Minireview: Signal Transduction by G Proteins: 1994 Edition

References

• Bimbaumer L. Transduction of receptor signal into modulation of effector activity by G proteins: the first 20 years or so.…. Faseb J. 1990; 4: 3178–3188
   Google Scholar
• Iyengar R., Bimbaumer L. Hormone receptor modulate the regulatory component of adenylyl cyclases by reducing its requirement for Mg2+ ion and enhancing its extent of activation by guanine nucleotides. Proc. Natl. Acad. Sci. USA 1982; 79: 5179–5183
   PubMed Web of Science ®Google Scholar
• Higashijima T., Ferguson K. M., Stemweis P. C., Smigel M. D., Gilman A. G. Effects of Mg2+ and the beta-gamma subunit complex on the interactions of guanine nucleotides with G proteins. J. Biol. Chem. 1987a; 262: 762–766
   PubMed Web of Science ®Google Scholar
• Casey P. J., Gilman A. G. G protein involvement in receptor-effector coupling. J. Biol. Chem. 1988; 263: 2577–2580
   PubMed Web of Science ®Google Scholar
• Graziano M. P., Freissmuth M., Gilman A. G. Expression of Gsα in Escherichia coli. Purification and properties of two forms of the protein. J. Biol. Chem. 1989; 264: 409–418
   Google Scholar
• Lee E., Taussig R., Gilman A. G. The G226AA mutant of Gsα highlights the requirement for dissociation of G protein subunits. J. Biol. Chem. 1992; 267: 1212–1218
   PubMed Web of Science ®Google Scholar
• Rodbell M., Krans H. M.J., Pohl S. L., Bimbaumer L. The glucagon-sensitive adenyl cyclase system in plasma membranes of rat liver. Iv. Binding of glucagon: effect of guanyl nucleotides. J. Biol. Chem. 1971; 246: 1872–1876
   Google Scholar
• Maguire M. E., Van Arsdale P. M., Gilman A. G. An agonist-specific effect of guanine nucleotides on binding to the beta adrenergic receptor. Mol. Pharmacol. 1976; 12: 335–339
   PubMed Web of Science ®Google Scholar
• Lefkowitz R. J., Mullikan D., Caron M. G. Regulation of β-adrenergic receptors by guanyl-5′-yl imidodiphosphate and other purine nucleotides. J. Biol. Chem. 1976; 251: 4686–4692
   PubMed Web of Science ®Google Scholar
• Berrie C. P., Birdsall N. J.M., Burgen A. S.V., Hulme E. C. Guanine nucleotides modulate muscarinic receptor binding in the heart. Biochem. Biophys. Res. Comm. 1979; 87: 1000–1005
   PubMed Web of Science ®Google Scholar
• Rosenberger L. B., Roeske W. R., Yamamura H. I. The regulation of muscarinic cholinergic receptors by guanine nucleotides in cardiac tissue. Europ. J. Pharmacol. 1979; 56: 179–180
   Google Scholar
• Wieland T., Hunzan M., Jakobs K. H. Stimulation and inhibition of human platelet adenylcyclase by thiophosphorylated transducin βγ-subunits. J. Biol. Chem. 1992; 267: 20791–20797
   Google Scholar
• Wieland T., Numbarg B., Ulibarr I., Kaldenberg-Stasch S., Schultz G., Jakobs K. H. Guanine nucleotide-specific phosphate transfer by guanine nucleotide-binding regulatory protein β subunits. Characterization of the phosphorylated amino acid. J. Biol. Chem. 1993; 268: 18111–18118
   Google Scholar
• Mumby S. M., Heukeroth R. O., Gordon J. E., Gilman A. G. G-protein α-subunit expression. myristoylation, and membrane association in COS cells. Proc. Natl. Acad. Sci. USA 1990; 87: 728–723
   Google Scholar
• Jones R. L.Z., Simonds W. F., Merendino J. J., Jr., Brann M. R., Spiegel A. M. Myristoylation of an inhibitory GTP-binding protein α subunit is essential for its membrane attachment. Proc. Natl. Acad. Sci. USA 1990; 87: 568–572
   Google Scholar
