{"status":"ok","message-type":"work","message-version":"1.0.0","message":{"indexed":{"date-parts":[[2026,10,14]],"date-time":"2026-10-14T10:59:49Z","timestamp":1791975589079,"version":"4.4.0"},"reference-count":242,"publisher":"Elsevier BV","issue":"6","license":[{"start":{"date-parts":[[2011,11,1]],"date-time":"2011-11-01T00:00:00Z","timestamp":1320105600000},"content-version":"tdm","delay-in-days":0,"URL":"https:\/\/www.elsevier.com\/tdm\/userlicense\/1.0\/"}],"funder":[{"name":"NIH","award":["EY011500"],"award-info":[{"award-number":["EY011500"]}]},{"name":"NIH","award":["GM077561"],"award-info":[{"award-number":["GM077561"]}]},{"name":"NIH","award":["GM081756"],"award-info":[{"award-number":["GM081756"]}]},{"name":"NIH","award":["NS045117"],"award-info":[{"award-number":["NS045117"]}]},{"name":"NIH","award":["NS065868"],"award-info":[{"award-number":["NS065868"]}]},{"name":"NIH","award":["EY008126"],"award-info":[{"award-number":["EY008126"]}]}],"content-domain":{"domain":[],"crossmark-restriction":false},"short-container-title":["Progress in Retinal and Eye Research"],"published-print":{"date-parts":[[2011,11]]},"DOI":"10.1016\/j.preteyeres.2011.07.002","type":"journal-article","created":{"date-parts":[[2011,8,2]],"date-time":"2011-08-02T18:04:56Z","timestamp":1312308296000},"page":"405-430","source":"Crossref","is-referenced-by-count":117,"title":["The functional cycle of visual arrestins in photoreceptor cells"],"prefix":"10.1016","volume":"30","author":[{"given":"Vsevolod V.","family":"Gurevich","sequence":"first","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Susan M.","family":"Hanson","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Xiufeng","family":"Song","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Sergey A.","family":"Vishnivetskiy","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]},{"given":"Eugenia V.","family":"Gurevich","sequence":"additional","affiliation":[],"role":[{"vocabulary":"crossref","role":"author"}]}],"member":"78","reference":[{"key":"10.1016\/j.preteyeres.2011.07.002_bib1","doi-asserted-by":"crossref","first-page":"3749","DOI":"10.1021\/bi200175q","article-title":"Ubiquitin ligase parkin promotes Mdm2-arrestin interaction but inhibits arrestin ubiquitination","author":"Ahmed","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib2","doi-asserted-by":"crossref","first-page":"6072","DOI":"10.1073\/pnas.96.11.6072","article-title":"A\u00a0role for the light-dependent phosphorylation of visual arrestin","volume":"96","author":"Alloway","year":"1999","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib3","doi-asserted-by":"crossref","first-page":"7439","DOI":"10.1073\/pnas.0802515105","article-title":"High-resolution distance mapping in rhodopsin reveals the pattern of helix movement due to activation","volume":"105","author":"Altenbach","year":"2008","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib4","doi-asserted-by":"crossref","first-page":"495","DOI":"10.1136\/bjo.77.8.495","article-title":"Ocular findings in a family with autosomal dominant retinitis pigmentosa and a frameshift mutation altering the carboxyl terminal sequence of rhodopsin","volume":"77","author":"Apfelstedt-Sylla","year":"1993","journal-title":"Br. J. Ophthalmol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib5","doi-asserted-by":"crossref","first-page":"1067","DOI":"10.1016\/j.jmb.2008.01.066","article-title":"Rapid incorporation of functional rhodopsin into nanoscale apolipoprotein bound bilayer (NABB) particles","volume":"377","author":"Banerjee","year":"2008","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib6","doi-asserted-by":"crossref","first-page":"14875","DOI":"10.1074\/jbc.M701433200","article-title":"Transducin activation by nanoscale lipid bilayers containing one and two rhodopsins","volume":"282","author":"Bayburt","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib7","doi-asserted-by":"crossref","first-page":"1420","DOI":"10.1074\/jbc.M110.151043","article-title":"Rhodopsin monomer is sufficient for normal rhodopsin kinase (GRK1) phosphorylation and arrestin-1 binding","volume":"286","author":"Bayburt","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib8","doi-asserted-by":"crossref","first-page":"613","DOI":"10.1113\/jphysiol.1979.sp012716","article-title":"Responses of retinal rods to single photons","volume":"288","author":"Baylor","year":"1979","journal-title":"J.\u00a0Physiol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib9","doi-asserted-by":"crossref","first-page":"591","DOI":"10.1113\/jphysiol.1980.sp013529","article-title":"Two components of electrical dark noise in toad retinal rod outer segments","volume":"309","author":"Baylor","year":"1980","journal-title":"J.\u00a0Physiol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib10","doi-asserted-by":"crossref","first-page":"235","DOI":"10.1126\/science.2552582","article-title":"Beta-adrenergic receptor kinase: primary structure delineates a multigene family","volume":"246","author":"Benovic","year":"1989","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib11","doi-asserted-by":"crossref","first-page":"8879","DOI":"10.1073\/pnas.84.24.8879","article-title":"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)","volume":"84","author":"Benovic","year":"1987","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib12","doi-asserted-by":"crossref","first-page":"20660","DOI":"10.1074\/jbc.M501338200","article-title":"Divergent distribution in vascular and avascular mammalian retinae links neuroglobin to cellular respiration","volume":"280","author":"Bentmann","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib13","doi-asserted-by":"crossref","first-page":"36971","DOI":"10.1074\/jbc.M705085200","article-title":"Arrestin-2 interacts with the ubiquitin-protein isopeptide ligase atrophin-interacting protein 4 and mediates endosomal sorting of the chemokine receptor CXCR4","volume":"282","author":"Bhandari","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib14","doi-asserted-by":"crossref","first-page":"15333","DOI":"10.1016\/S0021-9258(18)77260-8","article-title":"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","volume":"265","author":"Binder","year":"1990","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib15","doi-asserted-by":"crossref","first-page":"19826","DOI":"10.1074\/jbc.271.33.19826","article-title":"Phosphorylation of non-bleached rhodopsin in intact retinas and living frogs","volume":"271","author":"Binder","year":"1996","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib16","first-page":"1603","article-title":"Abnormal activation and inactivation mechanisms of rod transduction in patients with autosomal dominant retinitis pigmentosa and the pro-23-his mutation","volume":"36","author":"Birch","year":"1995","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib17","doi-asserted-by":"crossref","first-page":"3363","DOI":"10.1529\/biophysj.107.114058","article-title":"Diffusion of the second messengers in the cytoplasm acts as a variability suppressor of the single photon response in vertebrate phototransduction","volume":"94","author":"Bisegna","year":"2008","journal-title":"Biophys. J."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib18","doi-asserted-by":"crossref","first-page":"585","DOI":"10.1126\/science.3101175","article-title":"Diurnal expression of transducin mRNA and translocation of transducin in rods of rat retina","volume":"235","author":"Brann","year":"1987","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib19","doi-asserted-by":"crossref","first-page":"613","DOI":"10.3109\/02713688508999993","article-title":"Light induced shift and binding of S-antigen in retinal rods","volume":"4","author":"Broekhuyse","year":"1985","journal-title":"Curr. Eye Res."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib20","doi-asserted-by":"crossref","first-page":"18081","DOI":"10.1074\/jbc.M513640200","article-title":"Kappa opioid receptor activation of p38 MAPK is GRK3- and arrestin-dependent in neurons and astrocytes","volume":"281","author":"Bruchas","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib21","doi-asserted-by":"crossref","first-page":"387","DOI":"10.1016\/j.neuron.2005.10.014","article-title":"Beyond counting photons: trials and trends in vertebrate visual transduction","volume":"48","author":"Burns","year":"2005","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib22","doi-asserted-by":"crossref","first-page":"1036","DOI":"10.1523\/JNEUROSCI.3301-05.2006","article-title":"Deactivation of phosphorylated and nonphosphorylated rhodopsin by arrestin splice variants","volume":"26","author":"Burns","year":"2006","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib23","doi-asserted-by":"crossref","first-page":"72","DOI":"10.1152\/physiol.00001.2010","article-title":"Lessons from photoreceptors: turning off g-protein signaling in living cells","volume":"25","author":"Burns","year":"2010","journal-title":"Physiology (Bethesda)"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib24","doi-asserted-by":"crossref","first-page":"1538","DOI":"10.1016\/j.bpj.2009.06.037","article-title":"RGS9 concentration matters in rod phototransduction","volume":"97","author":"Burns","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib25","doi-asserted-by":"crossref","first-page":"1907","DOI":"10.1073\/pnas.90.5.1907","article-title":"Regulatory arrestin cycle secures the fidelity and maintenance of the fly photoreceptor cell","volume":"90","author":"Byk","year":"1993","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib26","doi-asserted-by":"crossref","first-page":"90","DOI":"10.1038\/35075083","article-title":"Membrane protein diffusion sets the speed of rod phototransduction","volume":"411","author":"Calvert","year":"2001","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib27","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1007\/978-1-4615-0121-3_3","article-title":"The time course of light adaptation in vertebrate retinal rods","volume":"514","author":"Calvert","year":"2002","journal-title":"Adv. Exp. Med. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib28","doi-asserted-by":"crossref","first-page":"865","DOI":"10.1016\/j.jmb.2005.06.048","article-title":"Conformational differences between arrestin2 and pre-activated mutants as revealed by hydrogen exchange mass spectrometry","volume":"351","author":"Carter","year":"2005","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib29","doi-asserted-by":"crossref","unstructured":"Caruso, G., Bisegna, P., Andreucci, D., Lenoci, L., Gurevich, V.V., Hamm, H.E., DiBenedetto, E., 2011. Identification of key factors that reduce the variability of the single photon response. Proc. Nat. Acad. Sci. USA, 108, 7804\u20137807.","DOI":"10.1073\/pnas.1018960108"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib30","doi-asserted-by":"crossref","first-page":"e1001031","DOI":"10.1371\/journal.pcbi.1001031","article-title":"Kinetics of rhodopsin inactivation and its role in regulating recovery and reproducibility of rod photoresponse","volume":"6","author":"Caruso","year":"2010","journal-title":"PLoS Computational Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib31","doi-asserted-by":"crossref","first-page":"9043","DOI":"10.1074\/jbc.M107400200","article-title":"Conservation of the phosphate-sensitive elements in the arrestin family of proteins","volume":"277","author":"Celver","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib32","doi-asserted-by":"crossref","first-page":"9395","DOI":"10.1021\/bi050720o","article-title":"Monomeric G-protein-coupled receptor as a functional unit","volume":"44","author":"Chabre","year":"2005","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib33","doi-asserted-by":"crossref","first-page":"1968","DOI":"10.1167\/iovs.06-1287","article-title":"Functional comparisons of visual arrestins in rod photoreceptors of transgenic mice","volume":"48","author":"Chan","year":"2007","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib34","doi-asserted-by":"crossref","first-page":"3718","DOI":"10.1073\/pnas.96.7.3718","article-title":"Abnormal photoresponses and light-induced apoptosis in rods lacking rhodopsin kinase","volume":"96","author":"Chen","year":"1999","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib35","doi-asserted-by":"crossref","first-page":"374","DOI":"10.1126\/science.7824934","article-title":"Mechanisms of rhodopsin inactivation in\u00a0vivo as revealed by a COOH-terminal truncation mutant","volume":"267","author":"Chen","year":"1995","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib36","doi-asserted-by":"crossref","first-page":"651","DOI":"10.1038\/nature09789","article-title":"Crystal structure of metarhodopsin II","volume":"471","author":"Choe","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib37","doi-asserted-by":"crossref","first-page":"328","DOI":"10.1073\/pnas.95.1.328","article-title":"Null mutation in the rhodopsin kinase gene slows recovery kinetics of rod and cone phototransduction in man","volume":"95","author":"Cideciyan","year":"1998","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib38","doi-asserted-by":"crossref","unstructured":"Cleghorn, W.M., Tsakem, E.L., Song, X., Vishnivetskiy, S.A., Seo, J., Chen, J., Gurevich, E.V., Gurevich, V.V., 2011. Progressive reduction of its expression in rods reveals two pools of arrestin-1 in the outer segment with different roles in photoresponse recovery. PLoS One 6, e22797.","DOI":"10.1371\/journal.pone.0022797"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib39","doi-asserted-by":"crossref","unstructured":"Coffa, S., Breitman, M., Spiller, B.W., Gurevich, V.V., 2011. A single mutation in arrestin-2 prevents ERK1\/2 activation by reducing c-Raf1 binding. Biochemistry. 50, 6951\u20136958.","DOI":"10.1021\/bi200745k"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib40","doi-asserted-by":"crossref","first-page":"820","DOI":"10.1038\/221820a0","article-title":"Rhodopsin cycle in the living eye of the rat","volume":"221","author":"Cone","year":"1969","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib41","doi-asserted-by":"crossref","first-page":"4613","DOI":"10.1016\/S0021-9258(17)41820-5","article-title":"Cone arrestin identified by targeting expression of a functional family","volume":"269","author":"Craft","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib42","doi-asserted-by":"crossref","first-page":"11703","DOI":"10.1074\/jbc.M111833200","article-title":"Insertional mutagenesis and immunochemical analysis of visual arrestin interaction with rhodopsin","volume":"277","author":"Dinculescu","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib43","doi-asserted-by":"crossref","first-page":"117","DOI":"10.1007\/s11010-009-0328-6","article-title":"Mg2+\/Ca2+ cation binding cycle of guanylyl cyclase activating proteins (GCAPs): role in regulation of photoreceptor guanylyl cyclase","volume":"334","author":"Dizhoor","year":"2010","journal-title":"Mol. Cell Biochem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib44","doi-asserted-by":"crossref","first-page":"11867","DOI":"10.1523\/JNEUROSCI.0819-09.2009","article-title":"Arrestin competition influences the kinetics and variability of the single-photon responses of mammalian rod photoreceptors","volume":"29","author":"Doan","year":"2009","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib45","doi-asserted-by":"crossref","first-page":"530","DOI":"10.1126\/science.1126612","article-title":"Multiple phosphorylation sites confer reproducibility of the rod\u2019s single-photon responses","volume":"313","author":"Doan","year":"2006","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib46","doi-asserted-by":"crossref","first-page":"711","DOI":"10.1017\/S0952523800175054","article-title":"Microtubules in a rod-specific cytoskeleton associated with outer segment incisures","volume":"17","author":"Eckmiller","year":"2000","journal-title":"Vis. Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib47","first-page":"672","article-title":"Temporal kinetics of the light\/dark translocation and compartmentation of arrestin and alpha-transducin in mouse photoreceptor cells","volume":"10","author":"Elias","year":"2004","journal-title":"Mol. Vis."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib48","doi-asserted-by":"crossref","first-page":"10859","DOI":"10.1073\/pnas.0701967104","article-title":"Monomeric G protein-coupled receptor rhodopsin in solution activates its G protein transducin at the diffusion limit","volume":"104","author":"Ernst","year":"2007","journal-title":"Proc. Natl. Acad. Sci. USA"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib49","doi-asserted-by":"crossref","first-page":"10733","DOI":"10.1021\/bi900544p","article-title":"Helix formation in arrestin accompanies recognition of photoactivated rhodopsin","volume":"48","author":"Feuerstein","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib50","doi-asserted-by":"crossref","first-page":"733","DOI":"10.1016\/S0896-6273(02)00822-X","article-title":"Mechanisms regulating variability of the single photon responses of mammalian rod photoreceptors","volume":"35","author":"Field","year":"2002","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib51","doi-asserted-by":"crossref","first-page":"491","DOI":"10.1146\/annurev.physiol.67.031103.151256","article-title":"Retinal processing near absolute threshold: from behavior to mechanism","volume":"67","author":"Field","year":"2005","journal-title":"Annu. Rev. Physiol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib52","doi-asserted-by":"crossref","first-page":"1296","DOI":"10.1124\/mol.108.053876","article-title":"Instability of a class a G protein-coupled receptor oligomer interface","volume":"75","author":"Fonseca","year":"2009","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib53","doi-asserted-by":"crossref","first-page":"252","DOI":"10.1016\/j.sbi.2006.03.013","article-title":"Structure of the rhodopsin dimer: a working model for G-protein-coupled receptors","volume":"16","author":"Fotiadis","year":"2006","journal-title":"Curr. Opin. Struct. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib54","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1038\/421127a","article-title":"Atomic-force microscopy: rhodopsin dimers in native disc membranes","volume":"421","author":"Fotiadis","year":"2003","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib55","doi-asserted-by":"crossref","first-page":"360","DOI":"10.1038\/ng0795-360","article-title":"A\u00a0homozygous 1-base pair deletion in the arrestin gene is a frequent cause of Oguchi disease in Japanese","volume":"10","author":"Fuchs","year":"1995","journal-title":"Nat. Genet."