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Arrestins - Pharmacology and Therapeutic Potential pp 153–170Cite as

Targeting Individual GPCRs with Redesigned Nonvisual Arrestins

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Part of the book series: Handbook of Experimental Pharmacology ((HEP,volume 219))

Abstract

Numerous human diseases are caused by excessive signaling of mutant G protein-coupled receptors (GPCRs) or receptors that are overstimulated due to upstream signaling imbalances. The feasibility of functional compensation by arrestins with enhanced ability to quench receptor signaling was recently tested in the visual system. The results showed that even in this extremely demanding situation of rods that have no ability to phosphorylate rhodopsin, enhanced arrestin improved rod morphology, light sensitivity, survival, and accelerated photoresponse recovery. Structurally distinct enhanced mutants of arrestins that bind phosphorylated and non-phosphorylated active GPCRs with much higher affinity than parental wild-type (WT) proteins have been constructed. These “super-arrestins” are likely to have the power to dampen the signaling by hyperactive GPCRs. However, most cells express 5–20 GPCR subtypes, only one of which would be overactive, while nonvisual arrestins are remarkably promiscuous, binding hundreds of different GPCRs. Thus, to be therapeutically useful, enhanced versions of nonvisual arrestins must be made fairly specific for particular receptors. Recent identification of very few arrestin residues as key receptor discriminators paves the way to the construction of receptor subtype-specific nonvisual arrestins.

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Notes

  1. 1.

    Different systems of arrestin names are used in the field and in this book. We use systematic names of arrestin proteins: arrestin-1 (historic names S-antigen, 48 kDa protein, visual or rod arrestin), arrestin-2 (β-arrestin or β-arrestin1), arrestin-3 (β-arrestin2 or hTHY-ARRX), and arrestin-4 (cone or X-arrestin; for unclear reasons its gene is called “arrestin 3” in the HUGO database).

References

  • Ahmed MR, Berthet A, Bychkov E, Porras G, Li Q, Bioulac BH, Carl YT, Bloch B, Kook S, Aubert I, Dovero S, Doudnikoff E, Gurevich VV, Gurevich EV, Bezard E (2010) Lentiviral overexpression of GRK6 alleviates L-dopa-induced dyskinesia in experimental Parkinson's disease. Sci Transl Med 2:28ra28

    PubMed Central  PubMed  Google Scholar 

  • Almen MS, Nordstrom KJ, Fredriksson R, Schioth HB (2009) Mapping the human membrane proteome: a majority of the human membrane proteins can be classified according to function and evolutionary origin. BMC Biol 7:50

    PubMed Central  PubMed  Google Scholar 

  • Apfelstedt-Sylla E, Kunisch M, Horn M, Ruther K, Gerding H, Gal A, Zrenner E (1993) Ocular findings in a family with autosomal dominant retinitis pigmentosa and a frameshift mutation altering the carboxyl terminal sequence of rhodopsin. Br J Ophthalmol 77:495–501

    CAS  PubMed Central  PubMed  Google Scholar 

  • Araujo AR, Reis M, Rocha H, Aguiar B, Morales-Hojas R, Macedo-Ribeiro S, Fonseca NA, Reboiro-Jato D, Reboiro-Jato M, Fdez-Riverola F, Vieira CP, Vieira J (2013) The Drosophila melanogaster methuselah gene: a novel gene with ancient functions. PloS One 8:e63747

    CAS  PubMed Central  PubMed  Google Scholar 

  • Attramadal H, Arriza JL, Aoki C, Dawson TM, Codina J, Kwatra MM, Snyder SH, Caron MG, Lefkowitz RJ (1992) Beta-arrestin2, a novel member of the arrestin/beta-arrestin gene family. J Biol Chem 267:17882–17890

    CAS  PubMed  Google Scholar 

  • Barak LS, Ferguson SS, Zhang J, Caron MG (1997) A beta-arrestin/green fluorescent protein biosensor for detecting G protein-coupled receptor activation. J Biol Chem 272:27497–27500

    CAS  PubMed  Google Scholar 

  • Barak LS, Oakley RH, Laporte SA, Caron MG (2001) Constitutive arrestin-mediated desensitization of a human vasopressin receptor mutant associated with nephrogenic diabetes insipidus. Proc Natl Acad Sci USA 98:93–98

