메뉴 건너뛰기




Volumn 36, Issue , 1996, Pages 481-509

Regulation of phosphoinositide phospholipases by hormones, neurotransmitters, and other agonists linked to G proteins

Author keywords

calcium; diacylglycerol; G(i); G(q); protein kinase C; receptors

Indexed keywords

CALCIUM; DIACYLGLYCEROL; GROWTH FACTOR; GUANINE NUCLEOTIDE BINDING PROTEIN; HORMONE; INOSITOL TRISPHOSPHATE; ISOENZYME; NEUROTRANSMITTER; PHOSPHATIDYLINOSITOL 4,5 BISPHOSPHATE PHOSPHODIESTERASE; PROTEIN KINASE C;

EID: 0029936331     PISSN: 00664251     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.pa.36.040196.002405     Document Type: Review
Times cited : (307)

References (180)
  • 1
    • 0027397544 scopus 로고
    • Inositol trisphosphate and calcium signalling
    • Berridge MJ. 1993. Inositol trisphosphate and calcium signalling. Nature 361:315-25
    • (1993) Nature , vol.361 , pp. 315-325
    • Berridge, M.J.1
  • 2
    • 0026578166 scopus 로고
    • Inositol 1,4,5-trisphosphate-activated calcium channels
    • Ferns CD, Snyder SH. 1992. Inositol 1,4,5-trisphosphate-activated calcium channels. Annu. Rev. Physiol. 54:469-88
    • (1992) Annu. Rev. Physiol. , vol.54 , pp. 469-488
    • Ferns, C.D.1    Snyder, S.H.2
  • 3
    • 0027512040 scopus 로고
    • Inositol 1,4,5-trisphosphate receptor
    • Mikoshiba K. 1993. Inositol 1,4,5-trisphosphate receptor. Trends Pharmacol. Sci. 14:86-89
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 86-89
    • Mikoshiba, K.1
  • 5
    • 0027926582 scopus 로고
    • A tale of two messengers
    • Berridge MJ. 1993. A tale of two messengers. Nature 365:388-89
    • (1993) Nature , vol.365 , pp. 388-389
    • Berridge, M.J.1
  • 6
    • 0028128083 scopus 로고
    • Cyclic ADP-ribose, the ADP-ribosyl cyclase pathway and calcium signalling
    • Galione A. 1994. Cyclic ADP-ribose, the ADP-ribosyl cyclase pathway and calcium signalling. Mol. Cell. Endocrinol. 98:125-31
    • (1994) Mol. Cell. Endocrinol. , vol.98 , pp. 125-131
    • Galione, A.1
  • 7
    • 0028298064 scopus 로고
    • Spatial and temporal signalling by calcium
    • Berridge MJ, Dupont G. 1994. Spatial and temporal signalling by calcium. Curr. Opin. Cell Biol. 6:267-74
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 267-274
    • Berridge, M.J.1    Dupont, G.2
  • 8
    • 0026655484 scopus 로고
    • Receptor classes and the transmitter-gated ion channels
    • Barnard EA. 1992. Receptor classes and the transmitter-gated ion channels. Trends Biochem. Sci. 17:368-74
    • (1992) Trends Biochem. Sci. , vol.17 , pp. 368-374
    • Barnard, E.A.1
  • 9
    • 0026018776 scopus 로고
    • Regulation of calcium channel activity by GTP binding proteins and second messengers
    • Dolphin AC. 1991. Regulation of calcium channel activity by GTP binding proteins and second messengers. Biochim. Biophys. Acta 1091:68-80
    • (1991) Biochim. Biophys. Acta , vol.1091 , pp. 68-80
    • Dolphin, A.C.1
  • 10
    • 0027422088 scopus 로고
    • The signal for capacitative calcium entry
    • Putney JW Jr. 1993. The signal for capacitative calcium entry. Cell 75:199-201
    • (1993) Cell , vol.75 , pp. 199-201
    • Putney Jr., J.W.1
  • 12
    • 0028899481 scopus 로고
    • Chromatographic resolution of an intracellular calcium influx factor from thapsigargin-activated Jurkat cells
    • 11b. Kim HY, Thomas D, Hanley MR. 1995. Chromatographic resolution of an intracellular calcium influx factor from thapsigargin-activated Jurkat cells. J. Biol. Chem. 270:9706-8
    • (1995) J. Biol. Chem. , vol.270 , pp. 9706-9708
    • Kim, H.Y.1    Thomas, D.2    Hanley, M.R.3
  • 13
    • 0026451081 scopus 로고
    • Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C
    • Nishizuka Y. 1992. Intracellular signaling by hydrolysis of phospholipids and activation of protein kinase C. Science 258:607-14
    • (1992) Science , vol.258 , pp. 607-614
    • Nishizuka, Y.1
  • 14
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug H, Sarre TF. 1993. Protein kinase C isoenzymes: divergence in signal transduction? Biochem. J. 291:329-43
    • (1993) Biochem. J. , vol.291 , pp. 329-343
    • Hug, H.1    Sarre, T.F.2
  • 15
    • 0027253641 scopus 로고
    • Differential translocation of protein kinase C isozymes by thrombin and platelet-derived growth factor
    • Ha K-S, Exton JH. 1993. Differential translocation of protein kinase C isozymes by thrombin and platelet-derived growth factor. J. Biol. Chem. 268: 10534-39
    • (1993) J. Biol. Chem. , vol.268 , pp. 10534-10539
    • Ha, K.-S.1    Exton, J.H.2
  • 16
    • 0027392102 scopus 로고
    • The MARCKS family of cellular protein kinase C substrate
    • Blackshear PJ. 1993. The MARCKS family of cellular protein kinase C substrate. J. Biol. Chem. 268:1501-4
    • (1993) J. Biol. Chem. , vol.268 , pp. 1501-1504
    • Blackshear, P.J.1
  • 18
    • 0027496454 scopus 로고
    • Convergent regulation of sodium channels by protein kinase C and cAMP-dependent protein kinase
    • Li M, West JW, Numann R, Murphy BJ, Scheur T, Catterall WA. 1993. Convergent regulation of sodium channels by protein kinase C and cAMP-dependent protein kinase. Science 261:1439-42
    • (1993) Science , vol.261 , pp. 1439-1442
    • Li, M.1    West, J.W.2    Numann, R.3    Murphy, B.J.4    Scheur, T.5    Catterall, W.A.6
  • 19
    • 0026055340 scopus 로고
    • Mechanisms of receptor-mediated regulation of Na-H exchange
    • Barber DL. 1991. Mechanisms of receptor-mediated regulation of Na-H exchange. Cell. Signal. 3:387-97
    • (1991) Cell. Signal , vol.3 , pp. 387-397
    • Barber, D.L.1
  • 20
    • 0028296793 scopus 로고
    • Phosphatidylcholine breakdown and signal transduction
    • Exton JH. 1994. Phosphatidylcholine breakdown and signal transduction. Biochim. Biophys. Acta 1212:26-42