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib56","doi-asserted-by":"crossref","first-page":"152","DOI":"10.1073\/pnas.78.1.152","article-title":"Flow of information in the light-triggered cyclic nucleotide cascade of vision","volume":"78","author":"Fung","year":"1981","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib57","doi-asserted-by":"crossref","first-page":"25590","DOI":"10.1074\/jbc.M400363200","article-title":"Beta-arrestin-dependent constitutive internalization of the human chemokine decoy receptor D6","volume":"279","author":"Galliera","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib58","doi-asserted-by":"crossref","first-page":"49","DOI":"10.1093\/chemse\/bjj005","article-title":"A\u00a0Drosophila nonvisual arrestin is required for the maintenance of olfactory sensitivity","volume":"31","author":"Ge","year":"2006","journal-title":"Chem. Senses"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib59","doi-asserted-by":"crossref","first-page":"59","DOI":"10.1016\/j.ceb.2008.12.002","article-title":"Walking the walk: how kinesin and dynein coordinate their steps","volume":"21","author":"Gennerich","year":"2009","journal-title":"Curr. Opin. Cell Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib60","doi-asserted-by":"crossref","first-page":"5738","DOI":"10.1021\/bi991857f","article-title":"Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin","volume":"39","author":"Gibson","year":"2000","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib61","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1038\/383447a0","article-title":"Beta-arrestin acts as a clathrin adaptor in endocytosis of the beta2-adrenergic receptor","volume":"383","author":"Goodman","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib62","first-page":"1717","article-title":"Lateral diffusion of rhodopsin in photoreceptor membrane: a reappraisal","volume":"15","author":"Govardovskii","year":"2009","journal-title":"Mol. Vis."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib63","doi-asserted-by":"crossref","first-page":"918","DOI":"10.1038\/36147","article-title":"X-ray crystal structure of arrestin from bovine rod outer segments","volume":"391","author":"Granzin","year":"1998","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib64","doi-asserted-by":"crossref","first-page":"7058","DOI":"10.1021\/bi963110k","article-title":"Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation0independent fashion","volume":"36","author":"Gray-Keller","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib65","doi-asserted-by":"crossref","first-page":"3450","DOI":"10.1523\/JNEUROSCI.5391-09.2010","article-title":"Control of rhodopsin\u2019s active lifetime by arrestin-1 expression in mammalian rods","volume":"30","author":"Gross","year":"2010","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib66","doi-asserted-by":"crossref","first-page":"421","DOI":"10.1016\/S0306-4522(01)00511-5","article-title":"Arrestin2 and arrestin3 are differentially expressed in the rat brain during postnatal development","volume":"109","author":"Gurevich","year":"2002","journal-title":"Neuroscience"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib67","doi-asserted-by":"crossref","first-page":"1404","DOI":"10.1111\/j.1471-4159.2004.02830.x","article-title":"Arrestin2 expression selectively increases during neural differentiation","volume":"91","author":"Gurevich","year":"2004","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib68","doi-asserted-by":"crossref","first-page":"236","DOI":"10.1186\/gb-2006-7-9-236","article-title":"Arrestins are ubiquitous regulators of cellular signaling pathways","volume":"7","author":"Gurevich","year":"2006","journal-title":"Genome Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib69","doi-asserted-by":"crossref","unstructured":"Gurevich, E.V., Tesmer, J.J.G., Mushegian, A., Gurevich, E.V., G protein-coupled receptor kinases: more than just kinases and not only for GPCRs. Pharm. Ther., in press.","DOI":"10.1016\/j.pharmthera.2011.08.001"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib70","doi-asserted-by":"crossref","first-page":"15501","DOI":"10.1074\/jbc.273.25.15501","article-title":"The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanisms","volume":"273","author":"Gurevich","year":"1998","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib71","doi-asserted-by":"crossref","first-page":"21919","DOI":"10.1016\/S0021-9258(19)36700-6","article-title":"Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interaction","volume":"267","author":"Gurevich","year":"1992","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib72","doi-asserted-by":"crossref","first-page":"11628","DOI":"10.1016\/S0021-9258(19)50248-4","article-title":"Visual arrestin interaction with rhodopsin: sequential multisite binding ensures strict selectivity towards light-activated phosphorylated rhodopsin","volume":"268","author":"Gurevich","year":"1993","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib73","doi-asserted-by":"crossref","first-page":"6010","DOI":"10.1074\/jbc.270.11.6010","article-title":"Visual arrestin binding to rhodopsin: diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin","volume":"270","author":"Gurevich","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib74","doi-asserted-by":"crossref","first-page":"161","DOI":"10.1124\/mol.51.1.161","article-title":"Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding state","volume":"51","author":"Gurevich","year":"1997","journal-title":"Mol. Pharmacol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib75","doi-asserted-by":"crossref","first-page":"8721","DOI":"10.1016\/S0021-9258(17)37028-X","article-title":"Visual arrestin binding to rhodopsin: intramolecular interaction between the basic N-terminus and acidic C-terminus of arrestin may regulate binding selectivity","volume":"269","author":"Gurevich","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib76","doi-asserted-by":"crossref","first-page":"720","DOI":"10.1074\/jbc.270.2.720","article-title":"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","volume":"270","author":"Gurevich","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib77","doi-asserted-by":"crossref","first-page":"105","DOI":"10.1016\/j.tips.2003.12.008","article-title":"The molecular acrobatics of arrestin activation","volume":"25","author":"Gurevich","year":"2004","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib78","doi-asserted-by":"crossref","first-page":"465","DOI":"10.1016\/j.pharmthera.2005.09.008","article-title":"The structural basis of arrestin-mediated regulation of G protein-coupled receptors","volume":"110","author":"Gurevich","year":"2006","journal-title":"Pharm. Ther."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib79","doi-asserted-by":"crossref","first-page":"74","DOI":"10.1016\/j.tins.2007.11.007","article-title":"GPCR monomers and oligomers: it takes all kinds","volume":"31","author":"Gurevich","year":"2008","journal-title":"Trends Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib80","doi-asserted-by":"crossref","first-page":"234","DOI":"10.1016\/j.tips.2008.02.004","article-title":"How and why do GPCRs dimerize?","volume":"29","author":"Gurevich","year":"2008","journal-title":"Trends Pharmacol. Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib81","doi-asserted-by":"crossref","first-page":"e13","DOI":"10.1017\/S1462399410001444","article-title":"Custom-designed proteins as novel therapeutic tools? The case of arrestins","volume":"12","author":"Gurevich","year":"2010","journal-title":"Expert Rev. Mol. Med."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib82","doi-asserted-by":"crossref","first-page":"370","DOI":"10.1016\/B978-0-12-374203-2.00190-1","article-title":"Phototransduction: inactivation in cones","volume":"3","author":"Gurevich","year":"2010","journal-title":"Encyclopedia of the Eye"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib83","series-title":"Signal Transduction in the Retina","first-page":"55","article-title":"How rod arrestin achieved perfection: regulation of its availability and binding selectivity","author":"Gurevich","year":"2007"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib84","doi-asserted-by":"crossref","first-page":"28849","DOI":"10.1074\/jbc.272.46.28849","article-title":"Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity","volume":"272","author":"Gurevich","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib85","doi-asserted-by":"crossref","first-page":"16879","DOI":"10.1016\/S0021-9258(19)85275-4","article-title":"Binding of wild type and chimeric arrestins to the m2 muscarinic cholinergic receptor","volume":"268","author":"Gurevich","year":"1993","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib86","doi-asserted-by":"crossref","first-page":"4512","DOI":"10.1021\/bi00364a010","article-title":"Protein complement of rod outer segments of frog retina","volume":"25","author":"Hamm","year":"1986","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib87","doi-asserted-by":"crossref","first-page":"869","DOI":"10.1016\/S0969-2126(01)00644-X","article-title":"Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane translocation","volume":"9","author":"Han","year":"2001","journal-title":"Structure"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib88","doi-asserted-by":"crossref","unstructured":"Hanson, S.M., Cleghorn, W.M., Francis, D.J., Vishnivetskiy, S.A., Raman, D., Song, X., Nair, K.S., Slepak, V.Z., Klug, C.S., Gurevich, V.V., 2007. Arrestin mobilizes signaling proteins to the cytoskeleton and redirects their activity. J. Mol. Biol., 368, 375\u2013387.","DOI":"10.1016\/j.jmb.2007.02.053"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib89","doi-asserted-by":"crossref","first-page":"924","DOI":"10.1016\/j.str.2008.03.006","article-title":"A\u00a0model for the solution structure of the rod arrestin tetramer","volume":"16","author":"Hanson","year":"2008","journal-title":"Structure"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib90","doi-asserted-by":"crossref","first-page":"9765","DOI":"10.1074\/jbc.M510738200","article-title":"Visual arrestin binding to microtubules involves a distinct conformational change","volume":"281","author":"Hanson","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib91","doi-asserted-by":"crossref","first-page":"4900","DOI":"10.1073\/pnas.0600733103","article-title":"Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsin","volume":"103","author":"Hanson","year":"2006","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib92","doi-asserted-by":"crossref","first-page":"3125","DOI":"10.1073\/pnas.0610886104","article-title":"Each rhodopsin molecule binds its own arrestin","volume":"104","author":"Hanson","year":"2007","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib93","doi-asserted-by":"crossref","first-page":"3458","DOI":"10.1074\/jbc.M512148200","article-title":"The differential engagement of arrestin surface charges by the various functional forms of the receptor","volume":"281","author":"Hanson","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib94","doi-asserted-by":"crossref","first-page":"1726","DOI":"10.1038\/sj.emboj.7601614","article-title":"Structure and function of the visual arrestin oligomer","volume":"26","author":"Hanson","year":"2007","journal-title":"EMBO J."