• Taussig R., Iñiguez-Lluhi J. A., Gilman A. G. Inhibition of adenylyl cyclase by Giα. Science 1993; 261: 218–221
   PubMedGoogle Scholar
• Linder M. E., Pang I. H., Duronio R. J., Gordon J. I., Stemweis P. C., Gilman A. G. Lipid modification of G protein subunits. Myristoylation of Goα increases its affinity for βγ. J. Biol. Chem. 1991; 266: 4654–4649
   PubMed Web of Science ®Google Scholar
• Linder M. E., Middleton P., Hepler J. R., Taussig R., Gilman A. G., Mumby S. M. Lipid modifications of G proteins: α subunits are palmitoylated. Proc. Natl. Acad. Sci. USA 1993; 90: 3675–3679
   PubMed Web of Science ®Google Scholar
• Parenti M., Vigano M. A., Newman C. M.H., Milligan G., Magee A. I. A novel n-terminal motif for palmitoylation of G-protein α subunits. Biochem. J. 1993; 291: 349–353
   PubMedGoogle Scholar
• Wedegaertner P. B., Chu D. H., Wilson P. T., Levis M. J., Boume H. R. Palmitoylation is required for signaling function and membrane attachment of Gqα and Gsα J. Biol. Chem. 1993; 268: 25001–25008
   Google Scholar
• Degtyarev M. Y., Speigel A. M., Jones T. L.Z. Increased palmitoylation of the Gs protein α subunit after activation by the β-adrenergic receptor or cholera toxin. J. Biol. Chem. 1993; 268: 23769–23772
   PubMedGoogle Scholar
• Mumby S. M., Casey P. J., Gilman A. G., Gutowski S., Stemweis P. C. G protein γ subunits contain a 20-carbon isoprenoid. Proc. Natl. Acad. Sci. USA 1990; 87: 5873–5877
   PubMedGoogle Scholar
• Simonds W. F., Butrynski J. E., Gautam N., Unsion C. G., Spiegel A. M. G-protein βγ dimers. Membrane targeting requires subunit co-expression and intact γ CAAX domain. J. Biol. Chem. 1991; 266: 5363–5366
   Google Scholar
• Sanford J., Codina J., Birnbaumer L. γ-subunits of G proteins, but not their α- or β-subunits, are polyisoprenylated. Studies on post-translational modifications using in vitro translation with rabbit reticulocyte lysates. J. Biol. Chem. 1991; 266: 9570–9579
   PubMedGoogle Scholar
• Iñiguez-Lluhi J. A., Simon M. I., Robishaw J. D., Gilman A. G. G protein βγ subunits synthesized in Sf9 cells. Functional characterization and the significance of prenylation of γ J. Biol. Chem. 1992; 267: 23409–23417
   Google Scholar
• Conklin B. R., Boume H. R. Structural elements of Gα subunits that interact with Gβγ. receptors, and effectors. Cell 1993; 73: 631–641
   Google Scholar
• Noel J. P, Hamm H. E., Sigler P. B. The 2.2 Å crystal structure of transducin α-GTPγS. Nature 1993; 366: 654–663
   PubMed Web of Science ®Google Scholar
• Ui M. Islet-activating protein. pertussis toxin: a probe for functions of the inhibitory guanine nucleotide regulatory component of adenylate cyclase. Trends Pharmacol. Sci. 1984; 5: 277–279
   Google Scholar
• Conklin B. R., Farfel Z., Lustig K. D., Julius D., Bourne H. R. Substitution of three amino acids switches receptor specificity. Nature 1993; 363: 274–276
   PubMed Web of Science ®Google Scholar
• Dratz E. A., Furstenau J. E., Lanbert C. G., Thireault D. L., Rarick H., Schepers T., Pakhlevaniants S., Hamm H. E. NMR structure of a receptor-bound G protein peptide. Nature 1993; 363: 276–281
   PubMedGoogle Scholar
• Navon S. E., Fung B. K.-K. Characterization of transducin from bovine retinal rod outer segments. Participation of the amino-terminal region of Tα in subunit interaction. J. Biol. Chem. 1987; 262: 15746–15751
   Google Scholar
• Graf R., Mattera R., Codina J., Estes M. K., Bimbaumer L. A truncated recombinant a subunit of Gi3 with a reduced affinity for βγ dimers and altered GTPγS binding. J. Biol. Chem. 1992; 267: 24307–24314
