GPCR monomers and oligomers: it takes all kinds

Trends in Neurosciences

Volumn 31, Issue 2, 2008, Pages 74-81

  Gurevich, Vsevolod V ^a   Gurevich, Eugenia V ^a  

^a VANDERBILT UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

G PROTEIN COUPLED RECEPTOR; G PROTEIN COUPLED RECEPTOR KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; MONOMER; OLIGOMER; RETINA S ANTIGEN;

CELL MATURATION; CELL MEMBRANE TRANSPORT; ENDOCYTOSIS; ENDOPLASMIC RETICULUM; ENDOSOME; GOLGI COMPLEX; HUMAN; LIFE CYCLE; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; PROTEIN SYNTHESIS; QUALITY CONTROL; REVIEW; STOICHIOMETRY;

ANIMALS; HUMANS; PROTEIN CONFORMATION; RECEPTORS, G-PROTEIN-COUPLED; SIGNAL TRANSDUCTION;

EID: 39149104024     PISSN: 01662236     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.tins.2007.11.007     Document Type: Review

References (70)

1. Kobilka B.K. G protein coupled receptor structure and activation. Biochim. Biophys. Acta 1768 (2007) 794-807
2. Moore C.A., et al. Regulation of receptor trafficking by GRKs and arrestins. Annu. Rev. Physiol. 69 (2007) 451-482
3. Gurevich V.V., and Gurevich E.V. The molecular acrobatics of arrestin activation. Trends Pharmacol. Sci. 25 (2004) 105-111
4. Goodman Jr. O.B., et al. β-Arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor. Nature 383 (1996) 447-450
5. Laporte S.A., et al. The β2-adrenergic receptor/βarrestin complex recruits the clathrin adaptor AP-2 during endocytosis. Proc. Natl. Acad. Sci. U. S. A. 96 (1999) 3712-3717
6. DeWire S.M., et al. β-Arrestins and cell signaling. Annu. Rev. Physiol. 69 (2007) 483-510
7. Gurevich E.V., and Gurevich V.V. Arrestins are ubiquitous regulators of cellular signaling pathways. Genome Biol. 7 (2006) 236
8. Fotiadis D., et al. Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors. Curr. Opin. Struct. Biol. 16 (2006) 252-259
9. Chabre M., and le Maire M. Monomeric G-protein-coupled receptor as a functional unit. Biochemistry 44 (2005) 9395-9403
10. White J.H., et al. Heterodimerization is required for the formation of a functional GABA(B) receptor. Nature 396 (1998) 679-682
11. Kaupmann K., et al. GABA(B)-receptor subtypes assemble into functional heteromeric complexes. Nature 396 (1998) 683-687
12. 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
13. Pin J.P., et al. Allosteric functioning of dimeric class C G-protein-coupled receptors. FEBS J. 272 (2005) 2947-2955
14. Kristiansen K. Molecular mechanisms of ligand binding, signaling, and regulation within the superfamily of G-protein-coupled receptors: molecular modeling and mutagenesis approaches to receptor structure and function. Pharmacol. Ther. 103 (2004) 21-80
15. Bulenger S., et al. Emerging role of homo- and heterodimerization in G-protein-coupled receptor biosynthesis and maturation. Trends Pharmacol. Sci. 26 (2005) 131-137
16. Meyer B.H., et al. FRET imaging reveals that functional neurokinin-1 receptors are monomeric and reside in membrane microdomains of live cells. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 2138-2143
17. Prinster S.C., et al. α2C-adrenergic receptors exhibit enhanced surface expression and signaling upon association with β2-adrenergic receptors. J. Pharmacol. Exp. Ther. 318 (2006) 974-981
18. Uberti M.A., et al. Heterodimerization with β2-adrenergic receptors promotes surface expression and functional activity of α1D-adrenergic receptors. J. Pharmacol. Exp. Ther. 313 (2005) 16-23
19. Concepcion F., et al. The carboxyl-terminal domain is essential for rhodopsin transport in rod photoreceptors. Vision Res. 42 (2002) 417-426
20. White J.F., et al. Dimerization of the class A G protein-coupled neurotensin receptor NTS1 alters G protein interaction. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 12199-12204