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib95","doi-asserted-by":"crossref","first-page":"1070","DOI":"10.1021\/bi7021359","article-title":"Opposing effects of inositol hexakisphosphate on rod arrestin and arrestin2 self-association","volume":"47","author":"Hanson","year":"2008","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib96","doi-asserted-by":"crossref","first-page":"2693","DOI":"10.1073\/pnas.0907915107","article-title":"Formation and dissociation of M1 muscarinic receptor dimers seen by total internal reflection fluorescence imaging of single molecules","volume":"107","author":"Hern","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib97","doi-asserted-by":"crossref","first-page":"593","DOI":"10.1111\/j.1469-7793.1999.0593v.x","article-title":"Sensitivity and kinetics of mouse rod flash responses determined in\u00a0vivo from paired-flash electroretinograms","volume":"516","author":"Hetling","year":"1999","journal-title":"J.\u00a0Physiol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib98","doi-asserted-by":"crossref","first-page":"257","DOI":"10.1016\/S0092-8674(00)80735-7","article-title":"The 2.8 A crystal structure of visual arrestin: a model for arrestin\u2019s regulation","volume":"97","author":"Hirsch","year":"1999","journal-title":"Cell"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib99","doi-asserted-by":"crossref","first-page":"9381","DOI":"10.1523\/JNEUROSCI.1207-10.2010","article-title":"Visual Arrestin 1 acts as a modulator for N-ethylmaleimide-sensitive factor in the photoreceptor synapse","volume":"30","author":"Huang","year":"2010","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib100","doi-asserted-by":"crossref","first-page":"243","DOI":"10.1016\/S0065-3233(03)63010-X","article-title":"Rhodopsin structure, dynamics, and activation: a perspective from crystallography, site-directed spin labeling, sulfhydryl reactivity, and disulfide cross-linking","volume":"63","author":"Hubbell","year":"2003","journal-title":"Adv. Protein Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib101","doi-asserted-by":"crossref","first-page":"1008","DOI":"10.1073\/pnas.87.3.1008","article-title":"Twenty Drosophila visual system cDNA clones: one is a homolog of human arrestin","volume":"87","author":"Hyde","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib102","doi-asserted-by":"crossref","first-page":"1186","DOI":"10.1016\/S0006-3495(03)74554-8","article-title":"Concentration-dependent tetramerization of bovine visual arrestin","volume":"85","author":"Imamoto","year":"2003","journal-title":"Biophys. J."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib103","doi-asserted-by":"crossref","first-page":"4880","DOI":"10.1074\/jbc.M409821200","article-title":"Phosphorylation-independent beta-arrestin translocation and internalization of leukotriene B4 receptors","volume":"280","author":"Jala","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib104","doi-asserted-by":"crossref","first-page":"463","DOI":"10.1083\/jcb.201009128","article-title":"Full characterization of GPCR monomer-dimer dynamic equilibrium by single molecule imaging","volume":"192","author":"Kasai","year":"2011","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib105","doi-asserted-by":"crossref","first-page":"2235","DOI":"10.1021\/bi1018607","article-title":"Robust self-association is a common feature of mammalian visual arrestin-1","volume":"50","author":"Kim","year":"2011","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib106","unstructured":"Kim, M., Vishnivetskiy, S.A., Van Eps, N., Zhan, X., Cleghorn, W.M., Alexander, N., Hanson, S.M., Meiler, J., Gurevich, V.V., Hubbell, W.L., 2011b. Conformation of receptor-bound arrestin-1: a site-directed spin labeling study. ASBMB meeting, 750, 759."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib107","doi-asserted-by":"crossref","first-page":"1518","DOI":"10.1001\/archopht.1993.01090110084030","article-title":"Dominant retinitis pigmentosa associated with two rhodopsin gene mutations. Leu-40-Arg and an insertion disrupting the 5\u2019-splice junction of exon 5","volume":"111","author":"Kim","year":"1993","journal-title":"Arch. Ophthalmol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib108","doi-asserted-by":"crossref","first-page":"139","DOI":"10.1016\/S0896-6273(00)00092-1","article-title":"A\u00a0molecular pathway for light-dependent photoreceptor apoptosis in Drosophila","volume":"28","author":"Kiselev","year":"2000","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib109","doi-asserted-by":"crossref","first-page":"16147","DOI":"10.1074\/jbc.270.27.16147","article-title":"Inhibition of rhodopsin kinase by recoverin. Further evidence for a negative feedback system in phototransduction","volume":"270","author":"Klenchin","year":"1995","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib110","doi-asserted-by":"crossref","first-page":"6831","DOI":"10.1074\/jbc.274.11.6831","article-title":"Targeted construction of phosphorylation-independent b-arrestin mutants with constitutive activity in cells","volume":"274","author":"Kovoor","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib111","doi-asserted-by":"crossref","first-page":"409","DOI":"10.1016\/j.neuron.2006.07.010","article-title":"RGS expression rate-limits recovery of rod photoresponses","volume":"51","author":"Krispel","year":"2006","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib112","doi-asserted-by":"crossref","first-page":"4389","DOI":"10.1021\/bi00614a006","article-title":"Light-regulated binding of rhodopsin kinase and other proteins to cattle photoreceptor membranes","volume":"17","author":"Kuhn","year":"1978","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib113","doi-asserted-by":"crossref","first-page":"473","DOI":"10.1016\/0014-5793(84)81221-1","article-title":"Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsin","volume":"176","author":"Kuhn","year":"1984","journal-title":"FEBS Lett."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib114","doi-asserted-by":"crossref","first-page":"pe12","DOI":"10.1126\/scisignal.3115pe12","article-title":"GPCR dimers fall apart","volume":"3","author":"Lambert","year":"2010","journal-title":"Sci. Signal."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib115","doi-asserted-by":"crossref","first-page":"311","DOI":"10.1038\/379311a0","article-title":"The 2.0 A crystal structure of a heterotrimeric G protein","volume":"379","author":"Lambright","year":"1996","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib116","doi-asserted-by":"crossref","first-page":"e17361","DOI":"10.1371\/journal.pone.0017361","article-title":"Internalization dissociates \u03b22-adrenergic receptors","volume":"6","author":"Lan","year":"2011","journal-title":"PLoS One"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib117","doi-asserted-by":"crossref","first-page":"3712","DOI":"10.1073\/pnas.96.7.3712","article-title":"The 2-adrenergic receptor\/arrestin complex recruits the clathrin adaptor AP-2 during endocytosis","volume":"96","author":"Laporte","year":"1999","journal-title":"Proc. Nat. Acad. Sci. USA"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib118","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/j.neuron.2004.06.014","article-title":"Light-dependent translocation of visual arrestin regulated by the NINAC myosin III","volume":"43","author":"Lee","year":"2004","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib119","doi-asserted-by":"crossref","first-page":"121","DOI":"10.1016\/S0896-6273(03)00390-8","article-title":"Light adaptation through phosphoinositide-regulated translocation of Drosophila visual arrestin","volume":"39","author":"Lee","year":"2003","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib120","doi-asserted-by":"crossref","DOI":"10.1073\/pnas.0402205101","article-title":"Rhodopsin kinase activity modulates the amplitude of the visual response in Drosophila","volume":"101","author":"Lee","year":"2004","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib121","doi-asserted-by":"crossref","first-page":"5818","DOI":"10.1073\/pnas.97.11.5818","article-title":"Scaffold proteins may biphasically affect the levels of mitogen-activated protein kinase signaling and reduce its threshold properties","volume":"97","author":"Levchenko","year":"2000","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib122","doi-asserted-by":"crossref","first-page":"1409","DOI":"10.1016\/j.jmb.2004.08.090","article-title":"Structure of bovine rhodopsin in a trigonal crystal form","volume":"343","author":"Li","year":"2004","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib123","doi-asserted-by":"crossref","first-page":"734","DOI":"10.1038\/287734a0","article-title":"ATP mediates rapid reversal of cyclic GMP phosphodiesterase activation in visual receptor membranes","volume":"287","author":"Liebman","year":"1980","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib124","doi-asserted-by":"crossref","first-page":"8599","DOI":"10.1073\/pnas.1002471107","article-title":"Flow of energy in the outer retina in darkness and in light","volume":"107","author":"Linton","year":"2010","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib125","doi-asserted-by":"crossref","first-page":"778","DOI":"10.1016\/j.neuron.2008.07.007","article-title":"Ca2+-dependent metarhodopsin inactivation mediated by calmodulin and NINAC myosin III","volume":"59","author":"Liu","year":"2008","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib126","doi-asserted-by":"crossref","first-page":"e1000099","DOI":"10.1371\/journal.pcbi.1000099","article-title":"Regulation of signal duration and the statistical dynamics of kinase activation by scaffold proteins","volume":"4","author":"Locasale","year":"2008","journal-title":"PLoS Comput. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib127","doi-asserted-by":"crossref","first-page":"8558","DOI":"10.1016\/S0021-9258(18)42479-9","article-title":"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","volume":"267","author":"Lohse","year":"1992","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib128","doi-asserted-by":"crossref","first-page":"1547","DOI":"10.1126\/science.2163110","article-title":"beta-Arrestin: a protein that regulates beta-adrenergic receptor function","volume":"248","author":"Lohse","year":"1990","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib129","doi-asserted-by":"crossref","first-page":"8715","DOI":"10.1073\/pnas.88.19.8715","article-title":"The receptor kinase family: primary structure of rhodopsin kinase reveals similarities to the beta-adrenergic receptor kinase","volume":"88","author":"Lorenz","year":"1991","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib130","doi-asserted-by":"crossref","first-page":"2449","DOI":"10.1073\/pnas.041604898","article-title":"Activation and targeting of extracellular signal-regulated kinases by beta-arrestin scaffolds","volume":"98","author":"Luttrell","year":"2001","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib131","doi-asserted-by":"crossref","first-page":"563","DOI":"10.1523\/JNEUROSCI.16-02-00563.1996","article-title":"Recovery phase of the murine rod photoresponse reconstructed from electroretinographic recordings","volume":"16","author":"Lyubarsky","year":"1996","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib132","doi-asserted-by":"crossref","first-page":"1574","DOI":"10.1126\/science.290.5496.1574","article-title":"Beta-arrestin 2: a receptor-regulated MAPK scaffold for the activation of JNK3","volume":"290","author":"McDonald","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib133","doi-asserted-by":"crossref","first-page":"10677","DOI":"10.1074\/jbc.274.16.10677","article-title":"Identification of NSF as a beta-arrestin1-binding protein. Implications for beta2-adrenergic receptor regulation","volume":"274","author":"McDonald","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib134","doi-asserted-by":"crossref","first-page":"290","DOI":"10.1002\/jnr.10120","article-title":"Cytoskeleton participation in subcellular trafficking of signal transduction proteins in rod photoreceptor cells","volume":"67","author":"McGinnis","year":"2002","journal-title":"J.\u00a0Neurosci. Res."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib135","doi-asserted-by":"crossref","first-page":"153","DOI":"10.1016\/S0896-6273(00)00093-3","article-title":"Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sites","volume":"28","author":"Mendez","year":"2000","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib136","doi-asserted-by":"crossref","first-page":"3124","DOI":"10.1523\/JNEUROSCI.23-08-03124.2003","article-title":"Light-dependent translocation of arrestin in the absence of rhodopsin phosphorylation and transducin signaling","volume":"23","author":"Mendez","year":"2003","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib137","doi-asserted-by":"crossref","first-page":"9812","DOI":"10.1074\/jbc.M512703200","article-title":"Nonvisual arrestin oligomerization and cellular localization are regulated by inositol hexakisphosphate binding","volume":"281","author":"Milano","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib138","doi-asserted-by":"crossref","first-page":"3321","DOI":"10.1021\/bi015905j","article-title":"Scaffolding functions of arrestin-2 revealed by crystal structure and mutagenesis","volume":"41","author":"Milano","year":"2002","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib139","doi-asserted-by":"crossref","first-page":"5","DOI":"10.1111\/j.1476-5381.2009.00169.x","article-title":"G\u00a0protein-coupled receptor hetero-dimerization: contribution to pharmacology and function","volume":"158","author":"Milligan","year":"2009","journal-title":"Br. J. Pharmacol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib140","doi-asserted-by":"crossref","first-page":"23","DOI":"10.1016\/j.coph.2009.09.010","article-title":"The role of dimerisation in the cellular trafficking of G-protein-coupled receptors","volume":"10","author":"Milligan","year":"2010","journal-title":"Curr. Opin. Pharmacol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib141","doi-asserted-by":"crossref","first-page":"17916","DOI":"10.1074\/jbc.M110479200","article-title":"Aspartic acid 564 in the third cytoplasmic loop of luteinizing hormone\/choriogonadotropin receptor is crucial for phosphorylation-independent interaction with arrestin2","volume":"277","author":"Mukherjee","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib142","doi-asserted-by":"crossref","first-page":"203","DOI":"10.1016\/0014-5793(93)81712-9","article-title":"X-arrestin: a new retinal arrestin mapping to the X chromosome","volume":"334","author":"Murakami","year":"1993","journal-title":"FEBS Lett."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib143","doi-asserted-by":"crossref","first-page":"41240","DOI":"10.1074\/jbc.M406768200","article-title":"Direct binding of visual arrestin to microtubules determines the differential subcellular localization of its splice variants in rod photoreceptors","volume":"279","author":"Nair","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib144","doi-asserted-by":"crossref","first-page":"555","DOI":"10.1016\/j.neuron.2005.03.023","article-title":"Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactions","volume":"46","author":"Nair","year":"2005","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib145","doi-asserted-by":"crossref","first-page":"5112","DOI":"10.1046\/j.1432-1033.2002.03240.x","article-title":"Ascidian arrestin (Ci-arr), the origin of the visual and nonvisual arrestins of vertebrate","volume":"269","author":"Nakagawa","year":"2002","journal-title":"Eur. J. Biochem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib146","doi-asserted-by":"crossref","first-page":"462","DOI":"10.1016\/j.neuron.2008.06.011","article-title":"Mouse cones require an arrestin for normal inactivation of phototransduction","volume":"59","author":"Nikonov","year":"2008","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib147","doi-asserted-by":"crossref","first-page":"343","DOI":"10.1177\/40.3.1372630","article-title":"S-antigen in rods and cones of the primate retina: different labeling patterns are revealed with antibodies directed against specific domains in the molecule","volume":"40","author":"Nir","year":"1992","journal-title":"J.\u00a0Histochem. Cytochem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib148","doi-asserted-by":"crossref","first-page":"307","DOI":"10.1006\/exer.1993.1129","article-title":"Ultrastructural analysis of arrestin distribution in mouse photoreceptors during dark\/light cycle","volume":"57","author":"Nir","year":"1993","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib149","doi-asserted-by":"crossref","first-page":"2428","DOI":"10.1002\/pro.5560031226","article-title":"Topographic study of arrestin using differential chemical modifications and hydrogen\/deuterium exchange","volume":"3","author":"Ohguro","year":"1994","journal-title":"Protein Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib150","doi-asserted-by":"crossref","first-page":"773","DOI":"10.1016\/0014-4835(91)90113-S","article-title":"Adaptive changes in visual cell transduction protein levels: effect of light","volume":"53","author":"Organisciak","year":"1991","journal-title":"Exp. Eye Res."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib151","doi-asserted-by":"crossref","first-page":"447","DOI":"10.1016\/j.cellsig.2009.10.016","article-title":"Light-dependent translocation of arrestin in rod photoreceptors is signaled through a phospholipase C cascade and requires ATP","volume":"22","author":"Orisme","year":"2010","journal-title":"Cell Signal."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib152","doi-asserted-by":"crossref","first-page":"15334","DOI":"10.1016\/S0021-9258(18)98620-5","article-title":"Role of the carboxyl-terminal region of arrestin in binding to phosphorylated rhodopsin","volume":"266","author":"Palczewski","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib153","doi-asserted-by":"crossref","first-page":"739","DOI":"10.1126\/science.289.5480.739","article-title":"Crystal structure of rhodopsin: a G protein-coupled receptor","volume":"289","author":"Palczewski","year":"2000","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib154","doi-asserted-by":"crossref","first-page":"15770","DOI":"10.1016\/S0021-9258(18)71543-3","article-title":"Regulation of rhodopsin dephosphorylation by arrestin","volume":"264","author":"Palczewski","year":"1989","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib155","doi-asserted-by":"crossref","first-page":"195","DOI":"10.1016\/0014-5793(91)81416-6","article-title":"Binding of inositol phosphates to arrestin","volume":"295","author":"Palczewski","year":"1991","journal-title":"FEBS Lett."