Interaction of a fragment of the cannabinoid CB1 receptor C-terminus with arrestin-2

FEBS Letters

Volumn 581, Issue 25, 2007, Pages 5009-5016

  Bakshi, Kunal ^a   Mercier, Richard W ^a   Pavlopoulos, Spiro ^a  

^a UNIVERSITY OF CONNECTICUT   (United States)

Author keywords

Arrestin; C terminus; CB1; Complex; NMR; Phosphorylation

Indexed keywords

CANNABINOID 1 RECEPTOR; GLYCINE; RETINA S ANTIGEN; RHODOPSIN;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DESENSITIZATION; HUMAN; HUMAN CELL; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN INTERACTION; PROTEIN STRUCTURE; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SEQUENCE; ARRESTINS; BINDING SITES; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; PEPTIDES; PROTEIN STRUCTURE, SECONDARY; RECEPTOR, CANNABINOID, CB1;

EID: 34948829679     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.09.030     Document Type: Article

References (43)

1. Lohse M.J., Benovic J.L., Codina J., Caron M.G., and Lefkowitz R.J. beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science 248 (1990) 1547-1550
2. Okada T., Le Trong I., Fox B.A., Behnke C.A., Stenkamp R.E., and Palczewski K. X-ray diffraction analysis of three-dimensional crystals of bovine rhodopsin obtained from mixed micelles. J. Struct. Biol. 130 (2000) 73-80
3. Palczewski K., et al. Crystal structure of rhodopsin: a G protein-coupled receptor. Science 289 (2000) 739-745
4. Yeagle P.L., and Albert A.D. G-protein coupled receptor structure. Biochim. Biophys. Acta 1768 (2007) 808-824
5. Klabunde T., and Hessler G. Drug design strategies for targeting G-protein-coupled receptors. Chembiochem 3 (2002) 928-944
6. Leifert W.R., Aloia A.L., Bucco O., and McMurchie E.J. GPCR-induced dissociation of G-protein subunits in early stage signal transduction. Mol. Membr. Biol. 22 (2005) 507-517
7. Premont R.T., and Gainetdinov R.R. Physiological roles of G protein-coupled receptor kinases and arrestins. Annu. Rev. Physiol. 69 (2007) 511-534
8. Gainetdinov R.R., Premont R.T., Bohn L.M., Lefkowitz R.J., and Caron M.G. Desensitization of G protein-coupled receptors and neuronal functions. Annu. Rev. Neurosci. 27 (2004) 107-144
9. Sibley D.R., Peters J.R., Nambi P., Caron M.G., and Lefkowitz R.J. Desensitization of turkey erythrocyte adenylate cyclase. Beta-adrenergic receptor phosphorylation is correlated with attenuation of adenylate cyclase activity. J. Biol. Chem. 259 (1984) 9742-9749
10. Stadel J.M., Nambi P., Shorr R.G., Sawyer D.F., Caron M.G., and Lefkowitz R.J. Phosphorylation of the beta-adrenergic receptor accompanies catecholamine-induced desensitization of turkey erythrocyte adenylate cyclase. Trans. Assoc. Am. Physicians 96 (1983) 137-145
11. Attramadal H., et al. Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family. J. Biol. Chem. 267 (1992) 17882-17890
12. Lefkowitz R.J., Inglese J., Koch W.J., Pitcher J., Attramadal H., and Caron M.G. G-protein-coupled receptors: regulatory role of receptor kinases and arrestin proteins. Cold Spring Harb. Symp. Quant. Biol. 57 (1992) 127-133
13. Lohse M.J., Andexinger S., Pitcher J., Trukawinski S., Codina J., Faure J.P., Caron M.G., and Lefkowitz R.J. Receptor-specific desensitization with purified proteins. Kinase dependence and receptor specificity of beta-arrestin and arrestin in the beta 2-adrenergic receptor and rhodopsin systems. J. Biol. Chem. 267 (1992) 8558-8564
14. Mukherjee S., Palczewski K., Gurevich V., Benovic J.L., Banga J.P., and Hunzicker-Dunn M. A direct role for arrestins in desensitization of the luteinizing hormone/choriogonadotropin receptor in porcine ovarian follicular membranes. Proc. Natl. Acad. Sci. USA 96 (1999) 493-498
15. Ferguson S.S.G., Zhang J., Barak L.S., and Caron M.G. G-protein-coupled receptor kinases and arrestins: Regulators of G-protein-coupled receptor sequestration. Biochem. Soc. Trans. 24 (1996) 953-959
16. Goodman Jr. O.B., Krupnick J.G., Santini F., Gurevich V.V., Penn R.B., Gagnon A.W., Keen J.H., and Benovic J.L. Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature 383 (1996) 447-450
17. Lefkowitz R.J. G protein-coupled receptors. III. New roles for receptor kinases and beta-arrestins in receptor signaling and desensitization. J. Biol. Chem. 273 (1998) 18677-18680
18. Lin F.T., Daaka Y., and Lefkowitz R.J. beta-arrestins regulate mitogenic signaling and clathrin-mediated endocytosis of the insulin-like growth factor I receptor. J. Biol. Chem. 273 (1998) 31640-31643
19. Hsieh C., Brown S., Derleth C., and Mackie K. Internalization and recycling of the CB1 cannabinoid receptor. J. Neurochem. 73 (1999) 493-501
