bond, C.T.2    Blair, T.A.3    Adelman, J.P.4
  • 111
    • 16144367499 scopus 로고
    • Retraction of cloning and functional expression of a rat heart KATP channel
    • Ashford MLJ, Bond CT, Blair TA, Adelman JP. 1995. Retraction of cloning and functional expression of a rat heart KATP channel. Nature 378:792
    • (1995) Nature , vol.378 , pp. 792
    • Ashford, M.L.J.1    Bond, C.T.2    Blair, T.A.3    Adelman, J.P.4
  • 113
    • 0023355659 scopus 로고
    • Stimulation of phospholipase A2 activity in bovine rod outer segments by the βγ subunits of transducin and its inhibition by the α subunit
    • Jelsema CL, Axelrod J. 1987. Stimulation of phospholipase A2 activity in bovine rod outer segments by the βγ subunits of transducin and its inhibition by the α subunit. Proc. Natl. Acad. Sci. USA 84:3623-27
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 3623-3627
    • Jelsema, C.L.1    Axelrod, J.2
  • 117
    • 0028792376 scopus 로고
    • Identification of structural elements involved in G protein gating of the GIRK1 potassium channel
    • Slesinger PA, Reuveny E, Jan YN, Jan LY. 1995. Identification of structural elements involved in G protein gating of the GIRK1 potassium channel. Neuron 15:1145-56
    • (1995) Neuron , vol.15 , pp. 1145-1156
    • Slesinger, P.A.1    Reuveny, E.2    Jan, Y.N.3    Jan, L.Y.4
  • 119
    • 0028826886 scopus 로고
    • Identification of domains conferring G protein regulation on inward rectifier potassium channels
    • Kunkel MT, Peralta EG. 1995. Identification of domains conferring G protein regulation on inward rectifier potassium channels. Cell 83:443-49
    • (1995) Cell , vol.83 , pp. 443-449
    • Kunkel, M.T.1    Peralta, E.G.2
  • 123
    • 0030004908 scopus 로고    scopus 로고
    • A recombinant inwardly rectifying potassium channel coupled to GTP-binding proteins
    • Chan KW, Langan N, Sui JL, Kozak A, Pabon A, et al. 1996. A recombinant inwardly rectifying potassium channel coupled to GTP-binding proteins. J. Gen. Physiol. 107:381-97
    • (1996) J. Gen. Physiol. , vol.107 , pp. 381-397
    • Chan, K.W.1    Langan, N.2    Sui, J.L.3    Kozak, A.4    Pabon, A.5
  • 124
    • 0343738265 scopus 로고    scopus 로고
    • Epitope-tagged GIRK1 and CIR inward rectifiers for studying subunit interactions and localization
    • In press
    • Kennedy M, Nemec J, Clapham DE. 1996. Epitope-tagged GIRK1 and CIR inward rectifiers for studying subunit interactions and localization. J. Neuropharmacol. In press
    • (1996) J. Neuropharmacol.
    • Kennedy, M.1    Nemec, J.2    Clapham, D.E.3
  • 128
    • 0027973423 scopus 로고
    • Modulation of ion-channel function by G-protein-coupled receptors
    • Hille B. 1994. Modulation of ion-channel function by G-protein-coupled receptors. Trends Neurosci. 17:531-36
    • (1994) Trends Neurosci. , vol.17 , pp. 531-536
    • Hille, B.1
  • 129
    • 0024354817 scopus 로고
    • Neurotransmitter inhibition of neuronal calcium currents by changes in channel voltage dependence
    • Bean BP. 1989. Neurotransmitter inhibition of neuronal calcium currents by changes in channel voltage dependence. Nature 340:153-56
    • (1989) Nature , vol.340 , pp. 153-156
    • Bean, B.P.1
  • 130
    • 0029921401 scopus 로고    scopus 로고
    • Voltage-dependent modulation of N-type calcium channels by G-protein βγ subunits
    • Ikeda SR. 1996. Voltage-dependent modulation of N-type calcium channels by G-protein βγ subunits. Nature 380:255-58
    • (1996) Nature , vol.380 , pp. 255-258
    • Ikeda, S.R.1
  • 132
    • 0028853081 scopus 로고
    • Transmitter-mediated inhibition of N-type calcium channels in sensory neurons involves multiple GTP-binding proteins and subunits
    • Diversé-Pierluissi M, Goldsmith PK, Dunlap K. 1995. Transmitter-mediated inhibition of N-type calcium channels in sensory neurons involves multiple GTP-binding proteins and subunits. Neuron 14:191-200
    • (1995) Neuron , vol.14 , pp. 191-200
    • Diversé-Pierluissi, M.1    Goldsmith, P.K.2    Dunlap, K.3
  • 134
    • 0028831997 scopus 로고
    • Calcium signalling
    • Clapham DE. 1995. Calcium signalling. Cell 80:259-69