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib156","doi-asserted-by":"crossref","first-page":"18649","DOI":"10.1016\/S0021-9258(18)55112-7","article-title":"Phosphorylated rhodopsin and heparin induce similar conformational changes in arrestin","volume":"266","author":"Palczewski","year":"1991","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib157","doi-asserted-by":"crossref","first-page":"15187","DOI":"10.1074\/jbc.M110.104612","article-title":"Arrestin and the multi-PDZ domain-containing protein MPZ-1 interact with phosphatase and tensin homolog (PTEN) and regulate Caenorhabditis elegans longevity","volume":"285","author":"Palmitessa","year":"2010","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib158","doi-asserted-by":"crossref","first-page":"24649","DOI":"10.1074\/jbc.M502637200","article-title":"Caenorhabditus elegans arrestin regulates neural G protein signaling and olfactory adaptation and recovery","volume":"280","author":"Palmitessa","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib159","doi-asserted-by":"crossref","first-page":"11623","DOI":"10.1074\/jbc.M209532200","article-title":"The nature of the arrestin x receptor complex determines the ultimate fate of the internalized receptor","volume":"278","author":"Pan","year":"2003","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib160","doi-asserted-by":"crossref","first-page":"183","DOI":"10.1038\/nature07063","article-title":"Crystal structure of the ligand-free G-protein-coupled receptor opsin","volume":"454","author":"Park","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib161","doi-asserted-by":"crossref","first-page":"3049","DOI":"10.1242\/jcs.01167","article-title":"Quantification of the cytoplasmic spaces of living cells with EGFP reveals arrestin-EGFP to be in disequilibrium in dark adapted rod photoreceptors","volume":"117","author":"Peet","year":"2004","journal-title":"J.\u00a0Cell Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib162","doi-asserted-by":"crossref","first-page":"73","DOI":"10.1017\/S0952523800008774","article-title":"Photoresponses of human rods in\u00a0vivo derived from paired-flash electroretinograms","volume":"14","author":"Pepperberg","year":"1997","journal-title":"Vis. Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib163","doi-asserted-by":"crossref","first-page":"9","DOI":"10.1017\/S0952523800006441","article-title":"Light-dependent delay in the falling phase of the retinal rod photoresponse","volume":"8","author":"Pepperberg","year":"1992","journal-title":"Vis. Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib164","doi-asserted-by":"crossref","first-page":"3988","DOI":"10.1167\/iovs.05-0567","article-title":"A\u00a0role for cytoskeletal elements in the light-driven translocation of proteins in rod photoreceptors","volume":"46","author":"Peterson","year":"2005","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib165","doi-asserted-by":"crossref","first-page":"891","DOI":"10.1126\/science.2988124","article-title":"Retinal S antigen identified as the 48K protein regulating light-dependent phosphodiesterase in rods","volume":"228","author":"Pfister","year":"1985","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib166","first-page":"261","article-title":"Identification of the so-called 48 K protein that interacts with illuminated rhodopsin in retinal rods, and the retinal S antigen, inductor of experimental autoimmune uveoretinitis","volume":"299","author":"Pfister","year":"1984","journal-title":"C\u00a0R Acad Sci. III"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib167","doi-asserted-by":"crossref","first-page":"127","DOI":"10.1016\/0014-5793(87)81144-4","article-title":"Light-stimulated protein movement in rod photoreceptor cells of the rat retina","volume":"225","author":"Philp","year":"1987","journal-title":"FEBS Lett."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib168","doi-asserted-by":"crossref","first-page":"26969","DOI":"10.1016\/S0021-9258(18)47113-X","article-title":"Mechanism of arrestin 2 function in rhabdomeric photoreceptors","volume":"269","author":"Plangger","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib169","series-title":"Handbook of Biological Physics. Molecular Mechanisms in Visual Transduction","first-page":"183","article-title":"Phototransduction in vertebrate rods and cones: molecular mechanisms of amplification, recovery and light adaptation","author":"Pugh","year":"2000"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib170","doi-asserted-by":"crossref","first-page":"185","DOI":"10.1016\/0014-5793(95)00225-X","article-title":"Synthetic phosphopeptide from rhodopsin sequence induces retinal arrestin binding to photoactivated unphosphorylated rhodopsin","volume":"362","author":"Puig","year":"1995","journal-title":"FEBS Lett."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib171","doi-asserted-by":"crossref","first-page":"9253","DOI":"10.1021\/bi970772g","article-title":"Functional differences in the interaction of arrestin and its splice variant, p44, with rhodopsin","volume":"36","author":"Pulvermuller","year":"1997","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib172","doi-asserted-by":"crossref","first-page":"37679","DOI":"10.1074\/jbc.M006776200","article-title":"Interactions of metarhodopsin II. Arrestin peptides compete with arrestin and transducin","volume":"275","author":"Pulvermuller","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib173","doi-asserted-by":"crossref","first-page":"5563","DOI":"10.1021\/bi9000062","article-title":"Growth factor receptor-bound protein 14 undergoes light-dependent intracellular translocation in rod photoreceptors: functional role in retinal insulin receptor activation","volume":"48","author":"Rajala","year":"2009","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib174","doi-asserted-by":"crossref","first-page":"785","DOI":"10.1002\/cm.20300","article-title":"The translocation of signaling molecules in dark adapting mammalian rod photoreceptor cells is dependent on the cytoskeleton","volume":"65","author":"Reidel","year":"2008","journal-title":"Cell Motil. Cytoskeleton"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib175","doi-asserted-by":"crossref","first-page":"207","DOI":"10.1093\/hmg\/2.2.207","article-title":"A\u00a0large deletion at the 3\u2019 end of the rhodopsin gene in an Italian family with a diffuse form of autosomal dominant retinitis pigmentosa","volume":"2","author":"Restagno","year":"1993","journal-title":"Hum. Mol. Genet."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib176","doi-asserted-by":"crossref","first-page":"1836","DOI":"10.1016\/S0006-3495(98)77625-8","article-title":"Origin of reproducibility in the responses of retinal rods to single photons","volume":"75","author":"Rieke","year":"1998","journal-title":"Biophys. J."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib177","doi-asserted-by":"crossref","first-page":"1281","DOI":"10.1093\/genetics\/155.3.1281","article-title":"kurtz, a novel nonvisual arrestin, is an essential neural gene in Drosophila","volume":"155","author":"Roman","year":"2000","journal-title":"Genetics"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib178","doi-asserted-by":"crossref","first-page":"845","DOI":"10.1126\/science.3136548","article-title":"Expression of transducin in retinal rod photoreceptor outer segments","volume":"241","author":"Roof","year":"1988","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib179","doi-asserted-by":"crossref","first-page":"487","DOI":"10.1083\/jcb.95.2.487","article-title":"Surfaces of rod photoreceptor disk membranes: integral membrane components","volume":"95","author":"Roof","year":"1982","journal-title":"J.\u00a0Cell Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib180","doi-asserted-by":"crossref","first-page":"5484","DOI":"10.1523\/JNEUROSCI.1421-07.2007","article-title":"Subunit dissociation and diffusion determine the subcellular localization of rod and cone transducins","volume":"27","author":"Rosenzweig","year":"2007","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib181","doi-asserted-by":"crossref","first-page":"915","DOI":"10.1089\/hum.2010.041","article-title":"Ocular gene therapy: an evaluation of recombinant adeno-associated virus-mediated gene therapy interventions for the treatment of ocular disease","volume":"21","author":"Roy","year":"2010","journal-title":"Hum. Gene Ther."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib182","doi-asserted-by":"crossref","first-page":"1722","DOI":"10.1016\/j.cub.2005.08.064","article-title":"Arrestin1 mediates light-dependent rhodopsin endocytosis and cell survival","volume":"15","author":"Satoh","year":"2005","journal-title":"Curr. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib183","doi-asserted-by":"crossref","first-page":"997","DOI":"10.1016\/j.neuron.2010.08.024","article-title":"Arrestin translocation is stoichiometric to rhodopsin isomerization and accelerated by phototransduction in Drosophila photoreceptors","volume":"67","author":"Satoh","year":"2010","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib184","doi-asserted-by":"crossref","first-page":"497","DOI":"10.1038\/nature07330","article-title":"Crystal structure of opsin in its G-protein-interacting conformation","volume":"455","author":"Scheerer","year":"2008","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib185","doi-asserted-by":"crossref","first-page":"1770","DOI":"10.1021\/bi00430a052","article-title":"Kinetics, binding constant, and activation energy of the 48-kDa protein-rhodopsin complex by extra-metarhodopsin II","volume":"28","author":"Schleicher","year":"1989","journal-title":"Biochemistry"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib186","doi-asserted-by":"crossref","first-page":"173","DOI":"10.1016\/j.pharmthera.2004.08.008","article-title":"Mutant G-protein-coupled receptors as a cause of human diseases","volume":"104","author":"Sch\u00f6neberg","year":"2004","journal-title":"Pharmacol. Ther."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib187","doi-asserted-by":"crossref","first-page":"21186","DOI":"10.1074\/jbc.274.30.21186","article-title":"Visual arrestin activity may be regulated by self-association","volume":"274","author":"Schubert","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib188","doi-asserted-by":"crossref","unstructured":"Seo, J., Tsakem, E.L., Breitman, M., Gurevich, V.V., Identification of arrestin-3-specific residues necessary for JNK3 kinase activation, 2011. J. Biol. Chem. 286, in press.","DOI":"10.1074\/jbc.M111.260448"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib189","doi-asserted-by":"crossref","first-page":"12","DOI":"10.1049\/iet-syb.2008.0154","article-title":"Dynamics of mouse rod phototransduction and its sensitivity to variation of key parameters","volume":"4","author":"Shen","year":"2010","journal-title":"IET Syst. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib190","doi-asserted-by":"crossref","first-page":"1307","DOI":"10.1126\/science.1063866","article-title":"Regulation of receptor fate by ubiquitination of activated beta 2-adrenergic receptor and beta-arrestin","volume":"294","author":"Shenoy","year":"2001","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib191","doi-asserted-by":"crossref","first-page":"10084","DOI":"10.1523\/JNEUROSCI.2211-07.2007","article-title":"Signaling properties of a short-wave cone visual pigment and its role in phototransduction","volume":"27","author":"Shi","year":"2007","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib192","doi-asserted-by":"crossref","first-page":"41184","DOI":"10.1074\/jbc.M506935200","article-title":"Light causes phosphorylation of nonactivated visual pigments in intact mouse rod photoreceptor cells","volume":"280","author":"Shi","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib193","doi-asserted-by":"crossref","first-page":"7040","DOI":"10.1016\/S0021-9258(17)38026-2","article-title":"Light-dependent phosphorylation of rhodopsin. Purification and properties of rhodopsin kinase","volume":"253","author":"Shichi","year":"1978","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib194","doi-asserted-by":"crossref","first-page":"14053","DOI":"10.1074\/jbc.M708974200","article-title":"Structures of rhodopsin kinase in different ligand states reveal key elements involved in G protein-coupled receptor kinase activation","volume":"283","author":"Singh","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib195","doi-asserted-by":"crossref","first-page":"2","DOI":"10.1002\/iub.7","article-title":"Mechanism of light-induced translocation of arrestin and transducin in photoreceptors: interaction-restricted diffusion","volume":"60","author":"Slepak","year":"2008","journal-title":"IUBMB Life"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib196","doi-asserted-by":"crossref","first-page":"156","DOI":"10.1016\/j.tig.2009.02.003","article-title":"Prospects for retinal gene replacement therapy","volume":"25","author":"Smith","year":"2009","journal-title":"Trends Genet."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib197","doi-asserted-by":"crossref","first-page":"1003","DOI":"10.1073\/pnas.87.3.1003","article-title":"Isolation and structure of an arrestin gene from Drosophila","volume":"87","author":"Smith","year":"1990","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib198","doi-asserted-by":"crossref","first-page":"1832","DOI":"10.1167\/iovs.10-5724","article-title":"Interaction of arrestin with enolase1 in photoreceptors","volume":"52","author":"Smith","year":"2011","journal-title":"Invest. Ophthalmol. Vis. Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib199","doi-asserted-by":"crossref","first-page":"15407","DOI":"10.1016\/S0021-9258(17)40691-0","article-title":"A\u00a0splice variant of arrestin. Molecular cloning and localization in bovine retina","volume":"269","author":"Smith","year":"1994","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib200","doi-asserted-by":"crossref","first-page":"95","DOI":"10.1016\/S0896-6273(02)00636-0","article-title":"Massive light-driven translocation of transducin between the two major compartments of rod cells: a novel mechanism of light adaptation","volume":"34","author":"Sokolov","year":"2002","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib201","doi-asserted-by":"crossref","first-page":"19149","DOI":"10.1074\/jbc.M311058200","article-title":"Phosducin facilitates light-driven transducin translocation in rod photoreceptors. Evidence from the phosducin knockout mouse","volume":"279","author":"Sokolov","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib202","doi-asserted-by":"crossref","first-page":"25560","DOI":"10.1074\/jbc.M702155200","article-title":"Dynamics of arrestin-rhodopsin interactions: loop movement is involved in arrestin activation and receptor binding","volume":"282","author":"Sommer","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib203","doi-asserted-by":"crossref","first-page":"7359","DOI":"10.1074\/jbc.M110.204941","article-title":"Arrestin-rhodopsin binding stoichiometry in isolated rod outer segment membranes depends on the percentage of activated receptors","volume":"286","author":"Sommer","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib204","doi-asserted-by":"crossref","first-page":"685","DOI":"10.1074\/jbc.M806124200","article-title":"How does arrestin assemble MAPKs into a signaling complex?","volume":"284","author":"Song","year":"2009","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib205","doi-asserted-by":"crossref","first-page":"1053","DOI":"10.1111\/j.1471-4159.2007.04842.x","article-title":"Cone arrestin binding to JNK3 and Mdm2: conformational preference and localization of interaction sites","volume":"103","author":"Song","year":"2007","journal-title":"J.\u00a0Neurochem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib206","doi-asserted-by":"crossref","first-page":"21491","DOI":"10.1074\/jbc.M603659200","article-title":"Visual and both non-visual arrestins in their \u201cinactive\u201d conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasm","volume":"281","author":"Song","year":"2006","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib207","doi-asserted-by":"crossref","first-page":"700","DOI":"10.1016\/j.cub.2009.02.065","article-title":"Enhanced arrestin facilitates recovery and Protects rod photoreceptors deficient in rhodopsin phosphorylation","volume":"19","author":"Song","year":"2009","journal-title":"Curr. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib208","doi-asserted-by":"crossref","first-page":"37","DOI":"10.1016\/j.neuroscience.2010.11.009","article-title":"Arrestin-1 expression in rods: balancing functional performance and photoreceptor health","volume":"174","author":"Song","year":"2011","journal-title":"Neuroscience"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib209","doi-asserted-by":"crossref","first-page":"656","DOI":"10.1038\/nature09795","article-title":"The structural basis of agonist-induced activation in constitutively active rhodopsin","volume":"471","author":"Standfuss","year":"2011","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib210","doi-asserted-by":"crossref","first-page":"58","DOI":"10.1016\/j.brainres.2007.10.083","article-title":"The locations of mitochondria in mammalian photoreceptors: relation to retinal vasculature","volume":"1189","author":"Stone","year":"2008","journal-title":"Brain Res."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib211","doi-asserted-by":"crossref","first-page":"40210","DOI":"10.1074\/jbc.M508001200","article-title":"Homo- and hetero-oligomerization of beta-arrestins in living cells","volume":"280","author":"Storez","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib212","doi-asserted-by":"crossref","first-page":"29250","DOI":"10.1074\/jbc.M501789200","article-title":"Recoverin undergoes light-dependent intracellular translocation in rod photoreceptors","volume":"280","author":"Strissel","year":"2005","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib213","doi-asserted-by":"crossref","first-page":"1146","DOI":"10.1523\/JNEUROSCI.4289-05.2006","article-title":"Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsin","volume":"26","author":"Strissel","year":"2006","journal-title":"J.