    CAS  PubMed Central  PubMed  Google Scholar 

  • Bartel MA, Weinstein JR, Schaffer DV (2012) Directed evolution of novel adeno-associated viruses for therapeutic gene delivery. Gene Ther 19:694–700

    CAS  PubMed  Google Scholar 

  • Breitman M, Kook S, Gimenez LE, Lizama BN, Palazzo MC, Gurevich EV, Gurevich VV (2012) Silent scaffolds: inhibition of c-Jun N-terminal kinase 3 activity in cell by dominant-negative arrestin-3 mutant. J Biol Chem 287:19653–19664

    CAS  PubMed Central  PubMed  Google Scholar 

  • Bruchas MR, Macey TA, Lowe JD, Chavkin C (2006) Kappa opioid receptor activation of p38 MAPK is GRK3- and arrestin-dependent in neurons and astrocytes. J Biol Chem 281:18081–18089

    CAS  PubMed Central  PubMed  Google Scholar 

  • Carman CV, Benovic JL (1998) G-protein-coupled receptors: turn-ons and turn-offs. Curr Opin Neurobiol 8:335–344

    CAS  PubMed  Google Scholar 

  • Carter JM, Gurevich VV, Prossnitz ER, Engen JR (2005) Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry. J Mol Biol 351:865–878

    CAS  PubMed  Google Scholar 

  • Celver J, Lowe J, Kovoor A, Gurevich VV, Chavkin C (2001) Threonine 180 is requred for G protein-coupled receptor kinase 3 and b-arrestin mediated desensitization of the m-opioid receptor in Xenopus oocytes. J Biol Chem 276:4894–4900

    CAS  PubMed  Google Scholar 

  • Celver J, Vishnivetskiy SA, Chavkin C, Gurevich VV (2002) Conservation of the phosphate-sensitive elements in the arrestin family of proteins. J Biol Chem 277:9043–9048

    CAS  PubMed  Google Scholar 

  • Chan S, Rubin WW, Mendez A, Liu X, Song X, Hanson SM, Craft CM, Gurevich VV, Burns ME, Chen J (2007) Functional comparisons of visual arrestins in rod photoreceptors of transgenic mice. Invest Ophthalmol Vis Sci 48:1968–1975

    PubMed Central  PubMed  Google Scholar 

  • Chen J, Makino CL, Peachey NS, Baylor DA, Simon MI (1995) Mechanisms of rhodopsin inactivation in-vivo as revealed by a CooH-terminal truncation mutant. Science 267:374–377

    CAS  PubMed  Google Scholar 

  • Claus M, Maier J, Paschke R, Kujat C, Stumvoll M, Fuhrer D (2005) Novel thyrotropin receptor germline mutation (Ile568Val) in a Saxonian family with hereditary nonautoimmune hyperthyroidism. Thyroid 15:1089–1094

    CAS  PubMed  Google Scholar 

  • Coffa S, Breitman M, Spiller BW, Gurevich VV (2011) A single mutation in arrestin-2 prevents ERK1/2 activation by reducing c-Raf1 binding. Biochemistry 50:6951–6958

    CAS  PubMed Central  PubMed  Google Scholar 

  • Craft CM, Whitmore DH, Wiechmann AF (1994) Cone arrestin identified by targeting expression of a functional family. J Biol Chem 269:4613–4619

    CAS  PubMed  Google Scholar 

  • Dalkara D, Byrne LC, Klimczak RR, Visel M, Yin L, Merigan WH, Flannery JG, Schaffer DV (2013) In vivo-directed evolution of a new adeno-associated virus for therapeutic outer retinal gene delivery from the vitreous. Sci Transl Med 5:189ra176

    Google Scholar 

  • DeWire SM, Ahn S, Lefkowitz RJ, Shenoy SK (2007) Beta-arrestins and cell signaling. Annu Rev Physiol 69:483–510