   Google Scholar
• Slepak V. Z., Wilkie T. M., Simon M. I. Mutational analysis of G protein a subunit Goα expressed in Escherichia coli. J. Biol. Chem. 1993; 268: 1414–1423
   Google Scholar
• Iñiguez-Lluhi J. A., Simon M. I., Robishaw J. D., Gilman A. G. G Protein βγ Subunits Synthesized in SF9 Cells. Functional Characterization and the Significance of Prenylation of γ. J. Biol. Chem. 1992; 267: 23409–23417
   PubMed Web of Science ®Google Scholar
• Berlot C. H., Bourne H. R. Identification of effector-activating residues of Gsα. Cell 1992; 68: 911–922
   PubMed Web of Science ®Google Scholar
• Rarick H. M., Artemyev N. O., Hamm H. E. A site on rod G protein α subunit that mediates effector activation. Science 1992; 256: 1031–1033
   Google Scholar
• Lyons J., Landis C. A., Harsh G., Vallar L., Grünwald K., Feichtinger H., Dull Q.-Y., Clark O. H., Kawasaki E., Boume H. R., McCormick F. Two G protein oncogenes in human endocrine tumors. Science 1990; 249: 655–659
   PubMed Web of Science ®Google Scholar
• Cassel D., Selinger Z. Mechanism of adenylate cyclase activation by cholera toxin: inhibition of GTP hydrolysis at the regulatory site. Proc. Natl. Acad. Sci. USA 1977; 74: 3307–3311
   PubMed Web of Science ®Google Scholar
• Abood M. E., Hurley J. B., Pappone M.-C., Boume H. R., Stryer L. Functional homology between signal-coupling proteins. Cholera toxin inactivates the GTPase activity of transducin. J. Biol. Chem. 1982; 257: 10540–10543
   Google Scholar
• Van Dop C., Tsubokawa M., Boume H. R., Ramachandran J. Amino acid sequence of retinal transducin at the site ADP-ribosylated by cholera toxin. J. Biol. Chem. 1984; 259: 696–699
   PubMedGoogle Scholar
• Graziano M. P., Gilman A. G. Synthesis in Escherichia coil of GTPasedeficient mutants of Gsα. J. Biol. Chem. 1990; 264: 15475–15482
   Google Scholar
• Gupta S. K., Gallego C., Johnson G., Heasley L. E. MAP kinase is constitutively activated in gip2 and src transformed Rat-1a fibroblasts. J. Biol. Chem. 1992; 267: 7987–7990
   PubMedGoogle Scholar
• Gupta S. K., Gallego C., Johnson G. L. Mitogenic pathways regulated by G protein oncogenes. Mol. Biol. Cell 1992; 3: 123–128
   PubMedGoogle Scholar
• De Vivo M., Chen J., Codina J., Iyengar R. Enhanced phospholipase C stimulation and transformation in NIH-3T3 cells expressing Q209L Gq-α subunits. J. Biol. Chem. 1992; 267: 18263–18266
   PubMedGoogle Scholar
• Kroll S. D., Chen J., De Vivo M., Carthy D. J., Buku A., Premont R. T., Iyengar R. The Q205L Go-α subunit expressed in NIH-3T3 cells induces transformation. J. Biol. Chem. 1992; 267: 23182–23188
   Google Scholar
• Jiang H., Wu D., Simon M. I. The transforming activity of ativated Gα12. FEBS Lett. 1993; 330: 319–322
   PubMed Web of Science ®Google Scholar
• Chen J. C., Iyengar R. Suppression ofras-induced transformation of NIH-3T3 cells by activated αs. Science 1994, In press
   Google Scholar
• Rudolph U., Finegold M. J., Rich S. S., Harriman G. R., Srinivasan Y., Brabet P., Bradley A., Bimbaumer L. G_i2-deficient mice develop inflammatory bowel disease and adenocarcinomas of the colon. 1994, Submitted
   Google Scholar
• Nakamoto J. M., Jones E. A., Zimmerman D., Scott M. L., Donlan M. A., Van Dop C. A missense mutation in the GS alpha gene is associated with pseudohypoparathyroidism Type I-A and gonadotropin-Independent precocious puberty. Clin. Res. 1993; 41: 44A, (Abs.)