    • (1995) Cell , vol.80 , pp. 259-269
    • Clapham, D.E.1
  • 135
    • 0028177677 scopus 로고
    • The active role of βγ in signal transduction
    • Sternweis P. 1994. The active role of βγ in signal transduction. Curr. Opin. Cell Biol. 6:403-6
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 403-406
    • Sternweis, P.1
  • 137
    • 0026497034 scopus 로고
    • βγ -Subunit activation of G-protein-regulated phospholipase C
    • Boyer JL, Waldo GL, Harden TK. 1992. βγ -Subunit activation of G-protein-regulated phospholipase C. J. Biol Chem. 267:25451-56
    • (1992) J. Biol Chem. , vol.267 , pp. 25451-25456
    • Boyer, J.L.1    Waldo, G.L.2    Harden, T.K.3
  • 138
    • 0026676806 scopus 로고
    • Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits
    • Camps M, Carozzi A, Schnabel P, Scheer A, Parker PJ, Gierschik P. 1992. Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits. Nature 360:684-86
    • (1992) Nature , vol.360 , pp. 684-686
    • Camps, M.1    Carozzi, A.2    Schnabel, P.3    Scheer, A.4    Parker, P.J.5    Gierschik, P.6
  • 139
    • 0026446880 scopus 로고
    • Activation of cytosolic phosphoinositide phospholipase C by G-protein βγ subunits
    • Blank JL, Brattain KA, Exton JH. 1992. Activation of cytosolic phosphoinositide phospholipase C by G-protein βγ subunits. J. Biol. Chem. 267:23069-75
    • (1992) J. Biol. Chem. , vol.267 , pp. 23069-23075
    • Blank, J.L.1    Brattain, K.A.2    Exton, J.H.3
  • 140
    • 0026676807 scopus 로고
    • Subunits βγ of heterotrimeric G protein activate β2 isoform of phospholipase C
    • Katz A, Wu DQ, Simon MI. 1992. Subunits βγ of heterotrimeric G protein activate β2 isoform of phospholipase C. Nature 360:686-89
    • (1992) Nature , vol.360 , pp. 686-689
    • Katz, A.1    Wu, D.Q.2    Simon, M.I.3
  • 142
    • 0027418803 scopus 로고
    • Activation of phospholipase C isozymes by G protein βγ subunits
    • Park D, Jhon D-Y, Lee C-W, Lee K-H, Rhee SG. 1993. Activation of phospholipase C isozymes by G protein βγ subunits. J. Biol. Chem. 268:4573-76
    • (1993) J. Biol. Chem. , vol.268 , pp. 4573-4576
    • Park, D.1    Jhon, D.-Y.2    Lee, C.-W.3    Lee, K.-H.4    Rhee, S.G.5
  • 143
    • 0027214868 scopus 로고
    • Regulation of purified subtypes of phosphatidylinositol-specific phospholipase Cβ by G protein α and βγ subunits
    • Smrcka AV, Sternweis PC. 1993. Regulation of purified subtypes of phosphatidylinositol-specific phospholipase Cβ by G protein α and βγ subunits. J. Biol. Chem. 268:9667-74
    • (1993) J. Biol. Chem. , vol.268 , pp. 9667-9674
    • Smrcka, A.V.1    Sternweis, P.C.2
  • 144
    • 0026654469 scopus 로고
    • Regulation of Inositol phospholipid-specific phospholipase C isozymes
    • Rhee SG, Choi KD. 1992. Regulation of Inositol phospholipid-specific phospholipase C isozymes. J. Biol. Chem. 267:12393-96
    • (1992) J. Biol. Chem. , vol.267 , pp. 12393-12396
    • Rhee, S.G.1    Choi, K.D.2
  • 145
    • 0028283331 scopus 로고
    • Activation of phospholipase C β4 by heterotrimeric GTP-binding proteins
    • Jiang HP, Wu DQ, Simon MI. 1994. Activation of phospholipase C β4 by heterotrimeric GTP-binding proteins. J. Biol. Chem. 269:7593-96
    • (1994) J. Biol. Chem. , vol.269 , pp. 7593-7596
    • Jiang, H.P.1    Wu, D.Q.2    Simon, M.I.3
  • 146
    • 0027531123 scopus 로고
    • Activation of phosphatidylinositol lipid-specific phospholipase C-β3 by G protein βγ subunits
    • Carozzi A, Camps M, Gierschik P, Parker PJ. 1993. Activation of phosphatidylinositol lipid-specific phospholipase C-β3 by G protein βγ subunits. FEBS Lett. 315:340-42
    • (1993) FEBS Lett. , vol.315 , pp. 340-342
    • Carozzi, A.1    Camps, M.2    Gierschik, P.3    Parker, P.J.4
  • 147
    • 0027465720 scopus 로고
    • Identification of critical regions on phospholipase C-β1 required for activation by G-proteins
    • Wu DQ, Jiang HP, Katz A, Simon MI. 1993. Identification of critical regions on phospholipase C-β1 required for activation by G-proteins. J. Biol. Chem. 268:3704-9
    • (1993) J. Biol. Chem. , vol.268 , pp. 3704-3709
    • Wu, D.Q.1    Jiang, H.P.2    Katz, A.3    Simon, M.I.4
  • 148