    CAS  PubMed  Google Scholar 

  • Dinculescu A, McDowell JH, Amici SA, Dugger DR, Richards N, Hargrave PA, Smith WC (2002) Insertional mutagenesis and immunochemical analysis of visual arrestin interaction with rhodopsin. J Biol Chem 277:11703–11708

    CAS  PubMed  Google Scholar 

  • Dohlman HG, Thorner J, Caron MG, Lefkowitz RJ (1991) Model systems for the study of seven-transmembrane-segment receptors. Ann Rev Biochem 60:653–688

    CAS  PubMed  Google Scholar 

  • Dorn GW 2nd, Force T (2005) Protein kinase cascades in the regulation of cardiac hypertrophy. J Clin Investig 115:527–537

    CAS  PubMed Central  PubMed  Google Scholar 

  • Gimenez LE, Hernandez CC, Mattos EC, Brandao IT, Olivieri B, Campelo RP, Araujo-Jorge T, Silva CL, Campos de Carvalho AC, Kurtenbach E (2005) DNA immunizations with M2 muscarinic and beta1 adrenergic receptor coding plasmids impair cardiac function in mice. J Mol Cell Cardiol 38:703–714

    CAS  PubMed  Google Scholar 

  • Gimenez LE, Kook S, Vishnivetskiy SA, Ahmed MR, Gurevich EV, Gurevich VV (2012a) Role of receptor-attached phosphates in binding of visual and non-visual arrestins to G protein-coupled receptors. J Biol Chem 287:9028–9040

    CAS  PubMed Central  PubMed  Google Scholar 

  • Gimenez LE, Vishnivetskiy SA, Baameur F, Gurevich VV (2012b) Manipulation of very few receptor discriminator residues greatly enhances receptor specificity of non-visual arrestins. J Biol Chem 287:29495–29505

    CAS  PubMed Central  PubMed  Google Scholar 

  • Gimenez LE, Ghildyal P, Fischer KE, Hu H, Ja WW, Eaton BA, Wu Y, Austad SN, Ranjan R (2013) Modulation of methuselah expression targeted to Drosophila insulin-producing cells extends life and enhances oxidative stress resistance. Aging cell 12:121–129

    CAS  PubMed  Google Scholar 

  • Goodman OB Jr, Krupnick JG, Santini F, Gurevich VV, Penn RB, Gagnon AW, Keen JH, Benovic JL (1996) Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor. Nature 383:447–450

    CAS  PubMed  Google Scholar 

  • Granzin J, Wilden U, Choe HW, Labahn J, Krafft B, Buldt G (1998) X-ray crystal structure of arrestin from bovine rod outer segments. Nature 391:918–921

    CAS  PubMed  Google Scholar 

  • Gray-Keller MP, Detwiler PB, Benovic JL, Gurevich VV (1997) Arrestin with a single amino acid sustitution quenches light-activated rhodopsin in a phosphorylation-independent fasion. Biochemistry 36:7058–7063

    CAS  PubMed  Google Scholar 

  • Gurevich VV (1998) The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms. J Biol Chem 273:15501–15506

    CAS  PubMed  Google Scholar 

  • Gurevich VV, Benovic JL (1992) Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction. J Biol Chem 267:21919–21923

    CAS  PubMed  Google Scholar 

  • Gurevich VV, Benovic JL (1993) Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin. J Biol Chem 268:11628–11638

    CAS  PubMed  Google Scholar 

  • Gurevich VV, Benovic JL (1995) Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin. J Biol Chem 270:6010–6016

    CAS  PubMed  Google Scholar 

  • Gurevich VV, Benovic JL (1997) Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state. Mol Pharmacol 51:161–169

    CAS  PubMed  Google Scholar 

  • Gurevich EV, Gurevich VV (2006a) Arrestins: ubiquitous regulators of cellular signaling pathways. Genome Biol 7:236

    PubMed Central  PubMed  Google Scholar 

  • Gurevich VV, Gurevich EV (2006b) The structural basis of arrestin-mediated regulation of G-protein-coupled receptors. Pharmacol Ther 110:465–502

    CAS  PubMed Central  PubMed  Google Scholar 

  • Gurevich VV, Richardson RM, Kim CM, Hosey MM, Benovic JL (1993) Binding of wild type and chimeric arrestins to the m2 muscarinic cholinergic receptor. J Biol Chem 268:16879–16882