    • (1994) Biochim. Biophys. Acta , vol.1212 , pp. 26-42
    • Exton, J.H.1
  • 21
    • 0026459635 scopus 로고
    • PI-specific phospholipase C "α" from sheep seminal vesicles is a proteolytic fragment of PI-PLCδ
    • Taylor CD, Fee JA, Silbert DF, Hofmann SL. 1992. PI-specific phospholipase C "α" from sheep seminal vesicles is a proteolytic fragment of PI-PLCδ. Biochem. Biophys. Res. Commun. 188: 1176-83
    • (1992) Biochem. Biophys. Res. Commun. , vol.188 , pp. 1176-1183
    • Taylor, C.D.1    Fee, J.A.2    Silbert, D.F.3    Hofmann, S.L.4
  • 22
    • 0025830169 scopus 로고
    • Purification and characterization of a new isozyme of thiol protein-disulfide oxidoreductase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A
    • Srivastava SP, Chen NQ, Liu YX, Holtzman JL. 1991. Purification and characterization of a new isozyme of thiol protein-disulfide oxidoreductase from rat hepatic microsomes. Relationship of this isozyme to cytosolic phosphatidylinositol-specific phospholipase C form 1A. J. Biol. Chem. 266:20337-44
    • (1991) J. Biol. Chem. , vol.266 , pp. 20337-20344
    • Srivastava, S.P.1    Chen, N.Q.2    Liu, Y.X.3    Holtzman, J.L.4
  • 23
    • 0027281905 scopus 로고
    • The reported cDNA sequence for phospholipase Cα encodes protein disuifide isomerase, isozyme Q-2 and not phospholipase-C
    • Srivastava SP, Fuchs JA, Holtzman JL. 1993. The reported cDNA sequence for phospholipase Cα encodes protein disuifide isomerase, isozyme Q-2 and not phospholipase-C. Biochem. Biophys. Res. Commun. 193:971-78
    • (1993) Biochem. Biophys. Res. Commun. , vol.193 , pp. 971-978
    • Srivastava, S.P.1    Fuchs, J.A.2    Holtzman, J.L.3
  • 25
    • 0028986998 scopus 로고
    • 2 hydrolysis and regulation of phospholipase C isozymes
    • 2 hydrolysis and regulation of phospholipase C isozymes. Curr. Opin. Cell Biol. 7 183-89
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 183-189
    • Lee, S.1    Rhee, S.G.2
  • 27
    • 0027508316 scopus 로고
    • Purification, molecular cloning, and sequencing of phospholipase C-β4
    • Lee C-W, Park DJ, Lee K-H, Kim CG, Rhee SG. 1993. Purification, molecular cloning, and sequencing of phospholipase C-β4. J. Biol. Chem. 268:21318-27
    • (1993) J. Biol. Chem. , vol.268 , pp. 21318-21327
    • Lee, C.-W.1    Park, D.J.2    Lee, K.-H.3    Kim, C.G.4    Rhee, S.G.5
  • 29
    • 0028921612 scopus 로고
    • Purification, characterization, and partial amino acid sequence of a G protein-activated phospholipase C from squid photoreceptors
    • Mitchell J, Gutierrez J, Northup JK. 1995. Purification, characterization, and partial amino acid sequence of a G protein-activated phospholipase C from squid photoreceptors. J. Biol. Chem. 270: 854-59
    • (1995) J. Biol. Chem. , vol.270 , pp. 854-859
    • Mitchell, J.1    Gutierrez, J.2    Northup, J.K.3
  • 30
    • 0026732665 scopus 로고
    • Molecular cloning and expression of a phosphoinositide-specific phospholipase C of Dictyostelium discoideum
    • Drayer AL, van Haastert PJM. 1992. Molecular cloning and expression of a phosphoinositide-specific phospholipase C of Dictyostelium discoideum. J. Biol. Chem. 267:18387-92
    • (1992) J. Biol. Chem. , vol.267 , pp. 18387-18392
    • Drayer, A.L.1    Van Haastert, P.J.M.2
  • 31
    • 0027403714 scopus 로고
    • The putative phosphoinositide-specific phospholipase C gene, PLC1, of the yeast Saccharomyces cerevisiae is important for cell growth
    • Yoko-O T, Matsui Y, Yagisawa H, Nojima H, Uno I, Toh-E A. 1993. The putative phosphoinositide-specific phospholipase C gene, PLC1, of the yeast Saccharomyces cerevisiae is important for cell growth. Proc. Natl. Acad. Sci. USA 90:1804-8
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 1804-1808
    • Yoko-O, T.1    Matsui, Y.2    Yagisawa, H.3    Nojima, H.4    Uno, I.5    Toh-E, A.6
  • 32
    • 0027304451 scopus 로고
    • Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae
    • Flick JS, Thorner J. 1993. Genetic and biochemical characterization of a phosphatidylinositol-specific phospholipase C in Saccharomyces cerevisiae. Mol. Cell. Biol. 13:5861-76
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 5861-5876
    • Flick, J.S.1    Thorner, J.2
  • 33
    • 0025866362 scopus 로고
    • Immunolocalization of phospholipase C-γ in rat embryo fibroblasts
    • McBride K, Rhee SG, Jaken S. 1991. Immunolocalization of phospholipase C-γ in rat embryo fibroblasts. Proc. Natl. Acad. Sci. USA 88:7111-15
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7111-7115
    • McBride, K.1    Rhee, S.G.2    Jaken, S.3
  • 34
    • 0028263973 scopus 로고
    • Epidermal growth factor-induced activation and translocation of phospholipase C-γ1 to the cytoskeleton in rat hepatocytes
    • Yang IJ, Rhee SG, Williamson JR. 1994. Epidermal growth factor-induced activation and translocation of phospholipase C-γ1 to the cytoskeleton in rat hepatocytes. J. Biol Chem 269:7156-62
    • (1994) J. Biol Chem , vol.269 , pp. 7156-7162
    • Yang, I.J.1    Rhee, S.G.2    Williamson, J.R.3
  • 36
    • 0027446592 scopus 로고
    • Phosphoinositide signalling enzymes in rat liver nuclei: Phosphoinositidase C isoform β1 is specifically, but not predominantly, located in the nucleus
    • Divecha N, Rhee SG, Letcher AJ, Irvine RF. 1993. Phosphoinositide signalling enzymes in rat liver nuclei: phosphoinositidase C isoform β1 is specifically, but not predominantly, located in the nucleus. Biochem. J. 289: 617-20
    • (1993) Biochem. J. , vol.289 , pp. 617-620
    • Divecha, N.1    Rhee, S.G.2    Letcher, A.J.3    Irvine, R.F.4
  • 37
    • 0028339978 scopus 로고
    • Purification and characterization of nuclear phospholipase C specific for phosphoinositides
