Insights into signaling from the β2-adrenergic receptor structure

Nature Chemical Biology

Volumn 4, Issue 7, 2008, Pages 397-403

  Audet, Martin ^a   Bouvier, Michel ^a  

^a INSTITUTE FOR RESEARCH IN IMMUNOLOGY AND CANCER   (Canada)

Author keywords

[No Author keywords available]

Indexed keywords

3 ISOPROPYLAMINO 1 (7 METHYL 4 INDANYLOXY) 2 BUTANOL; ALPRENOLOL; ATENOLOL; BETA 2 ADRENERGIC RECEPTOR; BISOPROLOL; BUCINDOLOL; CARAZOLOL; CARVEDILOL; G PROTEIN COUPLED RECEPTOR; MEMBRANE PROTEIN; METOPROLOL; PROPRANOLOL; RHODOPSIN; ADRENERGIC RECEPTOR BLOCKING AGENT; ADRENERGIC RECEPTOR STIMULATING AGENT; LIGAND;

DRUG BINDING; NONHUMAN; PRIORITY JOURNAL; PROTEIN CONFORMATION; PROTEIN STRUCTURE; REVIEW; SIGNAL TRANSDUCTION; ANIMAL; ARTICLE; BINDING SITE; CHEMICAL STRUCTURE; CHEMISTRY; GENETICS; HUMAN; METABOLISM; PROTEIN BINDING; X RAY CRYSTALLOGRAPHY; X RAY DIFFRACTION;

RUMEX;

ADRENERGIC AGONISTS; ADRENERGIC ANTAGONISTS; ANIMALS; BINDING SITES; CRYSTALLOGRAPHY, X-RAY; HUMANS; LIGANDS; MODELS, MOLECULAR; PROTEIN BINDING; PROTEIN CONFORMATION; RECEPTORS, ADRENERGIC, BETA-2; SIGNAL TRANSDUCTION; X-RAY DIFFRACTION;

EID: 45549108603     PISSN: 15524450     EISSN: 15524469     Source Type: Journal    
DOI: 10.1038/nchembio.97     Document Type: Review

References (34)