    CAS  PubMed  Google Scholar 

  • Gurevich VV, Dion SB, Onorato JJ, Ptasienski J, Kim CM, Sterne-Marr R, Hosey MM, Benovic JL (1995) Arrestin interaction with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, b2-adrenergic, and m2 muscarinic cholinergic receptors. J Biol Chem 270:720–731

    CAS  PubMed  Google Scholar 

  • Gurevich VV, Pals-Rylaarsdam R, Benovic JL, Hosey MM, Onorato JJ (1997) Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity. J Biol Chem 272:28849–28852

    CAS  PubMed  Google Scholar 

  • Gurevich VV, Hanson SM, Song X, Vishnivetskiy SA, Gurevich EV (2011) The functional cycle of visual arrestins in photoreceptor cells. Prog Retin Eye Res 30:405–430

    CAS  PubMed Central  PubMed  Google Scholar 

  • Han M, Gurevich VV, Vishnivetskiy SA, Sigler PB, Schubert C (2001) Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation. Structure 9:869–880

    CAS  PubMed  Google Scholar 

  • Hanson SM, Gurevich VV (2006) The differential engagement of arrestin surface charges by the various functional forms of the receptor. J Biol Chem 281:3458–3462

    CAS  PubMed Central  PubMed  Google Scholar 

  • Hanson SM, Francis DJ, Vishnivetskiy SA, Kolobova EA, Hubbell WL, Klug CS, Gurevich VV (2006) Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin. Proc Natl Acad Sci USA 103:4900–4905

    CAS  PubMed Central  PubMed  Google Scholar 

  • Hernandez CC, Barcellos LC, Gimenez LE, Cabarcas RA, Garcia S, Pedrosa RC, Nascimento JH, Kurtenbach E, Masuda MO, Campos de Carvalho AC (2003) Human chagasic IgGs bind to cardiac muscarinic receptors and impair L-type Ca2+ currents. Cardiovasc Res 58:55–65

    CAS  PubMed  Google Scholar 

  • Hernandez CC, Nascimento JH, Chaves EA, Costa PC, Masuda MO, Kurtenbach E, Campos DECAC, Gimenez LE (2008) Autoantibodies enhance agonist action and binding to cardiac muscarinic receptors in chronic Chagas' disease. J Recept Signal Transduct Res 28:375–401

    CAS  PubMed Central  PubMed  Google Scholar 

  • Hirsch JA, Schubert C, Gurevich VV, Sigler PB (1999) The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulation. Cell 97:257–269

    CAS  PubMed  Google Scholar 

  • Ishikawa K, Tilemann L, Fish K, Hajjar RJ (2011) Gene delivery methods in cardiac gene therapy. J Gene Med 13:566–572

    CAS  PubMed  Google Scholar 

  • Kenakin T, Christopoulos A (2013) Signalling bias in new drug discovery: detection, quantification and therapeutic impact. Nat Rev Drug Discov 12:205–216

    CAS  PubMed  Google Scholar 

  • Khoo DH, Parma J, Rajasoorya C, Ho SC, Vassart G (1999) A germline mutation of the thyrotropin receptor gene associated with thyrotoxicosis and mitral valve prolapse in a Chinese family. J Clin Endocrinol Metab 84:1459–1462

    CAS  PubMed  Google Scholar 

  • Kim YM, Benovic JL (2002) Differential roles of arrestin-2 interaction with clathrin and adaptor protein 2 in G protein-coupled receptor trafficking. J Biol Chem 277:30760–30768

    CAS  PubMed  Google Scholar 

  • Kim RY, al-Maghtheh M, Fitzke FW, Arden GB, Jay M, Bhattacharya SS, Bird AC (1993) Dominant retinitis pigmentosa associated with two rhodopsin gene mutations. Leu-40-Arg and an insertion disrupting the 5'-splice junction of exon 5. Arch Ophthalmol 111:1518–1524