   Google Scholar
• Shenker A., Laue L., Kosugi S., Merendino J. J., Minegishi T., Cutler G. B., Jr. A constitutively activating mutation of the luteinizing hormone receptor in familial male precocious puberty. Nature 1993; 365: 652–654
   PubMed Web of Science ®Google Scholar
• Wess J., Bonner T. I., Derje F., Brann M. R. Delineation of muscarinic receptor domains conferring selectivity of coupling to guanine nucleotide-binding proteins and second messengers. Mol. Pharmacol. 1990; 38: 517–523
   Google Scholar
• Blüml K., Mutschler E., Wess J. Identification of an intracellular tyrosine residue critical for muscarinic receptor-mediated stimulation of phosphatidylinositol hydrolysis. J. Biol. Chem. 1994; 269: 402–405
   Google Scholar
• Cotecchia S., Exum S., Caron M. G., Lefkowitz R. J. Regions of the α1-adrenergic receptor involved in coupling to phosphatidylinositol hydrolysis and enhanced sensitivity of biological function Proc. Natl. Acad. Sci. USA 1990; 87: 2896–2900
   PubMed Web of Science ®Google Scholar
• Kjelsberg M. A., Cotecchia S., Ostrowski J., Caron M. G., Lefkowitz R. J. Constitutive activation of the α1B-adrenergic receptor by all amino acid substitutions at a single site. J. Biol. Chem. 1992; 267: 1430–1433
   PubMed Web of Science ®Google Scholar
• Samama P., Cotecchia S., Costa T., Lefkowitz R. J. A mutation induced activated state of the β2-adrenergic receptor. Extending the ternary complex model. J. Biol. Chem. 1993; 268: 4625–4636
   Google Scholar
• Ren Q., Kurose H., Lefkowitz R. J., Cotecchia S. Constitutively active mutants of the α2-adrenergic receptor. J. Biol. Chem. 1993; 268: 16483–16487
   PubMed Web of Science ®Google Scholar
• Nishimoto I., Murayama Y., Katada T., Ui M., Ogata E. Possible direct linkage of insulin-like growth factor-II receptor with guanine nucleotide-binding proteins. J. Biol. Chem. 1989; 264: 14029–14038
   PubMed Web of Science ®Google Scholar
• Okamoto T., Katada T., Murayama Y., Ui M., Ogata E., Nishimoto I. A simple structure encodes G protein-activating function of the IGF-II/mannose 6-phosphate receptor. Cell 1990; 62: 709–717
   PubMed Web of Science ®Google Scholar
• Okamoto T., Murayama Y., Hayashi Y., Inagaki M., Ogata E., Nishimoto I. Identification of a Gs activator region of the β2-adrenergic receptor that is autoregulated via protein kinase A-dependent phosphorylation. Cell 1991; 67: 723–730
   Google Scholar
• Okamoto T., Nishimoto I. Detcctionm of G protein activator regions in the M4 subtype muscarinic cholinergic and α2-adrenergic receptors based upon characteristics of primary structure. J. Biol. Chem. 1992; 267: 8342–8346
   PubMed Web of Science ®Google Scholar
• Ikezu T., Okamoto T., Ogata E., Nishimoto I. Amino acids 356-372 constitute a Gi-activator sequence of the α2-adrenergic receptor and have a Phe substitute in the G protein-activator sequence motif. FEBS Lett. 1992; 311: 29–32
   PubMed Web of Science ®Google Scholar
• Nishimoto I. The IGF-II receptor system: a G protein-linked mechanism. Molecular Reproduction and Development 1993; 35: 398–407
   Google Scholar
• Kataoka R., Sherlock J., Lanier S. M. Signaling events initiated by transforming growth factor-β1 that require Giα1. J. Biol. Chem. 1993; 263: 19851–19857
