Functional significance of oligomerization of G-protein-coupled receptors

Trends in Endocrinology and Metabolism

Volumn 11, Issue 5, 2000, Pages 163-168

  Salahpour, Ali ^a   Angers, Stéphane ^a   Bouvier, Michel ^a  

^a UNIVERSITÉ DE MONTRÉAL   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

4 AMINOBUTYRIC ACID B RECEPTOR; CELL SURFACE RECEPTOR; G PROTEIN COUPLED RECEPTOR;

DIMERIZATION; IMMUNOPRECIPITATION; INTERNALIZATION; LIGAND BINDING; MOLECULAR WEIGHT; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN TARGETING; RECEPTOR INTRINSIC ACTIVITY; REVIEW; SIGNAL TRANSDUCTION;

ANIMALS; DIMERIZATION; GENES, DOMINANT; GTP-BINDING PROTEINS; POLYMERS; RECEPTORS, CELL SURFACE; RECEPTORS, GABA-B; STEREOISOMERISM;

EID: 0033947541     PISSN: 10432760     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1043-2760(00)00260-5     Document Type: Review

References (55)

1. Heldin C.H. Dimerization of cell surface receptors in signal transduction. Cell. 80:1995;213-223.
2. Gether U., Kobilka B.K. G-protein-coupled receptors. II. Mechanism of agonist activation (review). J. Biol. Chem. 273:1998;17979-17982.
3. Limbird L.E.et al. Beta-adrenergic receptors. evidence for negative cooperativity Biochem. Biophys. Res. Commun. 64:1975;1160-1168.
4. Limbird L.E., Lefkowitz R.J. Negative cooperativity among beta-adrenergic receptors in frog erythrocyte membranes. J. Biol. Chem. 251:1976;5007-5014.
5. Mattera R.et al. Guanine nucleotide regulation of a mammalian myocardial muscarinic receptor system. Evidence for homo- and heterotropic cooperativity in ligand binding analyzed by computer-assisted curve fitting. J. Biol. Chem. 260:1985;7410-7421.
6. Potter L.T.et al. Evidence for paired M2 muscarinic receptors. Mol. Pharmacol. 39:1991;211-221.
7. Hirschberg B.T., Schimerlik M.I. A kinetic model for oxotremorine M binding to recombinant porcine m2 muscarinic receptors expressed in Chinese hamster ovary cells. J. Biol. Chem. 269:1994;26127-26135.
8. Wreggett K.A., Wells J.W. Cooperativity manifest in the binding properties of purified cardiac muscarinic receptors. J. Biol. Chem. 270:1995;22488-22499.
9. Conn P.M.et al. Conversion of a gonadotropin-releasing hormone antagonist to an agonist. Nature. 296:1982;653-655.
10. Hazum E., Keinan D. Gonadotropin-releasing hormone activation is mediated by dimerization of occupied receptors. Biochem. Biophys. Res. Commun. 133:1985;449-456.
11. Fraser C.M., Venter J.C. The size of the mammalian lung beta 2-adrenergic receptor as determined by target size analysis and immunoaffinity chromatography. Biochem. Biophys. Res. Commun. 109:1982;21-29.
12. Venter J.C.et al. Molecular size of the human platelet alpha 2-adrenergic receptor as determined by radiation inactivation. Biochem. Biophys. Res. Commun. 116:1983;1070-1075.
13. Venter J.C.et al. Alpha 1-adrenergic receptor structure. Mol. Pharmacol. 26:1984;196-205.
14. Lilly L.et al. Molecular size of the canine and human brain D2 dopamine receptor as determined by radiation inactivation. Mol. Pharmacol. 24:1983;10-14.
15. Bouvier C.et al. Solubilization and characterization of D2-dopamine receptors in an estrone-induced, prolactin-secreting rat pituitary adenoma. J. Neurochem. 47:1986;1653-1660.
16. Conn P.M., Venter J.C. Radiation inactivation (target size analysis) of the gonadotropin-releasing hormone receptor. evidence for a high molecular weight complex Endocrinology. 116:1985;1324-1326.
17. Frame L.T.et al. Target size of the adenosine Ri receptor. Biochem. J. 235:1986;621-624.
18. Herberg J.T.et al. The hepatic glucagon receptor. Solubilization, characterization, and development of an affinity adsorption assay for the soluble receptor. J. Biol. Chem. 259:1984;9285-9294.
19. Avissar S.et al. Oligomeric structure of muscarinic receptors is shown by photoaffinity labeling. subunit assembly may explain high- and low-affinity agonist states Proc. Natl. Acad. Sci. U. S. A. 80:1983;156-159.
20. Peterson G.L.et al. Physical properties of the purified cardiac muscarinic acetylcholine receptor. Biochemistry. 25:1986;3189-3202.
21. Maggio R.et al. Coexpression studies with mutant muscarinic/adrenergic receptors provide evidence for intermolecular 'cross-talk' between G-protein-linked receptors. Proc. Natl. Acad. Sci. U. S. A. 90:1993;3103-3107.
22. Monnot C.et al. Polar residues in the transmembrane domain of the type 1 angiotensin II receptor are required for binding and coupling. Reconstitution of the binding site by co-expression of two deficient mutants. J. Biol. Chem. 271:1996;1507-1513.