    CAS  PubMed  Google Scholar 

  • Kim OJ, Gardner BR, Williams DB, Marinec PS, Cabrera DM, Peters JD, Mak CC, Kim KM, Sibley DR (2004) The role of phosphorylation in D1 dopamine receptor desensitization: evidence for a novel mechanism of arrestin association. J Biol Chem 279:7999–8010

    CAS  PubMed  Google Scholar 

  • Kim M, Vishnivetskiy SA, Van Eps N, Alexander NS, Cleghorn WM, Zhan X, Hanson SM, Morizumi T, Ernst OP, Meiler J, Gurevich VV, Hubbell WL (2012) Conformation of receptor-bound visual arrestin. Proc Natl Acad Sci USA 109:18407–18412

    CAS  PubMed Central  PubMed  Google Scholar 

  • Kohout TA, Lin FS, Perry SJ, Conner DA, Lefkowitz RJ (2001) beta-Arrestin 1 and 2 differentially regulate heptahelical receptor signaling and trafficking. Proc Natl Acad Sci USA 98:1601–1606

    CAS  PubMed Central  PubMed  Google Scholar 

  • Kovoor A, Celver J, Abdryashitov RI, Chavkin C, Gurevich VV (1999) Targeted construction of phosphorylation-independent b-arrestin mutants with constitutive activity in cells. J Biol Chem 274:6831–6834

    CAS  PubMed  Google Scholar 

  • Kraakman L, Lemaire K, Ma P, Teunissen AW, Donaton MC, Van Dijck P, Winderickx J, de Winde JH, Thevelein JM (1999) A Saccharomyces cerevisiae G-protein coupled receptor, Gpr1, is specifically required for glucose activation of the cAMP pathway during the transition to growth on glucose. Mol Microbiol 32:1002–1012

    CAS  PubMed  Google Scholar 

  • Krupnick JG, Gurevich VV, Schepers T, Hamm HE, Benovic JL (1994) Arrestin-rhodopsin interaction. Multi-site binding delineated by peptide inhibition. J Biol Chem 269:3226–3232

    CAS  PubMed  Google Scholar 

  • Kühn H (1978) Light-regulated binding of rhodopsin kinase and other proteins to cattle photoreceptor membranes. Biochemistry 17:4389–4395

    PubMed  Google Scholar 

  • Kühn H, Hall SW, Wilden U (1984) Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin. FEBS Lett 176:473–478

    PubMed  Google Scholar 

  • Lagerstrom MC, Schioth HB (2008) Structural diversity of G protein-coupled receptors and significance for drug discovery. Nat Rev Drug Discov 7:339–357

    PubMed  Google Scholar 

  • Laporte SA, Oakley RH, Zhang J, Holt JA, Ferguson SG, Caron MG, Barak LS (1999) The 2-adrenergic receptor/arrestin complex recruits the clathrin adaptor AP-2 during endocytosis. Proc Natl Acad Sci USA 96:3712–3717

    CAS  PubMed Central  PubMed  Google Scholar 

  • Lee KB, Ptasienski JA, Pals-Rylaarsdam R, Gurevich VV, Hosey MM (2000) Arrestin binding to the M2 muscarinic acetylcholine receptor is precluded by an inhibitory element in the third intracellular loop of the receptor. J Biol Chem 275:9284–9289

    CAS  PubMed  Google Scholar 

  • Lin YJ, Seroude L, Benzer S (1998) Extended life-span and stress resistance in the Drosophila mutant methuselah. Science 282:943–946

    CAS  PubMed  Google Scholar 

  • Lohse MJ, Benovic JL, Codina J, Caron MG, Lefkowitz RJ (1990) beta-Arrestin: a protein that regulates beta-adrenergic receptor function. Science 248:1547–1550

    CAS  PubMed  Google Scholar 

  • Meng D, Lynch MJ, Huston E, Beyermann M, Eichhorst J, Adams DR, Klusmann E, Houslay MD, Baillie GS (2009) MEK1 binds directly to betaarrestin1, influencing both its phosphorylation by ERK and the timing of its isoprenaline-stimulated internalization. J Biol Chem 284:11425–11435

    CAS  PubMed Central  PubMed  Google Scholar 

  • Moaven H, Koike Y, Jao CC, Gurevich VV, Langen R, Chen J (2013) Visual arrestin interaction with clathrin adaptor AP-2 regulates photoreceptor survival in the vertebrate retina. Proc Natl Acad Sci USA 110:9463–9468