    • 0027178468 scopus 로고
    • Activation of phospholipase Cβ2 by the α and βγ subunits of trimeric GTP-binding protein
    • Wu DQ, Katz A, Simon MI. 1993. Activation of phospholipase Cβ2 by the α and βγ subunits of trimeric GTP-binding protein. Proc. Natl. Acad. Sci. USA 90:5297-301
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5297-5301
    • Wu, D.Q.1    Katz, A.2    Simon, M.I.3
  • 150
    • 0027365766 scopus 로고
    • Purification of a 100-kDa phosphoinositide phospholipase C that is activated by G-protein βγ subunits
    • Blank JL, Shaw K, Ross AH, Exton JH. 1993. Purification of a 100-kDa phosphoinositide phospholipase C that is activated by G-protein βγ subunits. J. Biol. Chem. 268:25184-91
    • (1993) J. Biol. Chem. , vol.268 , pp. 25184-25191
    • Blank, J.L.1    Shaw, K.2    Ross, A.H.3    Exton, J.H.4
  • 152
    • 0027981982 scopus 로고
    • Selective activation of phospholipase C by recombinant G-protein α- and βγ-subunits
    • Boyer JL, Graber SG, Waldo GL, Harden TK, Garrison JC. 1994. Selective activation of phospholipase C by recombinant G-protein α- and βγ-subunits. J. Biol. Chem. 269:2814-19
    • (1994) J. Biol. Chem. , vol.269 , pp. 2814-2819
    • Boyer, J.L.1    Graber, S.G.2    Waldo, G.L.3    Harden, T.K.4    Garrison, J.C.5
  • 153
    • 0029786995 scopus 로고    scopus 로고
    • A carboxyl-terminal mutant of the G protein β subunit deficient in the activation of phospholipase Cβ
    • In press
    • Zhang S, Coso OA, Collins R, Gutkind JS, Simonds WF. 1996. A carboxyl-terminal mutant of the G protein β subunit deficient in the activation of phospholipase Cβ. J. Biol. Chem. In press
    • (1996) J. Biol. Chem.
    • Zhang, S.1    Coso, O.A.2    Collins, R.3    Gutkind, J.S.4    Simonds, W.F.5
  • 155
    • 0026418426 scopus 로고
    • Type-specific regulation of adenylyl cyclase by G protein βγ subunits
    • Tang W, Gilman AG. 1991. Type-specific regulation of adenylyl cyclase by G protein βγ subunits. Science 254:1500-3
    • (1991) Science , vol.254 , pp. 1500-1503
    • Tang, W.1    Gilman, A.G.2
  • 156
    • 0025719492 scopus 로고
    • Cloning and expression of a widely distributed (type IV) adenylyl cyclase
    • Gao BN, Gilman AG. 1991. Cloning and expression of a widely distributed (type IV) adenylyl cyclase. Proc. Natl. Acad. Sci. USA 88:10178-82
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10178-10182
    • Gao, B.N.1    Gilman, A.G.2
  • 157
    • 0028133063 scopus 로고
    • Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases
    • Taussig R, Tang WJ, Hepler JR, Gilman AG. 1994. Distinct patterns of bidirectional regulation of mammalian adenylyl cyclases. J. Biol. Chem. 269:6093-100
    • (1994) J. Biol. Chem. , vol.269 , pp. 6093-6100
    • Taussig, R.1    Tang, W.J.2    Hepler, J.R.3    Gilman, A.G.4
  • 161
    • 0026611045 scopus 로고
    • z-mediated hormonal inhibition of cyclic AMP accumulation
    • z-mediated hormonal inhibition of cyclic AMP accumulation. Science 255:339-42
    • (1992) Science , vol.255 , pp. 339-342
    • Wong, Y.H.1    Conklin, B.R.2    Bourne, H.R.3
  • 162
    • 0029891289 scopus 로고    scopus 로고
    • Purification and characterization of a soluble form of mammalian adenylyl cyclase
    • Dessauer CW, Gilman AG. 1996. Purification and characterization of a soluble form of mammalian adenylyl cyclase. J. Biol. Chem. 271:16967-74
    • (1996) J. Biol. Chem. , vol.271 , pp. 16967-16974
    • Dessauer, C.W.1    Gilman, A.G.2
  • 163
    • 0029069790 scopus 로고
    • A region of adenylyl cyclase 2 critical for regulation by G protein βγ subunits
    • Chen JQ, DeVivo M, Dingus J, Harry A, Li JR, et al. 1995. A region of adenylyl cyclase 2 critical for regulation by G protein βγ subunits. Science 268:1166-69
    • (1995) Science , vol.268 , pp. 1166-1169
    • Chen, J.Q.1    DeVivo, M.2    Dingus, J.3    Harry, A.4    Li, J.R.5
  • 164
    • 0026785920 scopus 로고
    • Adenylyl cyclases
    • Tang WJ, Gilman AG. 1992. Adenylyl cyclases. Cell 70:869-72
    • (1992) Cell , vol.70 , pp. 869-872
    • Tang, W.J.1    Gilman, A.G.2
  • 166
    • 0027983908 scopus 로고
    • Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae
    • Choi K-Y, Satterberg B, Lyons DM, Elion EA. 1994. Ste5 tethers multiple protein kinases in the MAP kinase cascade required for mating in S. cerevisiae. Cell 78:499-512
    • (1994) Cell , vol.78 , pp. 499-512
    • Choi, K.-Y.1    Satterberg, B.2    Lyons, D.M.3    Elion, E.A.4
  • 167
    • 0026684825 scopus 로고
    • Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from NCB-20 cells
    • Yoshimura M, Cooper DM. 1992. Cloning and expression of a Ca(2+)-inhibitable adenylyl cyclase from NCB-20 cells. Proc. Natl. Acad. Sci. USA 89:6716-20
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 6716-6720
    • Yoshimura, M.1    Cooper, D.M.2
  • 170
    • 0028049921 scopus 로고
    • Conditional activation of cAMP signal transduction by protein kinase C: The effect of phorbol esters on adenylyl cyclase in permeabilized and intact cells
    • Morimoto BH, Koshland DJ. 1994. Conditional activation of cAMP signal transduction by protein kinase C: the effect of phorbol esters on adenylyl cyclase in permeabilized and intact cells. J. Biol. Chem. 269:4065-69
    • (1994) J. Biol. Chem. , vol.269 , pp. 4065-4069
    • Morimoto, B.H.1    Koshland, D.J.2
  • 171
    • 0027232606 scopus 로고
    • s-stimulated adenylyl cyclases
    • s-stimulated adenylyl cyclases. FASEB J. 7:768-75
    • (1993) FASEB J. , vol.7 , pp. 768-775
    • Iyengar, R.1
  • 172
    • 0028937625 scopus 로고
    • Identification of functional domains of adenylyl cyclase using in vivo chimeras
    • Levin LR, Reed RR. 1995. Identification of functional domains of adenylyl cyclase using in vivo chimeras. J. Biol. Chem. 270:7573-79
    • (1995) J. Biol. Chem. , vol.270 , pp. 7573-7579
    • Levin, L.R.1    Reed, R.R.2
  • 173
    • 0028093610 scopus 로고
    • CRAC, a cytosolic protein containing a pleckstrin homology domain, is required for receptor and G protein-mediated activation of adenylyl cyclase in Dictyostelium
    • Insall R, Kuspa A, Lilly PJ, Shaulsky G, Levin LR, et al. 1994. CRAC, a cytosolic protein containing a pleckstrin homology domain, is required for receptor and G protein-mediated activation of adenylyl cyclase in Dictyostelium. J. Cell Biol. 126:1537-45
    • (1994) J. Cell Biol. , vol.126 , pp. 1537-1545
    • Insall, R.1    Kuspa, A.2    Lilly, P.J.3    Shaulsky, G.4    Levin, L.R.5
  • 175
    • 0027368165 scopus 로고
    • Structure and mechanism of the G protein-coupled receptor kinases
    • Inglese J, Freedman NJ, Koch WJ, Lefkowitz RJ. 1993. Structure and mechanism of the G protein-coupled receptor kinases. J. Biol. Chem. 268:23735-38
    • (1993) J. Biol. Chem. , vol.268 , pp. 23735-23738
    • Inglese, J.1    Freedman, N.J.2    Koch, W.J.3    Lefkowitz, R.J.4
  • 176
    • 0027981478 scopus 로고
    • G protein-coupled receptor kinases
    • Haga T, Haga K, Kameyama K. 1994. G protein-coupled receptor kinases. J. Neurochem. 63:400-12
    • (1994) J. Neurochem. , vol.63 , pp. 400-412
    • Haga, T.1    Haga, K.2    Kameyama, K.3
  • 177
    • 0026803164 scopus 로고
    • Role of βγ subunits of G proteins in targeting the β-adrenergic receptor kinase to membrane-bound receptors
    • Pitcher JA, Inglese J, Higgins JB, Arriza JL, Casey PJ, et al. 1992. Role of βγ subunits of G proteins in targeting the β-adrenergic receptor kinase to membrane-bound receptors. Science 257:1264-67
    • (1992) Science , vol.257 , pp. 1264-1267
    • Pitcher, J.A.1    Inglese, J.2    Higgins, J.B.3    Arriza, J.L.4    Casey, P.J.5
  • 178
    • 0026793617 scopus 로고
    • Activation by G protein βγ subunits of agonistor light-dependent phosphorylation of muscarinic acetylcholine receptors and rhodopsin
    • Haga K, Haga T. 1992. Activation by G protein βγ subunits of agonistor light-dependent phosphorylation of muscarinic acetylcholine receptors and rhodopsin. J. Biol. Chem. 267:2222-27
    • (1992) J. Biol. Chem. , vol.267 , pp. 2222-2227
    • Haga, K.1    Haga, T.2
  • 179
    • 0027185782 scopus 로고
    • Mechanism of β-adrenergic receptor kinase activation by G proteins
    • Kim CM, Dion SB, Benovic JL. 1993. Mechanism of β-adrenergic receptor kinase activation by G proteins. J. Biol. Chem. 268:15412-18