    • Asano M, Tamiya-Koizumi T, Homma Y, Takenawa T, Nimura Y, et al. 1994. Purification and characterization of nuclear phospholipase C specific for phosphoinositides J Biol. Chem. 269: 12360-66
    • (1994) J Biol. Chem. , vol.269 , pp. 12360-12366
    • Asano, M.1    Tamiya-Koizumi, T.2    Homma, Y.3    Takenawa, T.4    Nimura, Y.5
  • 38
    • 0026452643 scopus 로고
    • Receptor tyrosine kinase substrates; src homology domains and signal transduction
    • Carpenter G. 1992. Receptor tyrosine kinase substrates; src homology domains and signal transduction. FASEB J. 6:3283-89
    • (1992) FASEB J. , vol.6 , pp. 3283-3289
    • Carpenter, G.1
  • 39
    • 0028589148 scopus 로고
    • Platelet-derived growth factor receptor signals
    • Claesson-Welsh L. 1994. Platelet-derived growth factor receptor signals. J. Biol. Chem. 269:32023-26
    • (1994) J. Biol. Chem. , vol.269 , pp. 32023-32026
    • Claesson-Welsh, L.1
  • 40
    • 0028859279 scopus 로고
    • Protein modules and signalling networks
    • Pawson T. 1995. Protein modules and signalling networks. Nature 373:573-80
    • (1995) Nature , vol.373 , pp. 573-580
    • Pawson, T.1
  • 41
    • 0025805394 scopus 로고
    • PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254
    • Kim HK, Kim JW, Zilberstein A, Margolis B, Kim JG, et al. 1991. PDGF stimulation of inositol phospholipid hydrolysis requires PLC-γ1 phosphorylation on tyrosine residues 783 and 1254. Cell 65:435-41
    • (1991) Cell , vol.65 , pp. 435-441
    • Kim, H.K.1    Kim, J.W.2    Zilberstein, A.3    Margolis, B.4    Kim, J.G.5
  • 42
    • 0026700487 scopus 로고
    • Growth factor stimulation of phospholipase C-γ1 activity. Comparative properties of control and activated enzymes
    • Wahl MI, Jones GA, Nishibe S, Rhee SG, Carpenter G. 1992. Growth factor stimulation of phospholipase C-γ1 activity. Comparative properties of control and activated enzymes. J. Biol. Chem. 267:10447-56
    • (1992) J. Biol. Chem. , vol.267 , pp. 10447-10456
    • Wahl, M.I.1    Jones, G.A.2    Nishibe, S.3    Rhee, S.G.4    Carpenter, G.5
  • 44
    • 0023631429 scopus 로고
    • Epidermal growth factor and angiotensin II stimulate formation of inositol 1,4,5- and inositol 1,3,4-trisphosphate in hepatocytes. Differential inhibition by pertussis toxin and phorbol 12-myristate 13- acetate
    • Johnson RM, Garrison JC. 1987. Epidermal growth factor and angiotensin II stimulate formation of inositol 1,4,5- and inositol 1,3,4-trisphosphate in hepatocytes. Differential inhibition by pertussis toxin and phorbol 12-myristate 13- acetate. J. Biol. Chem. 262:17285-93
    • (1987) J. Biol. Chem. , vol.262 , pp. 17285-17293
    • Johnson, R.M.1    Garrison, J.C.2
  • 45
    • 0027053776 scopus 로고
    • Epidermal growth factor activates phospholipase C in rat hepatocytes via a different mechanism from that m A431 or RatlhER cells
    • Liang M, Garrison JC. 1992. Epidermal growth factor activates phospholipase C in rat hepatocytes via a different mechanism from that m A431 or RatlhER cells. Mol. Pharmacol. 42:743-52
    • (1992) Mol. Pharmacol. , vol.42 , pp. 743-752
    • Liang, M.1    Garrison, J.C.2
  • 48
    • 0026448369 scopus 로고
    • Tyrosine kinases and tyrosine-based activation motifs
    • Samelson LE, Klausner RD. 1992. Tyrosine kinases and tyrosine-based activation motifs. J. Biol. Chem. 267: 24913-16
    • (1992) J. Biol. Chem. , vol.267 , pp. 24913-24916
    • Samelson, L.E.1    Klausner, R.D.2
  • 49
    • 0028288927 scopus 로고
    • The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction
    • Chan AC, Desai DM, Weis A. 1994. The role of protein tyrosine kinases and protein tyrosine phosphatases in T cell antigen receptor signal transduction. Annu. Rev. Immunol. 12:555-92
    • (1994) Annu. Rev. Immunol. , vol.12 , pp. 555-592
    • Chan, A.C.1    Desai, D.M.2    Weis, A.3
  • 51
    • 0025835006 scopus 로고
    • T-cell antigen receptor ligations induce tyrosine phosphorylation of phospholipase C-γ1
    • Secrist JP, Kamitz L, Abraham RT. 1991. T-cell antigen receptor ligations induce tyrosine phosphorylation of phospholipase C-γ1. J. Biol. Chem. 266: 12135-39
    • (1991) J. Biol. Chem. , vol.266 , pp. 12135-12139
    • Secrist, J.P.1    Kamitz, L.2    Abraham, R.T.3
  • 52
    • 0026095639 scopus 로고
    • Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-γ1
    • Weiss A, Koretzky G, Schatzman RC, Kadlecek T. 1991. Functional activation of the T-cell antigen receptor induces tyrosine phosphorylation of phospholipase C-γ1. Proc. Natl. Acad. Sci. USA 88:5484-88
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 5484-5488
    • Weiss, A.1    Koretzky, G.2    Schatzman, R.C.3    Kadlecek, T.4
  • 53
    • 0025849698 scopus 로고
    • Tyrosine phosphorylation of phospholipase C induced by membrane immunoglobulin in B lymphocytes
    • Carter RH, Park DJ, Rhee SG, Fearon DT. 1991. Tyrosine phosphorylation of phospholipase C induced by membrane immunoglobulin in B lymphocytes. Proc. Natl. Acad. Sci. USA 88:2745-49
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 2745-2749
    • Carter, R.H.1    Park, D.J.2    Rhee, S.G.3    Fearon, D.T.4
  • 54
    • 0026352438 scopus 로고
    • IgE-induced tyrosine phosphorylation of phospholipase C-γ1 in rat basophilic leukemia cells
    • Park DJ, Min HK, Rhee SG. 1991. IgE-induced tyrosine phosphorylation of phospholipase C-γ1 in rat basophilic leukemia cells. J. Biol. Chem. 266: 24237-40
    • (1991) J. Biol. Chem. , vol.266 , pp. 24237-24240
    • Park, D.J.1    Min, H.K.2    Rhee, S.G.3
  • 55
    • 0026581309 scopus 로고
    • Tyrosine phosphorylation of phospholipase C-γ1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgbG in U937 cells