\u00a0Neurosci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib214","doi-asserted-by":"crossref","first-page":"1069","DOI":"10.1016\/j.jmb.2005.10.023","article-title":"Crystal structure of cone arrestin at 2.3\u00c5: evolution of receptor specificity","volume":"354","author":"Sutton","year":"2005","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib215","doi-asserted-by":"crossref","first-page":"501","DOI":"10.1016\/j.jmb.2010.04.029","article-title":"Monomeric rhodopsin is the Minimal functional unit required for arrestin binding","volume":"399","author":"Tsukamoto","year":"2010","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib216","doi-asserted-by":"crossref","first-page":"687","DOI":"10.1126\/science.277.5326.687","article-title":"A\u00a0G protein-coupled receptor phosphatase required for rhodopsin function","volume":"277","author":"Vin\u00f3s","year":"1997","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib217","doi-asserted-by":"crossref","first-page":"42","DOI":"10.1016\/j.jmb.2009.10.058","article-title":"The role of arrestin alpha-helix I in receptor binding","volume":"395","author":"Vishnivetskiy","year":"2010","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib218","doi-asserted-by":"crossref","first-page":"24288","DOI":"10.1074\/jbc.M110.213835","article-title":"Few residues within an extensive binding interface drive receptor interaction and determine the specificity of arrestin proteins","volume":"286","author":"Vishnivetskiy","year":"2011","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib219","doi-asserted-by":"crossref","first-page":"43961","DOI":"10.1074\/jbc.M206951200","article-title":"Transition of arrestin in the active receptor-binding state requires an extended interdomain hinge","volume":"277","author":"Vishnivetskiy","year":"2002","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib220","doi-asserted-by":"crossref","first-page":"1262","DOI":"10.1074\/jbc.M308834200","article-title":"Mapping the arrestin-receptor interface: structural elements responsible for receptor specificity of arrestin proteins","volume":"279","author":"Vishnivetskiy","year":"2004","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib221","doi-asserted-by":"crossref","first-page":"11451","DOI":"10.1074\/jbc.274.17.11451","article-title":"How does arrestin respond to the phosphorylated state of rhodopsin?","volume":"274","author":"Vishnivetskiy","year":"1999","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib222","doi-asserted-by":"crossref","first-page":"32075","DOI":"10.1074\/jbc.M706057200","article-title":"Regulation of arrestin binding by rhodopsin phosphorylation level","volume":"282","author":"Vishnivetskiy","year":"2007","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib223","doi-asserted-by":"crossref","first-page":"41049","DOI":"10.1074\/jbc.M007159200","article-title":"An additional phosphate-binding element in arrestin molecule: implications for the mechanism of arrestin activation","volume":"275","author":"Vishnivetskiy","year":"2000","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib224","doi-asserted-by":"crossref","first-page":"1949","DOI":"10.4049\/jimmunol.119.6.1949","article-title":"Experimental allergic uveitis. Isolation, characterization, and localization of a soluble uveitopathogenic antigen from bovine retina","volume":"119","author":"Wacker","year":"1977","journal-title":"J.\u00a0Immunol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib225","doi-asserted-by":"crossref","first-page":"30015","DOI":"10.1074\/jbc.M803953200","article-title":"Activation-dependent hindrance of photoreceptor G protein diffusion by lipid microdomains","volume":"283","author":"Wang","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib226","first-page":"27","article-title":"The cloning of GRK7, a candidate cone opsin kinase, from cone- and rod-dominant mammalian retinas","volume":"4","author":"Weiss","year":"1998","journal-title":"Mol. Vis."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib227","doi-asserted-by":"crossref","first-page":"381","DOI":"10.1073\/pnas.72.1.381","article-title":"Light-stimulated phosphorylation of rhodopsin in the retina: the presence of a protein kinase that is specific for photobleached rhodopsin","volume":"72","author":"Weller","year":"1975","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib228","doi-asserted-by":"crossref","first-page":"939","DOI":"10.1016\/j.bpj.2008.10.016","article-title":"Overexpression of rhodopsin alters the structure and photoresponse of rod photoreceptors","volume":"96","author":"Wen","year":"2009","journal-title":"Biophys. J."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib229","doi-asserted-by":"crossref","first-page":"263","DOI":"10.1002\/jnr.490200216","article-title":"Light-dependent subcellular movement of photoreceptor proteins","volume":"20","author":"Whelan","year":"1988","journal-title":"J.\u00a0Neurosci. Res."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib230","doi-asserted-by":"crossref","first-page":"12199","DOI":"10.1073\/pnas.0705312104","article-title":"Dimerization of the class A G protein-coupled neurotension receptor NTS1 alters G protein interaction","volume":"104","author":"White","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib231","doi-asserted-by":"crossref","first-page":"337","DOI":"10.1016\/S0896-6273(00)80784-9","article-title":"Variability in the time course of single photon responses from toad rods: termination of rhodopsin\u2019s activity","volume":"23","author":"Whitlock","year":"1999","journal-title":"Neuron"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib232","doi-asserted-by":"crossref","first-page":"7682","DOI":"10.1073\/pnas.0611448104","article-title":"A\u00a0monomeric G protein-coupled receptor isolated in a high-density lipoprotein particle efficiently activates its G protein","volume":"104","author":"Whorton","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U.S.A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib233","doi-asserted-by":"crossref","first-page":"4387","DOI":"10.1074\/jbc.M703346200","article-title":"Efficient coupling of transducin to monomeric rhodopsin in a phospholipid bilayer","volume":"283","author":"Whorton","year":"2008","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib234","doi-asserted-by":"crossref","first-page":"1174","DOI":"10.1073\/pnas.83.5.1174","article-title":"Phosphodiesterase activation by photoexcited rhodopsin is quenched when rhodopsin is phosphorylated and binds the intrinsic 48-kDa protein of rod outer segments","volume":"83","author":"Wilden","year":"1986","journal-title":"Proc. Natl. Acad. Sci."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib235","doi-asserted-by":"crossref","first-page":"955","DOI":"10.1016\/j.jmb.2006.09.075","article-title":"Arrestin binding to calmodulin: a direct interaction between two ubiquitous signaling proteins","volume":"364","author":"Wu","year":"2006","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib236","doi-asserted-by":"crossref","first-page":"12011","DOI":"10.1073\/pnas.0704849104","article-title":"Functional specialization of beta-arrestin interactions revealed by proteomic analysis","volume":"104","author":"Xiao","year":"2007","journal-title":"Proc. Natl. Acad. Sci. U S A"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib237","doi-asserted-by":"crossref","first-page":"505","DOI":"10.1038\/39068","article-title":"Prolonged photoresponses in transgenic mouse rods lacking arrestin","volume":"389","author":"Xu","year":"1997","journal-title":"Nature"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib238","doi-asserted-by":"crossref","first-page":"483","DOI":"10.1126\/science.2158671","article-title":"A\u00a049-kilodalton phosphoprotein in the Drosophila photoreceptor is an arrestin homolog","volume":"248","author":"Yamada","year":"1990","journal-title":"Science"},{"key":"10.1016\/j.preteyeres.2011.07.002_bib239","doi-asserted-by":"crossref","first-page":"175","DOI":"10.1038\/ng0297-175","article-title":"Defects in the rhodopsin kinase gene in the Oguchi form of stationary night blindness","volume":"15","author":"Yamamoto","year":"1997","journal-title":"Nat. Genet."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib240","doi-asserted-by":"crossref","first-page":"467","DOI":"10.1016\/j.jmb.2010.12.034","article-title":"Crystal structure of arrestin-3 reveals the basis of the difference in receptor binding between two non-visual arrestins","volume":"406","author":"Zhan","year":"2011","journal-title":"J.\u00a0Mol. Biol."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib241","doi-asserted-by":"crossref","first-page":"14762","DOI":"10.1074\/jbc.272.23.14762","article-title":"Rhodopsin phosphorylation sites and their role in arrestin binding","volume":"272","author":"Zhang","year":"1997","journal-title":"J.\u00a0Biol. Chem."},{"key":"10.1016\/j.preteyeres.2011.07.002_bib242","doi-asserted-by":"crossref","first-page":"10473","DOI":"10.1021\/bi101596g","article-title":"Elucidation of IP6 and heparin interaction sites and conformational changes in arrestin-1 by solution NMR","author":"Zhuang","year":"2010","journal-title":"Biochemistry"}],"container-title":["Progress in Retinal and Eye Research"],"original-title":[],"language":"en","link":[{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1350946211000528?httpAccept=text\/xml","content-type":"text\/xml","content-version":"vor","intended-application":"text-mining"},{"URL":"https:\/\/api.elsevier.com\/content\/article\/PII:S1350946211000528?httpAccept=text\/plain","content-type":"text\/plain","content-version":"vor","intended-application":"text-mining"}],"deposited":{"date-parts":[[2024,4,9]],"date-time":"2024-04-09T13:48:38Z","timestamp":1712670518000},"score":1,"resource":{"primary":{"URL":"https:\/\/linkinghub.elsevier.com\/retrieve\/pii\/S1350946211000528"}},"subtitle":[],"short-title":[],"issued":{"date-parts":[[2011,11]]},"references-count":242,"journal-issue":{"issue":"6","published-print":{"date-parts":[[2011,11]]}},"alternative-id":["S1350946211000528"],"URL":"https:\/\/doi.org\/10.1016\/j.preteyeres.2011.07.002","relation":{},"ISSN":["1350-9462"],"issn-type":[{"value":"1350-9462","type":"print"}],"subject":[],"published":{"date-parts":[[2011,11]]}}}