    • (1993) J. Biol. Chem. , vol.268 , pp. 15412-15418
    • Kim, C.M.1    Dion, S.B.2    Benovic, J.L.3
  • 180
    • 0026726050 scopus 로고
    • Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases
    • Inglese J, Koch WJ, Caron MG, Lefkowitz RJ. 1992. Isoprenylation in regulation of signal transduction by G-protein-coupled receptor kinases. Nature 359:147-50
    • (1992) Nature , vol.359 , pp. 147-150
    • Inglese, J.1    Koch, W.J.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 181
    • 0028174070 scopus 로고
    • Association of the regulatory β-adrenergic receptor kinase with rat liver microsomal membranes
    • Garcia-Higuera I, Penela P, Murga C, Egea G, Bonay P, et al. 1994. Association of the regulatory β-adrenergic receptor kinase with rat liver microsomal membranes. J. Biol. Chem. 269:1348-55
    • (1994) J. Biol. Chem. , vol.269 , pp. 1348-1355
    • Garcia-Higuera, I.1    Penela, P.2    Murga, C.3    Egea, G.4    Bonay, P.5
  • 184
    • 0027055668 scopus 로고
    • Role of heterotrimeric G proteins in membrane traffic
    • Bomsel M, Mostov M. 1992. Role of heterotrimeric G proteins in membrane traffic. Mol. Biol. Cell 3:1317-28
    • (1992) Mol. Biol. Cell , vol.3 , pp. 1317-1328
    • Bomsel, M.1    Mostov, M.2
  • 185
    • 0028143425 scopus 로고
    • Detection of G-protein heterotrimers on large dense core and small synaptic vesicles of neuroendocrine and neuronal cells
    • Ahnert-Hilger G, Schafer T, Spicher K, Grund C, Schultz G, Wiedenmann B. 1994. Detection of G-protein heterotrimers on large dense core and small synaptic vesicles of neuroendocrine and neuronal cells. Eur. J. Cell Biol. 65:26-38
    • (1994) Eur. J. Cell Biol. , vol.65 , pp. 26-38
    • Ahnert-Hilger, G.1    Schafer, T.2    Spicher, K.3    Grund, C.4    Schultz, G.5    Wiedenmann, B.6
  • 186
    • 0026470765 scopus 로고
    • Multiple GTP-binding proteins regulate vesicular transport from the ER to Golgi membranes
    • Schwaninger R, Plutner H, Bokoch GM, Balch WE. 1992. Multiple GTP-binding proteins regulate vesicular transport from the ER to Golgi membranes. J. Cell Biol. 119:1077-96
    • (1992) J. Cell Biol. , vol.119 , pp. 1077-1096
    • Schwaninger, R.1    Plutner, H.2    Bokoch, G.M.3    Balch, W.E.4
  • 187
    • 0026598576 scopus 로고
    • Evidence of a role for heterotrimeric GTP-binding proteins in endosome fusion
    • Colombo MI, Mayorga LS, Casey PJ, Stahl PD. 1992. Evidence of a role for heterotrimeric GTP-binding proteins in endosome fusion. Science 255:1695-97
    • (1992) Science , vol.255 , pp. 1695-1697
    • Colombo, M.I.1    Mayorga, L.S.2    Casey, P.J.3    Stahl, P.D.4
  • 189
    • 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, et al. 1989. The STE4 and STE18 genes of yeast encode potential β and γ subunits of the mating factor receptor-coupled G protein. Cell 56:467-77
    • (1989) Cell , vol.56 , pp. 467-477
    • Whiteway, M.1    Hougan, L.2    Dignard, D.3    Thomas, D.Y.4    Bell, L.5
  • 190
    • 0027434614 scopus 로고
    • Interactions among the subunits of the G protein involved in Saccharomyces cerevisiae mating
    • Clark KL, Dignard D, Thomas DY, Whiteway M. 1993. Interactions among the subunits of the G protein involved in Saccharomyces cerevisiae mating. Mol. Cell Biol. 13:1-8
    • (1993) Mol. Cell Biol. , vol.13 , pp. 1-8
    • Clark, K.L.1    Dignard, D.2    Thomas, D.Y.3    Whiteway, M.4
  • 191
    • 0027982807 scopus 로고
    • Mutational activation of the STE5 gene product bypasses the requirement for G protein beta and gamma subunits in the yeast pheromone response pathway
    • Hasson MS, Blinder D, Thorner J, Jenness DD. 1994. Mutational activation of the STE5 gene product bypasses the requirement for G protein beta and gamma subunits in the yeast pheromone response pathway. Mol. Cell Biol. 14:1054-65
    • (1994) Mol. Cell Biol. , vol.14 , pp. 1054-1065
    • Hasson, M.S.1    Blinder, D.2    Thorner, J.3    Jenness, D.D.4
  • 193
    • 0029066439 scopus 로고
    • Molecular characterization of Ste20p, a potential mitogenactivated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cereviaiae