   Google Scholar
• Nishimoto I., Okamoto T., Matsuura Y., Takahashi S., Okamoto T., Uriyama Y., Ogata E. Alzheimer amyloid protein precursor complexes with brain GTP-binding protein Go. Nature 1993; 362: 75–79, (b)
   PubMed Web of Science ®Google Scholar
• Ross E. M., Wong S. K.F., Rubenstein R. C., Higashijima T. Functional domains in the β-adrenergic receptor. Cold Spring Harbor Symp. Quant. Biol. 1988; 53: 99–506
   Google Scholar
• Antonelli M., Olate J., Graf R., Allende C. C., Allende J. E. Differential stimulation of the GTPase activity of G-proteins by polylysine. Biochem. Pharmacol. 1992; 44: 547–551
   Google Scholar
• Bimbaumer L. Receptor-to-effector signaling through G proteins: roles for βγ dimers as well as for α subunits. Cell 1992; 71: 1069–1072
   Google Scholar
• Harwood J. P., Löw H., Rodbell M. Stimulatory and inhibitory effects of guanyl nucleotides on fat cell adenylate cyclase. J. Biol. Chem. 1973; 248: 6239–6245
   PubMedGoogle Scholar
• Bimbaumer L. Hormone-sensitive adenylyl cyclases: useful models for studying hormone receptor functions in cell-free systems. Biochim. Biophys. Acta (Reviews on Biomembranes) 1973; 300: 129–158
   Google Scholar
• Bokoch G. M., Katada T., Northup J. K., Hewlett E. L., Gilman A. G. Identification of the predominant substrate for ADP-ribosylation by islet activating protein. J. Biol. Chem. 1983; 258: 2071–2075
   Google Scholar
• Codina J., Hildebrandt J. D., Iyengar R., Bimbaumer L., Sekura R. D., Manclark C. R. Pertussis toxin substrate, the putative Ni of adenylyl cyclases, is an alpha/beta heterodimer regulated by guanine nucleotide and magnesium. Proc. Natl. Acad. Sci. USA 1983; 80: 4276–4280
   PubMed Web of Science ®Google Scholar
• Hildebrandt J. D., Hanoune J., Bimbaumer L. Guanine nucleotide inhibition of cyc- s49 mouse lymphoma cell membrane adenylyl cyclase. J. Biol. Chem. 1982; 257: 14723–14725
   PubMedGoogle Scholar
• Hildebrandt J. D., Codina J., Bimbaumer L. Interaction of the stimulatory and inhibitory regulatory proteins of the adenylyl cyclase system with the catalytic component of cyc- s49 cell membranes. J. Biol. Chem. 1984; 259: 13178–13185
   PubMed Web of Science ®Google Scholar
• Toro M.-J., Montoya E., Bimbaumer L. Inhibitory regulation of adenylyl cyclases. Evidence against a role for βγ complexes of G proteins as mediators of G; dependent hormonal effects. Mol. Endocrinol. 1987; 1: 669–676
   Google Scholar
• Jacobowitz O., Chen J., Premont R. T., Iyengar R. Stimulation of specific types of Gs-stimulated adenylyl cyclases by phorbol esther treatment. J. Biol. Chem. 1993; 268: 3829–3832
   PubMedGoogle Scholar
• Chen J. C., Iyengar R. Inhibition of cloned adenylyl cyclases by mutant-activated Gi-α and specific suppression of type 2 adenylyl cyclase inhibition by phorbol ester wutreatment. J. Biol. Chem. 1993; 268: 12253–12256
   PubMedGoogle Scholar
• Waldo G. L., Boyer J. L., Morris A. J., Harden T. K. Purification of an AIF-4 and G-protein βγ-subunit-regulated phospholipase C-activating protein. J. Biol. Chem. 1991; 266: 14217–14255
   PubMedGoogle Scholar
• Cooper C. L., Morris A. J., Harden T. K. Guanine nucleotide-sensitive interaction of a radiolabeled agonist with a phospholipase C-linked P2y-purinergic receptor. J. Biol. Chem. 1989; 264: 6202–6206