21. Terrillon S., and Bouvier M. Roles of G-protein-coupled receptor dimerization. EMBO Rep. 5 (2004) 30-34
22. Huttenrauch F., et al. G protein-coupled receptor kinases promote phosphorylation and β-arrestin-mediated internalization of CCR5 homo- and hetero-oligomers. J. Biol. Chem. 280 (2005) 37503-37515
23. Guo W., et al. Crosstalk in G protein-coupled receptors: changes at the transmembrane homodimer interface determine activation. Proc. Natl. Acad. Sci. U. S. A. 102 (2005) 17495-17500
24. Klco J.M., et al. C5a receptor oligomerization. I. Disulfide trapping reveals oligomers and potential contact surfaces in a G protein-coupled receptor. J. Biol. Chem. 278 (2003) 35345-35353
25. Kota P., et al. Opsin is present as dimers in COS1 cells: identification of amino acids at the dimeric interface. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 3054-3059
26. Berthouze M., et al. Two transmembrane Cys residues are involved in 5-HT4 receptor dimerization. Biochem. Biophys. Res. Commun. 356 (2007) 642-647
27. Luttrell L.M., et al. β-Arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes. Science 283 (1999) 655-661
28. Fotiadis D., et al. Atomic-force microscopy: rhodopsin dimers in native disc membranes. Nature 421 (2003) 127-128
29. Liang Y., et al. Organization of the G protein-coupled receptors rhodopsin and opsin in native membranes. J. Biol. Chem. 278 (2003) 21655-21662
30. Grant M., et al. Agonist-dependent dissociation of human somatostatin receptor 2 dimers: a role in receptor trafficking. J. Biol. Chem. 279 (2004) 36179-36183
31. Cvejic S., and Devi L.A. Dimerization of the δ opioid receptor: implication for a role in receptor internalization. J. Biol. Chem. 272 (1997) 26959-26964
32. 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
33. Angers S., et al. Detection of β 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. U. S. A. 97 (2000) 3684-3689
34. Jastrzebska B., et al. Functional and structural characterization of rhodopsin oligomers. J. Biol. Chem. 281 (2006) 11917-11922
35. Bayburt T.H., et al. Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins. J. Biol. Chem. 282 (2007) 14875-14881
36. Baneres J.L., and Parello J. Structure-based analysis of GPCR function: evidence for a novel pentameric assembly between the dimeric leukotriene B4 receptor BLT1 and the G-protein. J. Mol. Biol. 329 (2003) 815-829
37. Damian M., et al. Asymmetric conformational changes in a GPCR dimer controlled by G-proteins. EMBO J. 25 (2006) 5693-5702
38. Hlavackova V., et al. Evidence for a single heptahelical domain being turned on upon activation of a dimeric GPCR. EMBO J. 24 (2005) 499-509
39. Ernst O.P., et al. Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 10859-10864
40. Whorton M.R., et al. A monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 7682-7687
41. Palczewski K., et al. Mechanism of rhodopsin kinase activation. J. Biol. Chem. 266 (1991) 12949-12955
42. Binder B.M., et al. Light activation of one rhodopsin molecule causes the phosphorylation of hundreds of others. A reaction observed in electropermeabilized frog rod outer segments exposed to dim illumination. J. Biol. Chem. 265 (1990) 15333-15340
43. Shi G.W., et al. Light causes phosphorylation of nonactivated visual pigments in intact mouse rod photoreceptor cells. J. Biol. Chem. 280 (2005) 41184-41191
44. Li J., et al. Structure of bovine rhodopsin in a trigonal crystal form. J. Mol. Biol. 343 (2004) 1409-1438
45. Palczewski K., et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289 (2000) 739-745
46. Hirsch J.A., et al. The 2.8 Å crystal structure of visual arrestin: a model for arrestin's regulation. Cell 97 (1999) 257-269