1. 2-adrenergic receptor: purification and characterization. Biochemistry 23, 4510-4518 (1984).
2. Rasmussen, S.G. et al. Crystal structure of the human beta2 adrenergic G-protein-coupled receptor. Nature 450, 383-387 (2007).
3. Cherezov, V. et al. High-resolution crystal structure of an engineered human β2-adrenergic G protein-coupled receptor. Science 318, 1258-1265 (2007).
4. Rosenbaum, D.M. et al. GPCR engineering yields high-resolution structural insights into β2-adrenergic receptor function. Science 318, 1266-1273 (2007).
5. Salom, D. et al. Crystal structure of a photoactivated deprotonated intermediate of rhodopsin. Proc. Natl. Acad. Sci. USA 103, 16123-16128 (2006).
6. Palczewski, K. et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289, 739-745 (2000).
7. Bockaert, J., Fagni, L., Dumuis, A. & Marin, P. GPCR interacting proteins (GIP). Pharmacol. Ther. 103, 203-221 (2004).
8. Lohse, M.J., Benovic, J.L., Codina, J., Caron, M.G. & Lefkowitz, R.J. β-Arrestin: a protein that regulates β-adrenergic receptor function. Science 248, 1547-1550 (1990).
9. Shenoy, S.K. & Lefkowitz, R.J. Multifaceted roles of β-arrestins in the regulation of seven-membrane-spanning receptor trafficking and signalling. Biochem. J. 375, 503-515 (2003).
10. Shenoy, S.K. et al. β-Arrestin-dependent, G protein-independent ERK1/2 activation by the β2 adrenergic receptor. J. Biol. Chem. 281, 1261-1273 (2006).
11. Daaka, Y., Luttrell, D.K. & Lefkowitz, R.J. Switching of the coupling of the β2-adrenergic receptor to different G proteins by protein kinase A. Nature 390, 88-91 (1997).
12. Azzi, M. et al. β-Arrestin-mediated activation of MAPK by inverse agonists reveals distinct active conformations for G protein-coupled receptors. Proc. Natl. Acad. Sci. USA 100, 11406-11411 (2003).
13. Galandrin, S., Oligny-Longpre, G. & Bouvier, M. The evasive nature of drug efficacy: implications for drug discovery. Trends Pharmacol. Sci. 28, 423-430 (2007).
14. Ghanouni, P. et al. Functionally different agonists induce distinct conformations in the G protein coupling domain of the β2 adrenergic receptor. J. Biol. Chem. 276, 24433-24436 (2001).
15. Swaminath, G. et al. Probing the β2 adrenoceptor binding site with catechol reveals differences in binding and activation by agonists and partial agonists. J. Biol. Chem. 280, 22165-22171 (2005).
16. Gales, C. et al. Probing the activation-promoted structural rearrangements in preassembled receptor-G protein complexes. Nat. Struct. Mol. Biol. 13, 778-786 (2006).
17. Roth, C.B., Hanson, M.A. & Stevens, R.C. Stabilization of the human β2-adrenergic receptor TM4-TM3-TM5 helix interface by mutagenesis of Glu122(3.41), a critical residue in GPCR structure. J. Mol. Biol. 376, 1305-1319 (2008).
18. Serrano-Vega, M.J., Magnani, F., Shibata, Y. & Tate, C.G. Conformational thermostabilization of the β1-adrenergic receptor in a detergent-resistant form. Proc. Natl. Acad. Sci. USA 105, 877-882 (2008).
19. Costa, T., Ogino, Y., Munson, P.J., Onaran, H.O. & Rodbard, D. Drug efficacy at guanine nucleotide-binding regulatory protein-linked receptors: thermodynamic interpretation of negative antagonism and of receptor activity in the absence of ligand. Mol. Pharmacol. 41, 549-560 (1992).
20. 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. 268, 4625-4636 (1993).
21. Chidiac, P., Hebert, T.E., Valiquette, M., Dennis, M. & Bouvier, M. Inverse agonist activity of β-adrenergic antagonists. Mol. Pharmacol. 45, 490-499 (1994).
22. Samama, P., Pei, G., Costa, T., Cotecchia, S. & Lefkowitz, R.J. Negative antagonists promote an inactive conformation of the β2- adrenergic receptor. Mol. Pharmacol. 45, 390-394 (1994).
23. Bond, R.A. & Ijzerman, A.P. Recent developments in constitutive receptor activity and inverse agonism, and their potential for GPCR drug discovery. Trends Pharmacol. Sci. 27, 92-96 (2006).
24. Milligan, G. Constitutive activity and inverse agonists of G protein-coupled receptors: a current perspective. Mol. Pharmacol. 64, 1271-1276 (2003).
25. Rovati, G.E., Capra, V. & Neubig, R.R. The highly conserved DRY motif of class A G protein-coupled receptors: beyond the ground state. Mol. Pharmacol. 71, 959-964 (2007).
26. Watson, C. et al. The use of stimulus-biased assay systems to detect agonist-specific receptor active states: implications for the trafficking of receptor stimulus by agonists. Mol. Pharmacol. 58, 1230-1238 (2000).
27. Kenakin, T. Agonist-receptor efficacy. II. Agonist trafficking of receptor signals. Trends Pharmacol. Sci. 16, 232-238 (1995).
28. Baker, J.G., Hall, I.P. & Hill, S.J. Agonist and inverse agonist actions of β-blockers at the human β 2-adrenoceptor provide evidence for agonist-directed signaling. Mol. Pharmacol. 64, 1357-1369 (2003).
29. Galandrin, S. & Bouvier, M. Distinct signaling profiles of β1 and β2 adrenergic receptor ligands towards adenylyl cyclase and mitogen-activated protein kinase reveals the pluridimensionality of efficacy. Mol. Pharmacol. 70, 1575-1584 (2006).
30. Yao, X. et al. Coupling ligand structure to specific conformational switches in the β2-adrenoceptor. Nat. Chem. Biol. 2, 417-422 (2006).
31. Janz, J.M. & Farrens, D.L. Rhodopsin activation exposes a key hydrophobic binding site for the transducin α-subunit C terminus. J. Biol. Chem. 279, 29767-29773 (2004).
32. Raimondi, F., Seeber, M., Benedetti, P.G. & Fanelli, F. Mechanisms of inter- and intramolecular communication in GPCRs and G proteins. J. Am. Chem. Soc. 130, 4310-4325 (2008).
33. 2- adrenergic receptor. EMBO J. 14, 5542-5549 (1995).
34. Karoor, V. & Malbon, C.C. Insulin-like growth factor receptor-1 stimulates phosphorylation of the β2-adrenergic receptor in vivo on sites distinct from those phosphorylated in response to insulin. J. Biol. Chem. 271, 29347-29352 (1996).