   PubMed Web of Science ®Google Scholar
• Park D., Jhon D. Y., Kritz R., Knopf J., Rhee S. G. Cloning, expression and Gq-independent activation of phospholipase C-β2. J. Biol. Chem. 1992; 267: 16048–16055
   PubMed Web of Science ®Google Scholar
• Lee C. H., Park D., Wu D., Rhee S. G., Simon M. I. Members of the Gq alpha subunit gene family activate phospholipase C-beta isozymes. J. Biol. Chem. 1992; 267: 16044–16047
   Google Scholar
• Camps M., Hou C., Sidiropoulos D., Stock J. B., Jakobs K. H., Gierschik P. Stimulation of phospholipase C by guanine-nucleotide-binding protein βγ subunits. Eur. J. Biochem. 1992a; 206: 821–831
   PubMedGoogle Scholar
• Camps M., Carozzi A., Schnabel P., Scheer A., Parker P. J., Gierschik P. Isozyme-selective stimulation of phospholipase C-β2 by G protein βγ-subunits. Nature 1992b; 360: 684–686
   PubMed Web of Science ®Google Scholar
• Katz A., Wu D., Simon M. I. βγ subunits of the heterotrimeric G protein activate the β2 isoform of phospholipase C. Nature 1992; 360: 686–689
   PubMed Web of Science ®Google Scholar
• Wu D., Lee C. H., Rhee S. G., Simon M. I. Activation of phospholipase C by the α subunit of the Gq and G11 protein in transfected COS-7 cells. J. Biol. Chem. 1992; 267: 1811–1817
   PubMedGoogle Scholar
• Wu D., Katz A., Simon M. I. Activation of phospholipase C β2 by the a and βγ subunits of trimeric GTP-binding protein. Proc. Natl. Acad. Sci. USA 1993a; 90: 5297–5301
   PubMed Web of Science ®Google Scholar
• Wu D., Jiang H., Katz A., Simon M. I. Identification of critical regions on phospholipase C-β1 required for activation by G-proteins. J. Biol. Chem. 1993b; 268: 3704–379
   PubMed Web of Science ®Google Scholar
• Blank J. L., Brattain K. A., Exton J. H. Activation of cytosolic phosphoinositide phospholipase C by G-protein βγ subunits. J. Biol. Chem. 1992; 267: 23069–23075
   PubMedGoogle Scholar
• Hepler J. R., Kozasa T., Smrcka A. V., Simon M. I., Rhee S. G., Sternweis P. C., Gilman A. G. Purification from Sf9 cells and characterization of recombinant Gaα and Gqα. Activation of purified phospholipase C isozymes by Gα subunits. J. Giol. Chem. 1993; 268: 14367–14375
   Google Scholar
• Carozzi A., Camps M., Gierschik P., Parker P. J. Activation of phosphatidylinositol lipid-specific phospholipase C-β3 by G-protein βγ subunits. FEBS Lett. 1993; 315: 340–342
   PubMed Web of Science ®Google Scholar
• Schnabel P., Schreck R., Schiller D. L., Camps M., Gierschik P. Stimulation of phospholipase C by a mutationally activated G protein α16 subunit. Biochem. Biophys. Res. Commun. 1993; 188: 1018–1023
   Google Scholar
• Park D., Jhon D. Y., Lee C. W., Ryu S., Rhee S. G. Removal of the carboxyterminal region of phospholipase C-β1 by calpain abolishes activation by Gqα. J. Biol. Chem. 1993; 268: 3710–374
   PubMed Web of Science ®Google Scholar
• Berstein G., Blank J. L., Smrcka A. V., Higashijima T., Sternweis P. C., Exton J. H., Ross E. M. Reconstitution of agonist-stimulated phosphatidylinositol 4,5-tris- phosphate hydrolysis using purified M1 muscarinic receptor, Gq/11 and phospholipase C-β1. J. Biol. Chem. 1992; 267: 8081–8088
   PubMed Web of Science ®Google Scholar