    • Liao F, Shin HS, Rhee SG. 1992. Tyrosine phosphorylation of phospholipase C-γ1 induced by cross-linking of the high-affinity or low-affinity Fc receptor for IgbG in U937 cells. Proc. Natl. Acad. Sci. USA 89:3659-63
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 3659-3663
    • Liao, F.1    Shin, H.S.2    Rhee, S.G.3
  • 56
    • 0026729146 scopus 로고
    • Predominant expression and activation-induced tyrosine phosphorylation of phospholipase C-γ2 in B lymphocytes
    • Coggeshall KM, McHugh JC, Altman A. 1992. Predominant expression and activation-induced tyrosine phosphorylation of phospholipase C-γ2 in B lymphocytes. Proc. Natl. Acad. Sci. USA 89:5660-64
    • (1992) Proc. Natl. Acad. Sci. USA , vol.89 , pp. 5660-5664
    • Coggeshall, K.M.1    McHugh, J.C.2    Altman, A.3
  • 57
    • 0025162775 scopus 로고
    • Purification from bovine liver membranes of a guanine nucleotide-dependent activator of phosphoinositide-specific phospholipase C. Immunologic identification as a novel G-protein α subunit
    • Taylor SJ, Smith JA, Exton JH. 1990. Purification from bovine liver membranes of a guanine nucleotide-dependent activator of phosphoinositide-specific phospholipase C. Immunologic identification as a novel G-protein α subunit. J. Biol. Chem. 265:17150-56
    • (1990) J. Biol. Chem. , vol.265 , pp. 17150-17156
    • Taylor, S.J.1    Smith, J.A.2    Exton, J.H.3
  • 59
    • 0025016132 scopus 로고
    • Purification of unique a subunits of GTP-binding regulatory proteins (G proteins) by affinity chromatography with immobilized βγ subunits
    • Pang I-H, Sternweis PC. 1990. Purification of unique a subunits of GTP-binding regulatory proteins (G proteins) by affinity chromatography with immobilized βγ subunits. J. Biol. Chem. 265: 18707-12
    • (1990) J. Biol. Chem. , vol.265 , pp. 18707-18712
    • Pang, I.-H.1    Sternweis, P.C.2
  • 60
    • 0025695580 scopus 로고
    • G protein diversity: A distinct class of a subunits is present in vertebrates and invertebrates
    • Strathmann M, Simon MI. 1990. G protein diversity: A distinct class of a subunits is present in vertebrates and invertebrates. Proc. Natl Acad. Sci. USA 87:9113-17
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 9113-9117
    • Strathmann, M.1    Simon, M.I.2
  • 61
    • 0025923550 scopus 로고
    • q class of G proteins stimulate phosphoinositide phospholipase C-β1 activity
    • q class of G proteins stimulate phosphoinositide phospholipase C-β1 activity. FEBS Lett. 286:214-16
    • (1991) FEBS Lett. , vol.286 , pp. 214-216
    • Taylor, S.J.1    Exton, J.H.2
  • 64
    • 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
  • 71
    • 0025097866 scopus 로고
    • Multiple second messenger pathways of α-adrenergic receptor subtypes expressed in eukaryotic cells
    • Cotecchia S, Kobilka BK, Daniel KW, Nolan RD, Lapetina EY, et al. 1990. Multiple second messenger pathways of α-adrenergic receptor subtypes expressed in eukaryotic cells. J. Biol. Chem. 265:63-69
    • (1990) J. Biol. Chem. , vol.265 , pp. 63-69
    • Cotecchia, S.1    Kobilka, B.K.2    Daniel, K.W.3    Nolan, R.D.4    Lapetina, E.Y.5
  • 72
    • 0024498192 scopus 로고
    • Functionally distinct G proteins selectively couple different receptors to PI hydrolysis in the same cell
    • Ashkenazi A, Peralta EG, Winslow JW, Ramachandran J, Capon DJ. 1989. Functionally distinct G proteins selectively couple different receptors to PI hydrolysis in the same cell. Cell 56:487-93
    • (1989) Cell , vol.56 , pp. 487-493
    • Ashkenazi, A.1    Peralta, E.G.2    Winslow, J.W.3    Ramachandran, J.4    Capon, D.J.5
  • 73
    • 0023032152 scopus 로고
    • Direct evidence for involvement of a guanine nucleotide-binding protein in chemotactic peptide-stimulated formation of inositol bisphosphate and trisphosphate in differentiated human leukemic (HL-60) cells
    • Kikuchi A, Kozawa O, Kaibuchi K, Katada T, Ui M, et al. 1986. Direct evidence for involvement of a guanine nucleotide-binding protein in chemotactic peptide-stimulated formation of inositol bisphosphate and trisphosphate in differentiated human leukemic (HL-60) cells. J. Biol. Chem. 261:11558-62
    • (1986) J. Biol. Chem. , vol.261 , pp. 11558-11562
    • Kikuchi, A.1    Kozawa, O.2    Kaibuchi, K.3    Katada, T.4    Ui, M.5
  • 74
    • 0025191971 scopus 로고
    • o protein as a signal transducer in the pertussis toxin-sensitive phosphatidylinositol pathway
    • o protein as a signal transducer in the pertussis toxin-sensitive phosphatidylinositol pathway. Nature 343:79-82
    • (1990) Nature , vol.343 , pp. 79-82
    • Moriarty, T.M.1    Padrell, E.2    Carty, D.J.3    Omri, G.4    Landau, E.M.5
  • 83
    • 0028082134 scopus 로고
    • Bradykinin modulates potassium and calcium currents in neuroblastoma hybrid cells via different pertussis toxin-insensitive pathways
    • Wilk-Blaszczak MA, Gutowski S, Sternweis PC, Belardetti F. 1994. Bradykinin modulates potassium and calcium currents in neuroblastoma hybrid cells via different pertussis toxin-insensitive pathways. Neuron 12:109-16
    • (1994) Neuron , vol.12 , pp. 109-116
    • Wilk-Blaszczak, M.A.1    Gutowski, S.2    Sternweis, P.C.3    Belardetti, F.4
  • 84
    • 0023773004 scopus 로고
    • Differential regulation of PI hydrolysis and adenylate cyclase by muscarinic receptor subtypes
    • Peralta EG, Ashkenazi A, Window JW, Ramachandran J, Capon DJ. 1988. Differential regulation of PI hydrolysis and adenylate cyclase by muscarinic receptor subtypes. Nature 334:434-37
    • (1988) Nature , vol.334 , pp. 434-437
    • Peralta, E.G.1    Ashkenazi, A.2    Window, J.W.3    Ramachandran, J.4    Capon, D.J.5
  • 86