23. Bai M.et al. Intermolecular interactions between dimeric calcium-sensing receptor monomers are important for its normal function. Proc. Natl. Acad. Sci. U. S. A. 96:1999;2834-2839.
24. 2+-sensing receptor. J. Biol. Chem. 271:1996;19537-19545.
25. Zhu X., Wess J. Truncated V2 vasopressin receptors as negative regulators of wild-type V2 receptor function. Biochemistry. 37:1998;15773-15784.
26. Benkirane M.et al. Mechanism of transdominant inhibition of CCR5-mediated HIV-1 infection by ccr5delta32. J. Biol. Chem. 272:1997;30603-30606.
27. Deng H.et al. Identification of a major co-receptor for primary isolates of HIV-1. Nature. 381:1996;661-666.
28. Samson M.et al. Resistance to HIV-1 infection in Caucasian individuals bearing mutant alleles of the CCR-5 chemokine receptor gene. Nature. 382:1996;722-725.
29. Liu R.et al. Homozygous defect in HIV-1 coreceptor accounts for resistance of some multiply-exposed individuals to HIV-1 infection. Cell. 86:1996;367-377.
30. Hebert T.E.et al. Functional rescue of a constitutively desensitized beta2AR through receptor dimerization. Biochem. J. 330:1998;287-293.
31. Furthmayr H., Marchesi V.T. Subunit structure of human erythrocyte glycophorin A. Biochemistry. 15:1976;1137-1144.
32. Tobkes N.et al. Secondary structure and assembly mechanism of an oligomeric channel protein. Biochemistry. 24:1985;1915-1920.
33. Danner M.et al. Folding and assembly of phage P22 tailspike endorhamnosidase lacking the N-terminal, head-binding domain. Eur. J. Biochem. 215:1993;653-661.
34. 2+ channels. J. Biol. Chem. 263:1988;9887-9895.
35. Salhany J.M.et al. In situ cross-linking of human erythrocyte band 3 by bis(sulfosuccinimidyl)suberate. Evidence for ligand modulation of two alternate quaternary forms: covalent band 3 dimers and noncovalent tetramers formed by the association of two covalent dimers. J. Biol. Chem. 265:1990;17688-17693.
36. Schatz G., Butow R.A. How are proteins imported into mitochondria? Cell. 32:1983;316-318.
37. Hebert T.E.et al. A peptide derived from a β2-adrenergic receptor transmembrane domain inhibits both receptor dimerization and activation. J. Biol. Chem. 271:1996;16384-16392.
38. Cvejic S., Devi L.A. Dimerization of the delta opioid receptor. implication for a role in receptor internalization J. Biol. Chem. 272:1997;26959-26964.
39. Romano C.et al. Metabotropic glutamate receptor 5 is a disulfide-linked dimer. J. Biol. Chem. 271:1996;28612-28616.
40. Bai M.et al. Dimerization of the extracellular calcium-sensing receptor (CaR) on the cell surface of CaR-transfected HEK293 cells. J. Biol. Chem. 273:1998;23605-23610.
41. Kaupmann K.et al. GABA(B)-receptor subtypes assemble into functional heteromeric complexes. Nature. 396:1998;683-687.
42. White J.H.et al. Heterodimerization is required for the formation of a functional GABA(B) receptor. Nature. 396:1998;679-682.
43. Jones K.A.et al. GABA(B) receptors function as a heteromeric assembly of the subunits GABA(B)R1 and GABA(B)R2. Nature. 396:1998;674-679.
44. Jordan B.A., Devi L.A. G-protein-coupled receptor heterodimerization modulates receptor function. Nature. 399:1999;697-700.
45. Zeng F.Y., Wess J. Identification and molecular characterization of m3 muscarinic receptor dimers. J. Biol. Chem. 274:1999;19487-19497.
46. Ng G.Y.et al. Dopamine D2 receptor dimers and receptor-blocking peptides. Biochem. Biophys. Res. Commun. 227:1996;200-204.
47. Tarasova N.I.et al. Inhibition of G-protein-coupled receptor function by disruption of transmembrane domain interactions. J. Biol. Chem. 274:1999;34911-34915.
48. Zeng F.Y., Wess J. Identification and molecular characterization of m3 muscarinic receptor dimers. J. Biol. Chem. 274:1999;19487-19497.
49. Couve A.et al. Intracellular retention of recombinant GABAB receptors. J. Biol. Chem. 273:1998;26361-26367.
50. Kuner R.et al. Role of heteromer formation in GABAB receptor function. Science. 283:1999;74-77.
51. Ng G.Y.et al. Identification of a GABAB receptor subunit, gb2, required for functional GABAB receptor activity. J. Biol. Chem. 274:1999;7607-7610.
52. Xu Y.et al. A bioluminescence resonance energy transfer (BRET) system. application to interacting circadian clock proteins Proc. Natl. Acad. Sci. U. S. A. 96:1999;151-156.
53. Angers S.et al. Detection of beta2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. U. S. A. 97:2000;3684-3689.
54. Overton M.C., Blumer K.J. G protein coupled receptors function as oligomers in vivo. Curr. Biol. 10:2000;341-344.
55. Gouldson P.R.et al. Domain swapping in G-protein coupled receptor dimers. Protein Eng. 11:1998;1181-1193.