• Berstein G., Blank J. L., Jhon D. Y., Exton J. H., Rhee S. G., Ross E. M. Phospholipase C-β1 is a GTPase-activating protein for Gg/11. its physiologic regulator. Cell 1992; 70: 411–418
   Google Scholar
• Bimbaumer L., Bearer C. F., Iyengar R. A two-state model of an enzyme with an allosteric regulatory site capable of metabolizing the regulatory ligand: Simplified mathematical treatments of transient and steady state kinetics of an activator and its competitive inhibition as applied to adenylyl cyclases. J. Biol. Chem. 1980; 255: 3552–3557
   Google Scholar
• Iyengar R., Abramowitz J., Bordelon-Riser M. E., Bimbaumer L. Hormone receptor-mediated stimulation of adenylyl cyclase systems. Nucleotide effects and analysis in terms of a two-state model for the basic receptor-affected enzyme. J. Biol. Chem. 1980; 255: 3558–3564
   Google Scholar
• Kleuss C., Hescheler J., Ewel C., Rosenthal W., Schultz G., Wittig B. Assignment of G-protein subtypes to specific receptors inducing inhibition of calcium currents. Nature 1991; 353: 43–48
   PubMed Web of Science ®Google Scholar
• Kleuss C., Scherübl H., Hescheler J., Schultz G., Wittig B. Different β-subunits determine G protein interaction with transmembrane receptors. Nature 1992; 358: 424–426
   PubMed Web of Science ®Google Scholar
• Kleuss C., Scherübl H., Hescheler J., Schultz G., Wittig B. Selectivity in signal transduction determined by γ subunits of heterotrimeric G proteins. Science 1993; 259: 832–834
   PubMed Web of Science ®Google Scholar
• Yatani A., Codina J., Sekura R. D., Bimbaumer L., Brown A. M. Reconstitution of somatostatin and muscarinic receptor mediated stimulation of K+ channels by isolated Gk protein in clonal rat anterior pituitary cell membranes. Mol. Endocrinol. 1987; 1: 283–289
   PubMedGoogle Scholar
• Amatruda T. T., III, Gerard N. P., Gerard C., Simon M. I. Specific interactions of chemoattractant factor receptors with G-proteins. J. Biol. Chem. 1993; 268: 10139–10144
   PubMedGoogle Scholar
• Wu D., LaRosa G. J., Simon M. I. G protein-coupled signal transduction pathways for interleukin-8. Science 1993c; 261: 101–103
   PubMed Web of Science ®Google Scholar
• Ashkenazi A., Winslow J. W., Peralta E. G., Peterson G. L., Schimerlik M. I., Capon D. J., Ramachandran J. An M2 muscarinic receptor subtype coupled to both adenylyl cyclase and phosphoinositide turnover. Science 1987; 238: 672–675
   PubMed Web of Science ®Google Scholar
• Fargin A., Reymond J. R., Regan J. W., Cotecchia S., Lefkowitz R. J., Caron M. G. Effector coupling mechanisms of the cloned 5-HT1A receptor. J. Biol. Chem. 1989; 264: 14949–14852
   Google Scholar
• Raymond J. R., Albers F. J., Middleton J. P., Lefkowitz R. J., Caron M. G., Obeid L. M., Dennis V. W. 5-HT1A and histamine H1 receptors in HeLa cells stimulate phosphoinositide hydrolysis and phosphate uptake via distinct G protein pools. J. Biol. Chem. 1991; 266: 372–379
   Google Scholar
• Vallar L., Muca C., Magni M., Albert P., Bunzow J., Meldolesi J., Civelli O. Differential coupling of dopaminergic D2 receptors expressed in different cell types. Stimulation of phosphatidylinositol 4,5-bisphosphate hydrolysis in Ltkfibroblasts, hyperpolarization, and cytosolic free Ca2+ concentration decrease in GH4C1 Cells. J. Biol. Chem. 1990; 265: 10320–10326