    CAS  PubMed Central  PubMed  Google Scholar 

  • Mukherjee S, Gurevich VV, Preninger A, Hamm HE, Bader M-F, Fazleabas AT, Birnbaumer L, Hunzicker-Dunn M (2002) Aspartic acid 564 in the third cytoplasmic loop of luteinizing hormone/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2. J Biol Chem 277:17916–17927

    CAS  PubMed  Google Scholar 

  • Namkung Y, Dipace C, Javitch JA, Sibley DR (2009a) G protein-coupled receptor kinase-mediated phosphorylation regulates post-endocytic trafficking of the D2 dopamine receptor. J Biol Chem 284:15038–15051

    CAS  PubMed Central  PubMed  Google Scholar 

  • Namkung Y, Dipace C, Urizar E, Javitch JA, Sibley DR (2009b) G protein-coupled receptor kinase-2 constitutively regulates D2 dopamine receptor expression and signaling independently of receptor phosphorylation. J Biol Chem 284:34103–34115

    CAS  PubMed Central  PubMed  Google Scholar 

  • Nguyen J, Szoka FC (2012) Nucleic acid delivery: the missing pieces of the puzzle? Acc Chem Res 45:1153–1162

    CAS  PubMed Central  PubMed  Google Scholar 

  • Nikonov SS, Brown BM, Davis JA, Zuniga FI, Bragin A, Pugh ENJ, Craft CM (2008) Mouse cones require an arrestin for normal inactivation of phototransduction. Neuron 59:462–474

    CAS  PubMed Central  PubMed  Google Scholar 

  • Nordstrom KJ, Sallman Almen M, Edstam MM, Fredriksson R, Schioth HB (2011) Independent HHsearch, Needleman–Wunsch-based, and motif analyses reveal the overall hierarchy for most of the G protein-coupled receptor families. Mol Biol Evol 28:2471–2480

    PubMed  Google Scholar 

  • Oakley RH, Laporte SA, Holt JA, Caron MG, Barak LS (2000) Differential affinities of visual arrestin, beta arrestin1, and beta arrestin2 for G protein-coupled receptors delineate two major classes of receptors. J Biol Chem 275:17201–17210

    CAS  PubMed  Google Scholar 

  • Ohguro H, Palczewski K, Walsh KA, Johnson RS (1994) Topographic study of arrestin using differential chemical modifications and hydrogen-deuterium exchange. Protein Sci 3:2428–2434

    CAS  PubMed Central  PubMed  Google Scholar 

  • Pals-Rylaarsdam R, Gurevich VV, Lee KB, Ptasienski J, Benovic JL, Hosey MM (1997) Internalization of the m2 muscarinic acetylcholine receptor: arrestin-independent and -dependent pathways. J Biol Chem 272:23682–23689

    CAS  PubMed  Google Scholar 

  • Pan L, Gurevich EV, Gurevich VV (2003) The nature of the arrestin x receptor complex determines the ultimate fate of the internalized receptor. J Biol Chem 278:11623–11632

    CAS  PubMed  Google Scholar 

  • Paschke R (1996) Constitutively activating TSH receptor mutations as the cause of toxic thyroid adenoma, multinodular toxic goiter and autosomal dominant non autoimmune hyperthyroidism. Exp Clin Endocrinal Diabetes 104:129–132

    CAS  Google Scholar 

  • Pulvermuller A, Schroder K, Fischer T, Hofmann KP (2000) Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin. J Biol Chem 275:37679–37685

    CAS  PubMed  Google Scholar 

  • Reiter E, Ahn S, Shukla AK, Lefkowitz RJ (2012) Molecular mechanism of beta-arrestin-biased agonism at seven-transmembrane receptors. Annu Rev Pharmacol Toxicol 52:179–197

    CAS  PubMed Central  PubMed  Google Scholar 

  • Restagno G, Maghtheh M, Bhattacharya S, Ferrone M, Garnerone S, Samuelly R, Carbonara A (1993) A large deletion at the 3' end of the rhodopsin gene in an Italian family with a diffuse form of autosomal dominant retinitis pigmentosa. Hum Mol Genet 2:207–208