    • 0025724957 scopus 로고
    • q subfamily of guanine nucleotide-binding regulatory protein α subunits attenuate activation of phosphatidylinositol 4,5-bisphosphate hydrolysis by hormones
    • q subfamily of guanine nucleotide-binding regulatory protein α subunits attenuate activation of phosphatidylinositol 4,5-bisphosphate hydrolysis by hormones. J. Biol. Chem. 266:20519-24
    • (1991) J. Biol. Chem. , vol.266 , pp. 20519-20524
    • Gutowski, S.1    Smrcka, A.2    Nowak, L.3    Wu, D.4    Simon, M.5    Sternweis, P.C.6
  • 89
    • 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. 269:5730-34
    • (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
  • 93
    • 0027310748 scopus 로고
    • Specific interactions of chemoattractant factor receptors with G-proteins
    • Amatruda TT, Gerard NP, Gerard C, Simon MI. 1993. Specific interactions of chemoattractant factor receptors with G-proteins. J. Biol. Chem. 268:10139-44
    • (1993) J. Biol. Chem. , vol.268 , pp. 10139-10144
    • Amatruda, T.T.1    Gerard, N.P.2    Gerard, C.3    Simon, M.I.4
  • 94
    • 0024854386 scopus 로고
    • i-proteins mediate formyl peptide receptor signal transduction in human leukemia (HL-60) cells
    • i-proteins mediate formyl peptide receptor signal transduction in human leukemia (HL-60) cells. J. Biol. Chem. 264:21470-73
    • (1989) J. Biol. Chem. , vol.264 , pp. 21470-21473
    • Gierschik, P.1    Sidiropoulos, D.2    Jakobs, K.H.3
  • 95
    • 0024849649 scopus 로고
    • Chemotactic peptide receptor-supported ADP-ribosylation of a pertussis toxin substrate GTP-binding protein by cholera toxin in neutrophil-type HL-60 cells
    • Iiri T, Tohkin M, Morishima N, Ohoka Y, Ui M, et al. 1989. Chemotactic peptide receptor-supported ADP-ribosylation of a pertussis toxin substrate GTP-binding protein by cholera toxin in neutrophil-type HL-60 cells. J. Biol. Chem. 264:21394-400
    • (1989) J. Biol. Chem. , vol.264 , pp. 21394-21400
    • Iiri, T.1    Tohkin, M.2    Morishima, N.3    Ohoka, Y.4    Ui, M.5
  • 96
    • 0025165219 scopus 로고
    • Agonist-sensitive binding of a photoreactive GTP analog to a G-protein α subunit in membranes of HL-60 cells
    • Offermans S, Schäfer SO, Hoffman B, Bombien E, Spicher K, et al. 1990. Agonist-sensitive binding of a photoreactive GTP analog to a G-protein α subunit in membranes of HL-60 cells. FEBS Lett. 260:14-18
    • (1990) FEBS Lett. , vol.260 , pp. 14-18
    • Offermans, S.1    Schäfer, S.O.2    Hoffman, B.3    Bombien, E.4    Spicher, K.5
  • 97
    • 0023902774 scopus 로고
    • The formyl peptide chemoattractant receptor copurifies with a GTP-binding protein containing a distinct 40-kDa pertussis toxin substrate
    • Polakis PG, Uhing RJ, Snyderman R. 1988. The formyl peptide chemoattractant receptor copurifies with a GTP-binding protein containing a distinct 40-kDa pertussis toxin substrate. J. Biol. Chem. 263:4969-76
    • (1988) J. Biol. Chem. , vol.263 , pp. 4969-4976
    • Polakis, P.G.1    Uhing, R.J.2    Snyderman, R.3
  • 99
    • 0028126950 scopus 로고
    • Differential coupling of G protein α subunits to seven-helix receptors expressed in Xenopus oocytes
    • Quick MW, Simon MI, Davidson N, Lester HA, Aragay AM. 1994. Differential coupling of G protein α subunits to seven-helix receptors expressed in Xenopus oocytes. J. Biol. Chem. 269: 30164-72
    • (1994) J. Biol. Chem. , vol.269 , pp. 30164-30172
    • Quick, M.W.1    Simon, M.I.2    Davidson, N.3    Lester, H.A.4    Aragay, A.M.5
  • 101
    • 0027953536 scopus 로고
    • Inhibition of human HL-60 cell responses to chemotactic factors by antisense messenger RNA depletion of G proteins
    • Goetzl EJ, Shames RS, Yang J, Birke FW, Liu YF, et al. 1994. Inhibition of human HL-60 cell responses to chemotactic factors by antisense messenger RNA depletion of G proteins. J. Biol. Chem. 269:809-12
    • (1994) J. Biol. Chem. , vol.269 , pp. 809-812
    • Goetzl, E.J.1    Shames, R.S.2    Yang, J.3    Birke, F.W.4    Liu, Y.F.5
  • 102
    • 0027416725 scopus 로고
    • Transfected m2 muscarinic acetylcholine receptors couple to Gαi2 and Gαi3 in Chinese hamster ovary cells. Activation and desensitization of the phospholipase C signaling pathway
    • Dell'Acqua ML, Carroll RC, Peralta EG. 1993. Transfected m2 muscarinic acetylcholine receptors couple to Gαi2 and Gαi3 in Chinese hamster ovary cells. Activation and desensitization of the phospholipase C signaling pathway. J. Biol. Chem. 268:5676-85
    • (1993) J. Biol. Chem. , vol.268 , pp. 5676-5685
    • Dell'Acqua, M.L.1    Carroll, R.C.2    Peralta, E.G.3
  • 104
    • 0026551650 scopus 로고
    • Adrenergic receptors as models for G protein-coupled receptors
    • Kobilka B. 1992. Adrenergic receptors as models for G protein-coupled receptors. Annu. Rev. Neurosci. 15:87-114
    • (1992) Annu. Rev. Neurosci. , vol.15 , pp. 87-114
    • Kobilka, B.1
  • 106
    • 0026548156 scopus 로고
    • In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors
    • Savarese TM, Fraser CM. 1992. In vitro mutagenesis and the search for structure-function relationships among G protein-coupled receptors. Biochem. J. 283:1-19
    • (1992) Biochem. J. , vol.283 , pp. 1-19
    • Savarese, T.M.1    Fraser, C.M.2
  • 107
    • 0027422737 scopus 로고
    • Specificity of receptor-G protein interactions: Searching for the structure behind the signal
    • Hedin KE, Duerson K, Clapham DE. 1993. Specificity of receptor-G protein interactions: searching for the structure behind the signal. Cell. Signal. 5:505-18
    • (1993) Cell. Signal. , vol.5 , pp. 505-518
    • Hedin, K.E.1    Duerson, K.2    Clapham, D.E.3
  • 108
    • 0025212680 scopus 로고
    • 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function