    • Wu C, Whiteway M, Thomas UY, Leberer E. 1995. Molecular characterization of Ste20p, a potential mitogenactivated protein or extracellular signal-regulated kinase kinase (MEK) kinase kinase from Saccharomyces cereviaiae. J. Biol. Chem. 270:15984-92
    • (1995) J. Biol. Chem. , vol.270 , pp. 15984-15992
    • Wu, C.1    Whiteway, M.2    Thomas, U.Y.3    Leberer, E.4
  • 194
    • 0028863672 scopus 로고
    • Truncated forms of a novel yeast protein suppress the lethality of a G protein a subunit deficiency by interacting with the β subunit
    • Spain BH, Koo D, Ramakrishnan M, Dzudzor B, Colicelli J. 1995. Truncated forms of a novel yeast protein suppress the lethality of a G protein a subunit deficiency by interacting with the β subunit. J. Biol. Chem. 270:25435-44
    • (1995) J. Biol. Chem. , vol.270 , pp. 25435-25444
    • Spain, B.H.1    Koo, D.2    Ramakrishnan, M.3    Dzudzor, B.4    Colicelli, J.5
  • 197
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits
    • Crespo P, Xu NZ, Simonds WF, Gutkind JS. 1994. Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits. Nature 369:418-20
    • (1994) Nature , vol.369 , pp. 418-420
    • Crespo, P.1    Xu, N.Z.2    Simonds, W.F.3    Gutkind, J.S.4
  • 198
    • 0028176297 scopus 로고
    • cAMP and βγ subunits of heterotrimeric G proteins stimulate the mitogen-activated protein kinase pathway in COS-7 cells
    • Faure M, Voyno-Yasenetskaya TA, Bourne HR. 1994. cAMP and βγ subunits of heterotrimeric G proteins stimulate the mitogen-activated protein kinase pathway in COS-7 cells. J. Biol. Chem. 269:7851-54
    • (1994) J. Biol. Chem. , vol.269 , pp. 7851-7854
    • Faure, M.1    Voyno-Yasenetskaya, T.A.2    Bourne, H.R.3
  • 200
    • 0028999856 scopus 로고
    • G protein βγ subunit activates Ras, Raf, and MAP kinase in HEK 293 cells
    • Ito A, Satoh T, Kaziro Y, Itoh H. 1995. G protein βγ subunit activates Ras, Raf, and MAP kinase in HEK 293 cells. FEBS Lett. 368:183-87
    • (1995) FEBS Lett. , vol.368 , pp. 183-187
    • Ito, A.1    Satoh, T.2    Kaziro, Y.3    Itoh, H.4
  • 202
    • 0028973270 scopus 로고
    • Dual effect of β-adrenergic receptors on mitogen-activated protein kinase
    • Crespo P, Cachera TG, Xu NZ, Gutkind JS. 1995. Dual effect of β-adrenergic receptors on mitogen-activated protein kinase. J. Biol. Chem. 270:25259-65
    • (1995) J. Biol. Chem. , vol.270 , pp. 25259-25265
    • Crespo, P.1    Cachera, T.G.2    Xu, N.Z.3    Gutkind, J.S.4
  • 204
    • 0029670821 scopus 로고    scopus 로고
    • G(o)-protein α-subunits activate mitogen-activated protein kinase via a novel protein kinase C-dependent mechanism
    • van Biesen T, Hawes BE, Raymond JR, Luttrell LM, Koch WJ, Lefkowitz RJ. 1996. G(o)-protein α-subunits activate mitogen-activated protein kinase via a novel protein kinase C-dependent mechanism. J. Biol. Chem. 271:1266-69
    • (1996) J. Biol. Chem. , vol.271 , pp. 1266-1269
    • Van Biesen, T.1    Hawes, B.E.2    Raymond, J.R.3    Luttrell, L.M.4    Koch, W.J.5    Lefkowitz, R.J.6
  • 205
    • 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, Hawkins PT. 1994. A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein βγ subunits. Cell 77:83-93
    • (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
  • 207
    • 0029664925 scopus 로고    scopus 로고
    • Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm exchange factor by muscarinic receptors and G protein βγ subunits
    • Mattingly RR, Macara IG. 1996. Phosphorylation-dependent activation of the Ras-GRF/CDC25Mm exchange factor by muscarinic receptors and G protein βγ subunits. Nature 382:268-72
    • (1996) Nature , vol.382 , pp. 268-272
    • Mattingly, R.R.1    Macara, I.G.2
  • 208
    • 0029002493 scopus 로고
    • A direct interaction between G-protein βγ subunits and the Raf-1 protein kinase
    • Pumiglia KM, LeVine H, Haske T, Habib T, Jove R, Decker SJ. 1995. A direct interaction between G-protein βγ subunits and the Raf-1 protein kinase. J. Biol. Chem. 270:14251-54
    • (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
  • 209
    • 0028173394 scopus 로고
    • Binding of βγ subunits ot heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase
    • Tsukada S, Simon MI, Witte ON Katz A. 1994. Binding of βγ subunits ot heterotrimeric G proteins to the PH domain of Bruton tyrosine kinase. Proc. Natl. Acad. Sci. USA 91:11256-60
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11256-11260
    • Tsukada, S.1    Simon, M.I.2    Witte, O.N.3    Katz, A.4
  • 211
    • 0022523427 scopus 로고
    • Interaction of GTP-binding proteins with calmodulin
    • Asano T, Ogasawara N, Kitajima S, Sano M. 1986. Interaction of GTP-binding proteins with calmodulin. FEBS Lett. 203:135-38
    • (1986) FEBS Lett. , vol.203 , pp. 135-138
    • Asano, T.1    Ogasawara, N.2    Kitajima, S.3    Sano, M.4
  • 212
    • 0023645429 scopus 로고
    • A novel mechanism for the inhibition of adenylate cyclase via inhibitory GTP-binding proteins
    • Katada T, Kusakabe K, Oinuma M, Ui M. 1987. A novel mechanism for the inhibition of adenylate cyclase via inhibitory GTP-binding proteins. J. Biol. Chem. 262:11897-900
    • (1987) J. Biol. Chem. , vol.262 , pp. 11897-11900
    • Katada, T.1    Kusakabe, K.2    Oinuma, M.3    Ui, M.4
  • 213
    • 0023668192 scopus 로고
    • A novel complex from bovine visual cells of a 33,000 dalton phosphoprotein with band γ transducin: Purification and subunit structure
    • Lee RH, Lieberman BS, Lolley RN. 1987. A novel complex from bovine visual cells of a 33,000 dalton phosphoprotein with band γ transducin: purification and subunit structure. Biochemistry 26:3983-90
    • (1987) Biochemistry , vol.26 , pp. 3983-3990
    • Lee, R.H.1    Lieberman, B.S.2    Lolley, R.N.3
  • 214
    • 0024339789 scopus 로고
    • Isolation of a novel retina-specific clone (MEKA cDNA) encoding a photoreceptor soluble protein Mol
    • Kuo C-H. 1989. Isolation of a novel retina-specific clone (MEKA cDNA) encoding a photoreceptor soluble protein Mol. Brain Res. 6:1-10
    • (1989) Brain Res. , vol.6 , pp. 1-10
    • Kuo, C.-H.1
  • 215
    • 0025120917 scopus 로고
    • Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein from photoreceptor cells
    • Lee RH, Fowler A, McGinnis JF, Lolley RN, Craft CM. 1990. Amino acid and cDNA sequence of bovine phosducin, a soluble phosphoprotein from photoreceptor cells. J. Biol. Chem. 265:15867-73
    • (1990) J. Biol. Chem. , vol.265 , pp. 15867-15873
    • Lee, R.H.1    Fowler, A.2    McGinnis, J.F.3    Lolley, R.N.4    Craft, C.M.5
  • 216
    • 0025236741 scopus 로고
    • Pineal transduction: Adrenergic cyclic AMP-dependent phosphorylation of cytoplasmic 33-kDA protein (MEKA) which binds βγ-complex of transducin
    • Reig JA, Klein DC. 1990. Pineal transduction: Adrenergic cyclic AMP-dependent phosphorylation of cytoplasmic 33-kDA protein (MEKA) which binds βγ-complex of transducin. J. Biol. Chem. 267:5816-24
    • (1990) J. Biol. Chem. , vol.267 , pp. 5816-5824
    • Reig, J.A.1    Klein, D.C.2
  • 217
    • 0025989987 scopus 로고
    • Rat pineal gland phosducin: cDNA isolation, nucleotide sequence, and chromosomal assignment in the mouse
    • Craft CM, Lolley RN, Seldin MF, Lee RH. 1991. Rat pineal gland phosducin: cDNA isolation, nucleotide sequence, and chromosomal assignment in the mouse. Genomics 10:400-9
    • (1991) Genomics , vol.10 , pp. 400-409
    • Craft, C.M.1    Lolley, R.N.2    Seldin, M.F.3    Lee, R.H.4
  • 218
    • 0026716049 scopus 로고
    • Phosducin is a protein kinase A-regulated G-protein regulator
    • Bauer PH, Muller S, Puzicha M, Pippig S, Obermaier B, et al. 1992. Phosducin is a protein kinase A-regulated G-protein regulator. Nature 358:73-76
    • (1992) Nature , vol.358 , pp. 73-76
    • Bauer, P.H.1    Muller, S.2    Puzicha, M.3    Pippig, S.4    Obermaier, B.5
  • 219
    • 0026453108 scopus 로고
    • Regulation of retinal cGMP cascade by phosducin in bovine rod photoreceptor cells: Interaction of phosducin and transducin
    • Lee RH, Ting TD, Lieberman BS, Tobias DE, Lolley RN, Ho Y-K. 1992. Regulation of retinal cGMP cascade by phosducin in bovine rod photoreceptor cells: Interaction of phosducin and transducin. J. Biol. Chem. 267:25104-12
    • (1992) J. Biol. Chem. , vol.267 , pp. 25104-25112