20. Jin W., Brown S., Roche J.P., Hsieh C., Celver J.P., Kovoor A., Chavkin C., and Mackie K. Distinct domains of the CB1 cannabinoid receptor mediate desensitization and internalization. J. Neurosci. 19 (1999) 3773-3780
21. Kohout T.A., Nicholas S.L., Perry S.J., Reinhart G., Junger S., and Struthers R.S. Differential desensitization, receptor phosphorylation, beta-arrestin recruitment, and ERK1/2 activation by the two endogenous ligands for the CC chemokine receptor 7. J. Biol. Chem. 279 (2004) 23214-23222
22. Craft C.M., Whitmore D.H., and Wiechmann A.F. Cone arrestin identified by targeting expression of a functional family. J. Biol. Chem. 269 (1994) 4613-4619
23. Hirsch J.A., Schubert C., Gurevich V.V., and Sigler P.B. The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell 97 (1999) 257-269
24. Benovic J.L., Kuhn H., Weyand I., Codina J., Caron M.G., and Lefkowitz R.J. Functional desensitization of the isolated beta-adrenergic receptor by the beta-adrenergic receptor kinase: potential role of an analog of the retinal protein arrestin (48-kDa protein). Proc. Natl. Acad. Sci. USA 84 (1987) 8879-8882
25. Granzin J., Wilden U., Choe H.W., Labahn J., Krafft B., and Buldt G. X-ray crystal structure of arrestin from bovine rod outer segments. Nature 391 (1998) 918-921
26. Han M., Gurevich V.V., Vishnivetskiy S.A., Sigler P.B., and Schubert C. Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation. Structure 9 (2001) 869-880
27. Kisselev O.G., Downs M.A., McDowell J.H., and Hargrave P.A. Conformational changes in the phosphorylated C-terminal domain of rhodopsin during rhodopsin arrestin interactions. J. Biol. Chem. 279 (2004) 51203-51207
28. Kisselev O.G., McDowell J.H., and Hargrave P.A. The arrestin-bound conformation and dynamics of the phosphorylated carboxy-terminal region of rhodopsin. FEBS Lett. 564 (2004) 307-311
29. Hanson S.M., Francis D.J., Vishnivetskiy S.A., Kolobova E.A., Hubbell W.L., Klug C.S., and Gurevich V.V. Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc. Natl. Acad. Sci. USA 103 (2006) 4900-4905
30. Pavlopoulos S., Thakur G.A., Nikas S.P., and Makriyannis A. Cannabinoid receptors as therapeutic targets. Curr. Pharm. Des. 12 (2006) 1751-1769
31. Choi G., Guo J., and Makriyannis A. The conformation of the cytoplasmic helix 8 of the CB1 cannabinoid receptor using NMR and circular dichroism. Biochim. Biophys. Acta 1668 (2005) 1-9
32. Clore G.M., and Gronenborn A.M. The two-dimensional transferred nuclear Overhauser effect. J. Magn. Reson. 48 (1982) 402-417
33. Clore G.M., Nilges M., Sukumaran D.K., Brunger A.T., Karplus M., and Gronenborn A.M. The three-dimensional structure of alpha1-purothionin in solution: combined use of nuclear magnetic resonance, distance geometry and restrained molecular dynamics. Embo J. 5 (1986) 2729-2735
34. Williamson M.P., Havel T.F., and Wuthrich K. Solution conformation of proteinase inhibitor IIA from bull seminal plasma by 1H nuclear magnetic resonance and distance geometry. J. Mol. Biol. 182 (1985) 295-315
35. Clore G.M., Gronenborn A.M., Nilges M., and Ryan C.A. Three-dimensional structure of potato carboxypeptidase inhibitor in solution. A study using nuclear magnetic resonance, distance geometry, and restrained molecular dynamics. Biochemistry 26 (1987) 8012-8023
36. Wagner G., Braun W., Havel T.F., Schaumann T., Go N., and Wuthrich K. Protein structures in solution by nuclear magnetic resonance and distance geometry. The polypeptide fold of the basic pancreatic trypsin inhibitor determined using two different algorithms, DISGEO and DISMAN. J. Mol. Biol. 196 (1987) 611-639
37. Wuthrich K. NMR of Proteins and Nucleic Acids (1986), Wiley, New York
38. Chou Y.T., and Gierasch L.M. The conformation of a signal peptide bound by Escherichia coli preprotein translocase SecA. J. Biol. Chem. 280 (2005) 32753-32760
39. Blaber M., Zhang X.J., and Matthews B.W. Structural basis of amino acid alpha helix propensity. Science 260 (1993) 1637-1640
40. Yeagle P.L., Alderfer J.L., and Albert A.D. Structure of the carboxy-terminal domain of bovine rhodopsin. Nat. Struct. Biol. 2 (1995) 832-834
41. Palczewski K., Rispoli G., and Detwiler P.B. The influence of arrestin (48 K protein) and rhodopsin kinase on visual transduction. Neuron 8 (1992) 117-126
42. Zhang L., Sports C.D., Osawa S., and Weiss E.R. Rhodopsin phosphorylation sites and their role in arrestin binding. J. Biol. Chem. 272 (1997) 14762-14768
43. Szilak L., Moitra J., Krylov D., and Vinson C. Phosphorylation destabilizes alpha-helices. Nat. Struct. Biol. 4 (1997) 112-114