    • 1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function. Proc. Natl. Acad. Sci. USA 87: 2896-900
    • (1990) Proc. Natl. Acad. Sci. USA , vol.87 , pp. 2896-2900
    • Cotecchia, S.1    Exum, S.2    Caron, M.G.3    Lefkowitz, R.J.4
  • 109
    • 0026592357 scopus 로고
    • 1B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation
    • 1B-adrenergic receptor by all amino acid substitutions at a single site. Evidence for a region which constrains receptor activation. J. Biol. Chem. 267:1430-33
    • (1992) J. Biol. Chem. , vol.267 , pp. 1430-1433
    • Kjelsberg, M.A.1    Cotecchia, S.2    Ostrowski, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 111
    • 0027328091 scopus 로고
    • Molecular basis of muscarinic acetylcholine receptor function
    • Wess J. 1993. Molecular basis of muscarinic acetylcholine receptor function. Trends Pharmacol. Sci. 14:308-13
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 308-313
    • Wess, J.1
  • 112
    • 0028158607 scopus 로고
    • Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidylinositol hydrolysis
    • Blüml K, Mutschler E, Wess J. 1994. Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidylinositol hydrolysis. J. Biol. Chem. 269: 402-5
    • (1994) J. Biol. Chem. , vol.269 , pp. 402-405
    • Blüml, K.1    Mutschler, E.2    Wess, J.3
  • 113
    • 0028270938 scopus 로고
    • Inhibition of G protein-coupled receptor signaling by expression of cytoplasmic domains of the receptor
    • Hawes BE, Luttrell LM, Exum ST, Lefkowitz RJ 1994. Inhibition of G protein-coupled receptor signaling by expression of cytoplasmic domains of the receptor. J. Biol. Chem. 269:15776-85
    • (1994) J. Biol. Chem. , vol.269 , pp. 15776-15785
    • Hawes, B.E.1    Luttrell, L.M.2    Exum, S.T.3    Lefkowitz, R.J.4
  • 114
    • 0025817671 scopus 로고
    • 2A-adrenergic receptor alter receptor G protein coupling by distinct mechanisms
    • 2A-adrenergic receptor alter receptor G protein coupling by distinct mechanisms. J. Biol. Chem. 266: 11025-29
    • (1991) J. Biol. Chem. , vol.266 , pp. 11025-11029
    • Dalman, H.M.1    Neubig, R.R.2
  • 115
    • 0028013155 scopus 로고
    • Domains of the human neutrophil N-formyl peptide receptor involved in G protein coupling. Mapping with receptor-derived peptides
    • 113a. Schreiber RE, Prossnitz ER, Ye RD, Cochrane CG, Bokoch GM. 1994. Domains of the human neutrophil N-formyl peptide receptor involved in G protein coupling. Mapping with receptor-derived peptides. J. Biol. Chem. 269:326-31
    • (1994) J. Biol. Chem. , vol.269 , pp. 326-331
    • Schreiber, R.E.1    Prossnitz, E.R.2    Ye, R.D.3    Cochrane, C.G.4    Bokoch, G.M.5
  • 117
    • 0026780341 scopus 로고
    • 2a-adrenergic receptor-GTP-binding protein complexes using GTP-binding protein selective antisera. Changes in receptor/GTP-binding protein interaction following agonist binding
    • 2a-adrenergic receptor-GTP-binding protein complexes using GTP-binding protein selective antisera. Changes in receptor/GTP-binding protein interaction following agonist binding. J. Biol. Chem. 267:14826-31
    • (1992) J. Biol. Chem. , vol.267 , pp. 14826-14831
    • Okuma, Y.1    Reisine, T.2
  • 118
    • 0027132717 scopus 로고
    • The 2.2 Å crystal structure of transducin-α complexed with GTPγS
    • Noel JP, Hamm HE, Sigler PB. 1993. The 2.2 Å crystal structure of transducin-α complexed with GTPγS. Nature 366:654-63
    • (1993) Nature , vol.366 , pp. 654-663
    • Noel, J.P.1    Hamm, H.E.2    Sigler, P.B.3
  • 119
    • 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
  • 122
    • 0023716027 scopus 로고
    • Site of G-protein binding to rhodopsin mapped with synthetic peptides from the α subunit
    • Hamm HE, Deretic D, Arendt A, Hargrave PA, Koenig B, et al. 1988. Site of G-protein binding to rhodopsin mapped with synthetic peptides from the α subunit. Science 241:832-35
    • (1988) Science , vol.241 , pp. 832-835
    • Hamm, H.E.1    Deretic, D.2    Arendt, A.3    Hargrave, P.A.4    Koenig, B.5
  • 125
    • 0027495918 scopus 로고
    • Tryptophan W207 in transducin Ta is the fluorescence sensor of the G protein activation switch and is involved in the effector binding
    • 120c. Faurobert E, Otto-Bruce A, Chardin P, Chabre M. 1993. Tryptophan W207 in transducin Ta is the fluorescence sensor of the G protein activation switch and is involved in the effector binding. EMBO J. 12:4191-98
    • (1993) EMBO J. , vol.12 , pp. 4191-4198
    • Faurobert, E.1    Otto-Bruce, A.2    Chardin, P.3    Chabre, M.4
  • 130
    • 0027214868 scopus 로고
    • Regulation of purified subtypes of phosphatidylinositol-specific phospholipase Cβ by G protein α and βγ subunits
    • Smrcka AV, Sternwess 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    Sternwess, P.C.2
  • 133
    • 0027362142 scopus 로고
    • A G-protein-coupled 130 kDa phospholipase C isozymes, PLC-β4, from the particulate fraction of bovine cerebellum
    • Min DS, Kim Y, Lee YH, Suh P-G, Ryu SH. 1993. A G-protein-coupled 130 kDa phospholipase C isozymes, PLC-β4, from the particulate fraction of bovine cerebellum. FEBS Lett. 331:38-42
    • (1993) FEBS Lett. , vol.331 , pp. 38-42
    • Min, D.S.1    Kim, Y.2    Lee, Y.H.3    Suh, P.-G.4    Ryu, S.H.5
  • 134
    • 0028283331 scopus 로고
    • Activation of phospholipase C β4 by heterotrimeric GTP-binding proteins
    • Jiang H, Wu D, 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.1    Wu, D.2    Simon, M.I.3
  • 136
    • 0027465720 scopus 로고
    • Identification of critical regions on phospholipase C-β1 required for activation by G-proteins
    • Wu D, Jiang H, 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.1    Jiang, H.2    Katz, A.3    Simon, M.I.4