    • Lee, R.H.1    Ting, T.D.2    Lieberman, B.S.3    Tobias, D.E.4    Lolley, R.N.5    Ho, Y.-K.6
  • 220
    • 0027971161 scopus 로고
    • The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin
    • Yoshida T, Willardson BM, Wilkins JF, Jensen GJ, Thornton BD, Bitensky MW. 1994. The phosphorylation state of phosducin determines its ability to block transducin subunit interactions and inhibit transducin binding to activated rhodopsin. J. Biol. Chem. 269:24050-57
    • (1994) J. Biol. Chem. , vol.269 , pp. 24050-24057
    • Yoshida, T.1    Willardson, B.M.2    Wilkins, J.F.3    Jensen, G.J.4    Thornton, B.D.5    Bitensky, M.W.6
  • 221
    • 0028223896 scopus 로고
    • Phosducin inhibits receptor phosphorylation by the β-adrenergic receptor kinase in a PKA-regulated manner
    • Hekman M, Bauer PH, Sohlemann P, Lohse MJ. 1994. Phosducin inhibits receptor phosphorylation by the β-adrenergic receptor kinase in a PKA-regulated manner. FEBS Lett. 343:120-24
    • (1994) FEBS Lett. , vol.343 , pp. 120-124
    • Hekman, M.1    Bauer, P.H.2    Sohlemann, P.3    Lohse, M.J.4
  • 223
    • 0029935648 scopus 로고    scopus 로고
    • Inhibition of G-protein βγ-subunit functions by phosducin-like protein
    • Schröder S, Lohse MJ. 1996. Inhibition of G-protein βγ-subunit functions by phosducin-like protein. Proc. Natl. Acad. Sci. USA 93:2100-4
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 2100-2104
    • Schröder, S.1    Lohse, M.J.2
  • 224
    • 0028968341 scopus 로고
    • The N terminus of phosducin is involved in binding of βγ subunits of G protein
    • Xu J, Wu DQ, Slepak VZ, Simon MI. 1995. The N terminus of phosducin is involved in binding of βγ subunits of G protein. Proc. Natl. Acad. Sci. USA 92:2086-90
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 2086-2090
    • Xu, J.1    Wu, D.Q.2    Slepak, V.Z.3    Simon, M.I.4
  • 226
    • 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, Sigler PB. 1996. Crystal structure at 2.4 Å resolution of the complex of transducin βγ and its regulator, phosducin. Cell 87:577-88
    • (1996) Cell , vol.87 , pp. 577-588
    • Gaudet, R.1    Bohm, A.2    Sigler, P.B.3
  • 227
    • 0029939448 scopus 로고    scopus 로고
    • PH domains: Diverse sequences with a common fold recruit signaling molecules to the cell surface
    • Lemmon MA, Ferguson KM, Schlessinger J. 1996. PH domains: diverse sequences with a common fold recruit signaling molecules to the cell surface. Cell 85:621-24
    • (1996) Cell , vol.85 , pp. 621-624
    • Lemmon, M.A.1    Ferguson, K.M.2    Schlessinger, J.3
  • 230
    • 0027945789 scopus 로고
    • Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamic
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. 1994. Crystal structure at 2.2 Å resolution of the pleckstrin homology domain from human dynamic. Cell 79:199-209
    • (1994) Cell , vol.79 , pp. 199-209
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4
  • 232
    • 0027304398 scopus 로고
    • Identification of novel pleckstrin homology (PH) domains provided a hypothesis for PH domain function
    • Shaw G. 1993. Identification of novel pleckstrin homology (PH) domains provided a hypothesis for PH domain function. Biochem. Biophys. Res. Commun. 195:1145-51
    • (1993) Biochem. Biophys. Res. Commun. , vol.195 , pp. 1145-1151
    • Shaw, G.1
  • 237
    • 0028021882 scopus 로고
    • Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate
    • Harlan JE, Hajduk PJ, Yoon HS, Fesik SW. 1994. Pleckstrin homology domains bind to phosphatidylinositol-4,5-bisphosphate. Nature 371:168-70
    • (1994) Nature , vol.371 , pp. 168-170
    • Harlan, J.E.1    Hajduk, P.J.2    Yoon, H.S.3    Fesik, S.W.4
  • 238
    • 0029617615 scopus 로고
    • Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain
    • Ferguson KM, Lemmon MA, Schlessinger J, Sigler PB. 1995. Structure of the high affinity complex of inositol trisphosphate with a phospholipase C pleckstrin homology domain. Cell 83:1037-46
    • (1995) Cell , vol.83 , pp. 1037-1046
    • Ferguson, K.M.1    Lemmon, M.A.2    Schlessinger, J.3    Sigler, P.B.4


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