    CAS  PubMed  Google Scholar 

  • Ribeiro AL, Gimenez LE, Hernandez CC, de Carvalho AC, Teixeira MM, Guedes VC, Barros MV, Lombardi F, Rocha MO (2007) Early occurrence of anti-muscarinic autoantibodies and abnormal vagal modulation in Chagas disease. Int J Cardiol 117:59–63

    PubMed  Google Scholar 

  • Rim J, Oprian DD (1995) Constitutive activation of opsin: interaction of mutants with rhodopsin kinase and arrestin. Biochemistry 34:11938–11945

    CAS  PubMed  Google Scholar 

  • Rockman HA, Chien KR, Choi DJ, Iaccarino G, Hunter JJ, Ross JJ, Lefkowitz RJ, Koch WJ (1998) Expression of a beta-adrenergic receptor kinase 1 inhibitor prevents the development of myocardial failure in gene-targeted mice. Proc Natl Acad Sci USA 95:7000–7005

    CAS  PubMed Central  PubMed  Google Scholar 

  • Schattauer SS, Miyatake M, Shankar H, Zietz C, Levin JR, Liu-Chen LY, Gurevich VV, Rieder MJ, Chavkin C (2012) Ligand directed signaling differences between rodent and human κ-opioid receptors. J Biol Chem 287:41595–41607

    CAS  PubMed Central  PubMed  Google Scholar 

  • Schipani E, Kruse K, Juppner H (1995) A constitutively active mutant PTH-PTHrP receptor in Jansen-type metaphyseal chondrodysplasia. Science 268:98–100

    CAS  PubMed  Google Scholar 

  • Schöneberg T, Schulz A, Biebermann H, Hermsdorf T, Römpler H, Sangkuhl K (2004) Mutant G-protein-coupled receptors as a cause of human diseases. Pharmacol Ther 104:173–206

    PubMed  Google Scholar 

  • Seo J, Tsakem EL, Breitman M, Gurevich VV (2011) Identification of arrestin-3-specific residues necessary for JNK3 activation. J Biol Chem 286:27894–27901

    CAS  PubMed Central  PubMed  Google Scholar 

  • Shukla AK, Manglik A, Kruse AC, Xiao K, Reis RI, Tseng WC, Staus DP, Hilger D, Uysal S, Huang LY, Paduch M, Tripathi-Shukla P, Koide A, Koide S, Weis WI, Kossiakoff AA, Kobilka BK, Lefkowitz RJ (2013) Structure of active β-arrestin-1 bound to a G-protein-coupled receptor phosphopeptide. Nature 497:137–141

    CAS  PubMed Central  PubMed  Google Scholar 

  • Song X, Vishnivetskiy SA, Gross OP, Emelianoff K, Mendez A, Chen J, Gurevich EV, Burns ME, Gurevich VV (2009) Enhanced arrestin facilitates recovery and protects rods lacking rhodopsin phosphorylation. Curr Biol 19:700–705

    CAS  PubMed Central  PubMed  Google Scholar 

  • Stavrakis S, Yu X, Patterson E, Huang S, Hamlett SR, Chalmers L, Pappy R, Cunningham MW, Morshed SA, Davies TF, Lazzara R, Kem DC (2009) Activating autoantibodies to the beta-1 adrenergic and m2 muscarinic receptors facilitate atrial fibrillation in patients with Graves’ hyperthyroidism. J Am Coll Cardiol 54:1309–1316

    CAS  PubMed Central  PubMed  Google Scholar 

  • Stavrakis S, Kem DC, Patterson E, Lozano P, Huang S, Szabo B, Cunningham MW, Lazzara R, Yu X (2011) Opposing cardiac effects of autoantibody activation of beta-adrenergic and M2 muscarinic receptors in cardiac-related diseases. Int J Cardiol 148:331–336

    PubMed Central  PubMed  Google Scholar 

  • Sutton RB, Vishnivetskiy SA, Robert J, Hanson SM, Raman D, Knox BE, Kono M, Navarro J, Gurevich VV (2005) Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity. J Mol Biol 354:1069–1080