  • 137
    • 0027537482 scopus 로고
    • Removal of the carboxyl-terminal region of phospholipase C-β1 by calpain abolishes activation by Gαq
    • Park D, Jhon D-Y, Lee C-W, Ryu S-H, Rhee SG. 1993. Removal of the carboxyl-terminal region of phospholipase C-β1 by calpain abolishes activation by Gαq. J. Biol. Chem. 268:3710-14
    • (1993) J. Biol. Chem. , vol.268 , pp. 3710-3714
    • Park, D.1    Jhon, D.-Y.2    Lee, C.-W.3    Ryu, S.-H.4    Rhee, S.G.5
  • 138
    • 0027365766 scopus 로고
    • Purification of a 110 kDa phospholipase C from bovine brain cytosol that is activated by G-protein βγ-subunits
    • Blank JL, Shaw K, Ross AH, Exton JH. 1993. Purification of a 110 kDa phospholipase C from bovine brain cytosol 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
  • 139
    • 0026636674 scopus 로고
    • Stimulation of phospholipase C by guanine-nucleotide-binding protein βγ subunits
    • Camps M, Hou C, Sidiropoulos D, Stock JB, Jakobs KH, et al. 1992. Stimulation of phospholipase C by guanine-nucleotide-binding protein βγ subunits. Eur. J. Biochem. 206:821-31
    • (1992) Eur. J. Biochem. , vol.206 , pp. 821-831
    • Camps, M.1    Hou, C.2    Sidiropoulos, D.3    Stock, J.B.4    Jakobs, K.H.5
  • 140
    • 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
  • 141
    • 0026497034 scopus 로고
    • βγ-subunit activation of G-protein-regulated phospholipase C
    • 135a. 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
  • 142
    • 0028964404 scopus 로고
    • Endogenous cleavage of phospholipase C-β3 by agonist-induced activation of calpain in human platelets
    • 135b. Banno Y, Nakashima S, Hachiya T, Nozawa Y 1995. Endogenous cleavage of phospholipase C-β3 by agonist-induced activation of calpain in human platelets. J. Biol. Chem. 270:4318-24
    • (1995) J. Biol. Chem. , vol.270 , pp. 4318-4324
    • Banno, Y.1    Nakashima, S.2    Hachiya, T.3    Nozawa, Y.4
  • 143
    • 0026676806 scopus 로고
    • Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ subunits
    • Camps M, Carozzi A, Schnabel P, Scheer P, Parker PJ, et al. 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, P.4    Parker, P.J.5
  • 144
    • 0026676807 scopus 로고
    • Subunits βγ of heterotrimeric G protein activate β2 isoform of phospholipase C
    • Katz A, Wu D, 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.2    Simon, M.I.3
  • 145
    • 0027418803 scopus 로고
    • Activation of phospholipase C isozymes by G protein βγ subunits
    • Park D, Jhon D-Y, Lee C-W, Lee C-H, Rhee SG. 1993. Activation of phospholipase C isozymes by G protein βγ subunits. J. Biol. Chem. 268:4573-77
    • (1993) J. Biol. Chem. , vol.268 , pp. 4573-4577
    • Park, D.1    Jhon, D.-Y.2    Lee, C.-W.3    Lee, C.-H.4    Rhee, S.G.5
  • 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
  • 148
  • 149
    • 0026655342 scopus 로고
    • Interaction between G-protein β and γ subunit types is selective
    • 140b. 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
  • 150
    • 0026452219 scopus 로고
    • G protein βγ subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of γ
    • 140c. Iñiguez-Lluhi JA, Simon MI, Robishaw JD, Gilman AG. 1992. G protein βγ subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of γ. J. Biol. Chem. 267:23409-17
    • (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
  • 151
    • 0028363744 scopus 로고
    • In vitro processing of recombinant G protein γ subunits. Requirements for assembly of an active βγ complex
    • Higgjns JB, Casey PJ. 1994. In vitro processing of recombinant G protein γ subunits. Requirements for assembly of an active βγ complex. J. Biol. Chem. 269:9067-73
    • (1994) J. Biol. Chem. , vol.269 , pp. 9067-9073
    • Higgjns, J.B.1    Casey, P.J.2
  • 153
    • 0027056925 scopus 로고
    • Selective tissue distribution of G protein y subunits including a new form of the γ subunits identified by cDNA cloning
    • Cali JJ, Balcueva EA, Rybalkin I, Robishaw JD. 1992. Selective tissue distribution of G protein y subunits including a new form of the γ subunits identified by cDNA cloning. J. Biol. Chem. 267:24023-27
    • (1992) J. Biol. Chem. , vol.267 , pp. 24023-24027
    • Cali, J.J.1    Balcueva, E.A.2    Rybalkin, I.3    Robishaw, J.D.4
  • 154
    • 0028068380 scopus 로고
    • A fifth member of the mammalian G-protein β-subunit family. Expression in brain and activation of the β2 isotype of phospholipase C
    • Watson AJ, Katz A, Simon MI. 1994. A fifth member of the mammalian G-protein β-subunit family. Expression in brain and activation of the β2 isotype of phospholipase C. J. Biol. Chem. 269: 22150-56
    • (1994) J. Biol. Chem. , vol.269 , pp. 22150-22156
    • Watson, A.J.1    Katz, A.2    Simon, M.I.3
  • 155
    • 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
  • 156
    • 0025719492 scopus 로고
    • Cloning and expression of a widely distributed (type IV) adeaylyl cyclase
    • Gao B, Gilman AG. 1991. Cloning and expression of a widely distributed (type IV) adeaylyl cyclase. Proc. Natl. Acad. Sci. USA 88:10178-82
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 10178-10182
    • Gao, B.1    Gilman, A.G.2
  • 157
    • 0026418426 scopus 로고
    • Type-specific regulation of adenylyl cyclase by G protein βγ subunits
    • Tang W-J, 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.-J.1    Gilman, A.G.2
  • 158
    • 0027458559 scopus 로고
    • Regulation of purified type I and type II adenylyl cyclases by G protein βγ subunits
    • Taussig R, Quarmby LM, Gilman AG. 1993. Regulation of purified type I and type II adenylyl cyclases by G protein βγ subunits. J. Biol. Chem. 268:9-12
    • (1993) J. Biol. Chem. , vol.268 , pp. 9-12