47. Han M., et al. Crystal structure of β-arrestin at 1.9 Å: possible mechanism of receptor binding and membrane translocation. Structure 9 (2001) 869-880
48. Sutton R.B., et al. Crystal structure of cone arrestin at 2.3 Å: evolution of receptor specificity. J. Mol. Biol. 354 (2005) 1069-1080
49. Nair K.S., et al. Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions. Neuron 46 (2005) 555-567
50. Hanson S.M., et al. Each rhodopsin molecule binds its own arrestin. Proc. Natl. Acad. Sci. U. S. A. 104 (2007) 3125-3128
51. Strissel K.J., et al. Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsin. J. Neurosci. 26 (2006) 1146-1153
52. Hanson S.M., et al. Structure and function of the visual arrestin oligomer. EMBO J. 26 (2007) 1726-1736
53. Celver J., et al. Conservation of the phosphate-sensitive elements in the arrestin family of proteins. J. Biol. Chem. 277 (2002) 9043-9048
54. Kovoor A., et al. Targeted construction of phosphorylation-independent β-arrestin mutants with constitutive activity in cells. J. Biol. Chem. 274 (1999) 6831-6834
55. Vishnivetskiy S.A., et al. Mapping the arrestin-receptor interface: structural elements responsible for receptor specificity of arrestin proteins. J. Biol. Chem. 279 (2004) 1262-1268
56. Vishnivetskiy S.A., et al. How does arrestin respond to the phosphorylated state of rhodopsin?. J. Biol. Chem. 274 (1999) 11451-11454
57. Gurevich V.V., et al. Arrestin interaction with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, β2-adrenergic, and m2 muscarinic cholinergic receptors. J. Biol. Chem. 270 (1995) 720-731
58. Lefkowitz R.J., and Shenoy S.K. Transduction of receptor signals by β-arrestins. Science 308 (2005) 512-517
59. Gurevich V.V., and Gurevich E.V. The structural basis of arrestin-mediated regulation of G protein-coupled receptors. Pharmacol. Ther. 110 (2006) 465-502
60. Kim Y.M., and Benovic J.L. Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking. J. Biol. Chem. 277 (2002) 30760-30768
61. Hanson S.M., et al. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 4900-4905
62. Daaka Y., et al. Essential role for G protein-coupled receptor endocytosis in the activation of mitogen-activated protein kinase. J. Biol. Chem. 273 (1998) 685-688
63. DeGraff J.L., et al. Role of arrestins in endocytosis and signaling of α2-adrenergic receptor subtypes. J. Biol. Chem. 274 (1999) 11253-11259
64. Jordan B.A., and Devi L.A. G-protein-coupled receptor heterodimerization modulates receptor function. Nature 399 (1999) 697-700
65. Jordan B.A., et al. Oligomerization of opioid receptors with β 2-adrenergic receptors: a role in trafficking and mitogen-activated protein kinase activation. Proc. Natl. Acad. Sci. U. S. A. 98 (2001) 343-348
66. Shcherbakova O.G., et al. Organization of β-adrenoceptor signaling compartments by sympathetic innervation of cardiac myocytes. J. Cell Biol. 176 (2007) 521-533
67. Brum P.C., et al. Differential targeting and function of α2A and α2C adrenergic receptor subtypes in cultured sympathetic neurons. Neuropharmacology 51 (2006) 397-413
68. Vilardaga J.P., et al. Differential conformational requirements for activation of G proteins and the regulatory proteins arrestin and G protein-coupled receptor kinase in the G protein-coupled receptor for parathyroid hormone (PTH)/PTH-related protein. J. Biol. Chem. 276 (2001) 33435-33443
69. Norgaard-Nielsen K., et al. Zn(2+) site engineering at the oligomeric interface of the dopamine transporter. FEBS Lett. 524 (2002) 87-91
70. Jeschke G., and Polyhach Y. Distance measurements on spin-labelled biomacromolecules by pulsed electron paramagnetic resonance. Phys. Chem. Chem. Phys. 9 (2007) 1895-1910