    CAS  PubMed  Google Scholar 

  • Suwa M, Ono Y (2009) Computational overview of GPCR gene universe to support reverse chemical genomics study. Methods Mol Biol 577:41–54

    Google Scholar 

  • Vassart G, Costagliola S (2011) G protein-coupled receptors: mutations and endocrine diseases. Nat Rev Endocrinol 7:362–372

    CAS  PubMed  Google Scholar 

  • Versele M, Lemaire K, Thevelein JM (2001) Sex and sugar in yeast: two distinct GPCR systems. EMBO Rep 2:574–579

    CAS  PubMed Central  PubMed  Google Scholar 

  • Vishnivetskiy SA, Paz CL, Schubert C, Hirsch JA, Sigler PB, Gurevich VV (1999) How does arrestin respond to the phosphorylated state of rhodopsin? J Biol Chem 274:11451–11454

    CAS  PubMed  Google Scholar 

  • Vishnivetskiy SA, Schubert C, Climaco GC, Gurevich YV, Velez MG, Gurevich VV (2000) An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activation. J Biol Chem 275:41049–41057

    CAS  PubMed  Google Scholar 

  • Vishnivetskiy SA, Hosey MM, Benovic JL, Gurevich VV (2004) Mapping the arrestin-receptor interface: structural elements responsible for receptor specificity of arrestin proteins. J Biol Chem 279:1262–1268

    CAS  PubMed  Google Scholar 

  • Vishnivetskiy SA, Francis D, Van Eps N, Kim M, Hanson SM, Klug CS, Hubbell WL, Gurevich VV (2010) The role of arrestin alpha-helix I in receptor binding. J Mol Biol 395:42–54

    CAS  PubMed Central  PubMed  Google Scholar 

  • Vishnivetskiy SA, Gimenez LE, Francis DJ, Hanson SM, Hubbell WL, Klug CS, Gurevich VV (2011) Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins. J Biol Chem 286:24288–24299

    CAS  PubMed Central  PubMed  Google Scholar 

  • Vishnivetskiy SA, Baameur F, Findley KR, Gurevich VV (2013) Critical role of the central 139-loop in stability and binding selectivity of arrestin-1. J Biol Chem 288:11741–11750

    CAS  PubMed  Google Scholar 

  • Walther C, Nagel S, Gimenez LE, Morl K, Gurevich VV, Beck-Sickinger AG (2010) Ligand-induced internalization and recycling of the human neuropeptide Y2 receptor is regulated by its carboxyl-terminal tail. J Biol Chem 285:41578–41590

    CAS  PubMed Central  PubMed  Google Scholar 

  • Zhan X, Gimenez LE, Gurevich VV, Spiller BW (2011) Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual subtypes. J Mol Biol 406:467–478

    CAS  PubMed Central  PubMed  Google Scholar 

  • Zhuang T, Chen Q, Cho MK, Vishnivetskiy SA, Iverson TM, Gurevich VV, Sanders CR (2013) Involvement of distinct arrestin-1 elements in binding to different functional forms of rhodopsin. Proc Natl Acad Sci USA 110:942–947

    CAS  PubMed Central  PubMed  Google Scholar 

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Authors and Affiliations

  1. Department of Pharmacology, Vanderbilt University, 2200 Pierce Avenue, Nashville, TN, 37232, USA

    Luis E. Gimenez, Sergey A. Vishnivetskiy & Vsevolod V. Gurevich

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  1. Luis E. Gimenez
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  2. Sergey A. Vishnivetskiy
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  3. Vsevolod V. Gurevich
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Correspondence to Luis E. Gimenez .

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  1. Professor of Pharmacology, Vanderbilt University Medical Center, Nashville, Tennessee, USA

    Vsevolod V. Gurevich

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Gimenez, L.E., Vishnivetskiy, S.A., Gurevich, V.V. (2014). Targeting Individual GPCRs with Redesigned Nonvisual Arrestins. In: Gurevich, V. (eds) Arrestins - Pharmacology and Therapeutic Potential. Handbook of Experimental Pharmacology, vol 219. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-41199-1_8

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