    • Taussig, R.1    Quarmby, L.M.2    Gilman, A.G.3
  • 159
    • 0027495684 scopus 로고
    • New roles for G-protein βγ-dimers in transmembrane signalling
    • Clapham DE, Neer EJ. 1993. New roles for G-protein βγ-dimers in transmembrane signalling. Nature 365:403-6
    • (1993) Nature , vol.365 , pp. 403-406
    • Clapham, D.E.1    Neer, E.J.2
  • 160
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein β subunits
    • Stephens L, Smrcka A, Cooke FT, Jackson TR, Sternweis PC, et al. 1994. A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein β 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
  • 161
    • 0028178715 scopus 로고
    • A G-protein βγ-subunit-responsive phosphoinositide 3 kinase activity in human platelet cytosol
    • Thomason PA, James SR, Casey PJ, Downes CP. 1994. A G-protein βγ-subunit-responsive phosphoinositide 3 kinase activity in human platelet cytosol. J. Biol. Chem. 269:16525-28
    • (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
  • 162
    • 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
  • 163
    • 0028240869 scopus 로고
    • Ras-dependent activation of MAP kinase pathway mediated by G-protein βγ subunits
    • Crespo P, Xu N, 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.2    Simonds, W.F.3    Gutkind, J.S.4
  • 164
    • 0028085776 scopus 로고
    • Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates Gβγ-mediated signaling
    • Koch WJ, Hawes BE, Inglese J, Luttrell LM, Lefkowitz RJ. 1994. Cellular expression of the carboxyl terminus of a G protein-coupled receptor kinase attenuates Gβγ-mediated signaling. J. Biol. Chem. 269:6193-97
    • (1994) J. Biol. Chem. , vol.269 , pp. 6193-6197
    • Koch, W.J.1    Hawes, B.E.2    Inglese, J.3    Luttrell, L.M.4    Lefkowitz, R.J.5
  • 166
    • 0026700191 scopus 로고
    • Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate
    • Zachary I, Sinnett-Smith J, Rozengurt E. 1992. Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. Identification of a novel tyrosine kinase as a major substrate. J. Biol. Chem. 267: 19031-34
    • (1992) J. Biol. Chem. , vol.267 , pp. 19031-19034
    • Zachary, I.1    Sinnett-Smith, J.2    Rozengurt, E.3
  • 168
    • 0027370725 scopus 로고
    • Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phosphorylation of the focal adhesion-associated protein paxillin in Swiss 3T3 cells
    • Zachary I, Sinnett-Smith J, Turner CE, Rozengurt E. 1993. Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phosphorylation of the focal adhesion-associated protein paxillin in Swiss 3T3 cells J. Biol. Chem. 268: 22060-65
    • (1993) J. Biol. Chem. , vol.268 , pp. 22060-22065
    • Zachary, I.1    Sinnett-Smith, J.2    Turner, C.E.3    Rozengurt, E.4
  • 169
    • 0027931186 scopus 로고
    • Regulation of endothelin-1- and lysophosphatidic acid-stimulated tyrosine phosphorylation of focal adhesion kinase (pp125fak) in Rat-I fibroblasts
    • Seville MK, Graham A, Malarkey K, Paterson A, Gould GW, et al. 1994. Regulation of endothelin-1- and lysophosphatidic acid-stimulated tyrosine phosphorylation of focal adhesion kinase (pp125fak) in Rat-I fibroblasts. Biochem. J. 301:407-14
    • (1994) Biochem. J. , vol.301 , pp. 407-414
    • Seville, M.K.1    Graham, A.2    Malarkey, K.3    Paterson, A.4    Gould, G.W.5
  • 170
    • 0028246461 scopus 로고
    • Angiotensin II stimulates tyrosine phosphorylation of phospholipase C-γ1 in vascular smooth muscle cells
    • Marrero MB, Paxton WG, Duff JL, Berk BC, Bernstein KE. 1994 Angiotensin II stimulates tyrosine phosphorylation of phospholipase C-γ1 in vascular smooth muscle cells J Biol. Chem. 269:10935-39
    • (1994) J Biol. Chem. , vol.269 , pp. 10935-10939
    • Marrero, M.B.1    Paxton, W.G.2    Duff, J.L.3    Berk, B.C.4    Bernstein, K.E.5
  • 172
    • 0027240231 scopus 로고
    • i-coupled acetylcholine muscarinic m2 receptor activation of mitogen-activated protein (MAP) kinase kinase and MAP kinase
    • i-coupled acetylcholine muscarinic m2 receptor activation of mitogen-activated protein (MAP) kinase kinase and MAP kinase. J. Biol. Chem. 268:19196-99
    • (1993) J. Biol. Chem. , vol.268 , pp. 19196-19199
    • Winitz, S.1    Russell, M.2    Qian, N.-X.3    Gardner, A.4    Dwyer, L.5
  • 175
    • 0027263039 scopus 로고
    • Direct evidence for tyrosine and threonine phosphorylation and activation of mitogen-activated protein kinase by vasopressin in cultured rat vascular smooth muscle cells
    • Granot Y, Erikson E, Fridman H, Putten VV, Williams B, et al. 1993. Direct evidence for tyrosine and threonine phosphorylation and activation of mitogen-activated protein kinase by vasopressin in cultured rat vascular smooth muscle cells. J. Biol. Chem. 268:9564-69
    • (1993) J. Biol. Chem. , vol.268 , pp. 9564-9569
    • Granot, Y.1    Erikson, E.2    Fridman, H.3    Putten, V.V.4    Williams, B.5
  • 177
    • 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
  • 178
    • 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, Wittig B. 1991. Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents. Nature 353:43-48
    • (1991) Nature , vol.353 , pp. 43-48
    • Kleuss, C.1    Hescheler, J.2    Ewel, C.3    Rosenthal, W.4    Schultz, G.5    Wittig, B.6
  • 179
    • 0027530916 scopus 로고
    • Selectivity of signal transduction determined by 7 subunits of heterotrimeric G proteins
    • Kleuss C, Scherubl H, Hescheler J, Schultz G, Wittig B. 1993. Selectivity of signal transduction determined by 7 subunits of heterotrimeric G proteins. Science 259:832-34
    • (1993) Science , vol.259 , pp. 832-834
    • Kleuss, C.1    Scherubl, H.2    Hescheler, J.3    Schultz, G.4    Wittig, B.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.