   PubMed Web of Science ®Google Scholar
• VanSande J., Raspe E., Perret J., Lejeune C., Manhaut C., Vassart G., Dumont J. E. Thyrotropin activates both the cAMP and the PIP2 cascade in CHO cells expressing the human cDNA of the TSH receptor. Mol. Cell. Endo. 1990; 74: R1–R6
   Google Scholar
• Gudermann T., Bimbaumer M., Bimbaumer L. Evidence for dual coupling of the murine LH receptor to adenylyl cyclase and phosphoinositide breakdown/Ca2+ mobilization. studies with the cloned murine LH receptor expressed in L cells. J. Biol. Chem. 1992; 267: 4479–4488
   Google Scholar
• Chabre O., Conklin B. R., Lin H. Y., Lodish H. F., Wilson E., Ives H. E., Catanzariti L., Hemmings B. A., Bourne H. R. A recombinant calcitonin receptor independently stimulates 3′,5′-cyclic adenosine monophosphate and Ca2+/inositol phosphate signaling pathways. Mol. Endocrinol. 1992; 6: 551–556
   PubMedGoogle Scholar
• Abou-Sambra A. B., Jüpmer H., Force T., Freeman M. W., Kong X. F., Schipani E., Urena P., Richards J., Bonventre J. V., Potts J. T., Jr., Kronenberg H. M., Segre G. V. Expression cloning of a common receptor for parathryoid hormone and parathyroid hormone-related peptide from rat osteoblast-like cells: A single receptor stimulates intracellular accumulation of both cAMP and inositol trisphosphates and increases intracellular free calcium. Proc. Natl. Acad. Sci. USA 1992; 89: 2732–2736
   Google Scholar
• Northup J. K., Smigel M. D., Sternweis P. C., Gilman A. G. The Subunits of the stimulatory regulatory component of adenylate cyclase. Resolution of the activated 45,000-dalton (alpha) subunit. J. Biol. Chem. 1983; 258: 11369–11376
   Google Scholar
• Codina J., Hildebrandt J. D., Sekura R. D., Bimbaumer M., Bryan J., Manclark C. R., Iyengar R., Bimbaumer L. Ns and Ni. the stimulatory and inhibitory regulatory components of adenylyl cyclases. Purification of the human erythrocyte proteins without the use of activating regulatory ligands. J. Biol. Chem. 1984; 259: 5871–5886
   Google Scholar
• Eason M. G., Kurose H., Holt B. D., Raymond J. R., Liggett S. B. Simultaneous coupling of α2-adrenergic receptors to two G-proteins with opposing effects. Subtype selective coupling of α2C10, α2C4 and a2α2C2 adrenergic receptors to Gi and Gs J. Biol. Chem. 1992; 267: 15795–15801
   Google Scholar
• Kisselev O., Gautam N. Specific interactions with rhodopsin is dependent on the γ subunit type in a G protien. J. Biol. Chem. 1993; 268: 24519–24522
   PubMed Web of Science ®Google Scholar
• Luttrell L. M., Ostrowski J., Cotecchia S., Kendall H., Lefkowitz R. J. Antagonism of catecholamine receptor signaling by expression of cytoplasmic domains of the receptor. Science 1993; 259: 1453–1457
   Google Scholar
• Bimbaumer L., Abramowitz J., Brown A. M. Signal transduction by G proteins. Biochim. Biophys. Acta. (Reviews in Biomembranes) 1990; 1031: 163–224
   Google Scholar
• Artemyev N. O., Mills J. S., Thomburg K. R., Knapp D. R., Schey K. L., Hamm H. A site on transducin α-subunit of interaction with the polycationic region of cGMP phosphodiesterase inhibitory subunit. J. Biol. Chem. 1993; 268: 23611–23615
   Google Scholar