Regulation of arrestin binding by rhodopsin phosphorylation level

scientific article published on 11 September 2007

Regulation of arrestin binding by rhodopsin phosphorylation level is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1074/JBC.M706057200
P932PMC publication ID2638115
P698PubMed publication ID17848565
P5875ResearchGate publication ID5991104

P50authorVsevolod V. GurevichQ42173663
P2093author name stringMatthew J Kennedy
Dayanidhi Raman
Sergey A Vishnivetskiy
James B Hurley
Junhua Wei
P2860cites workArrestins: ubiquitous regulators of cellular signaling pathwaysQ21184142
Regulation of rhodopsin dephosphorylation by arrestinQ24309628
Molecular tinkering of G protein-coupled receptors: an evolutionary successQ24534016
Structural and functional impairment of endocytic pathways by retinitis pigmentosa mutant rhodopsin-arrestin complexesQ24563320
The structural basis of arrestin-mediated regulation of G-protein-coupled receptorsQ24657537
The 2.8 A crystal structure of visual arrestin: a model for arrestin's regulationQ27618047
Crystal structure of beta-arrestin at 1.9 A: possible mechanism of receptor binding and membrane TranslocationQ27634946
Transduction of receptor signals by beta-arrestinsQ28246395
Functional antagonism of different G protein-coupled receptor kinases for beta-arrestin-mediated angiotensin II receptor signalingQ33819399
Different G protein-coupled receptor kinases govern G protein and beta-arrestin-mediated signaling of V2 vasopressin receptorQ33819496
Structure and function in rhodopsin: asymmetric reconstitution of rhodopsin in liposomesQ34159475
Origin of reproducibility in the responses of retinal rods to single photonsQ34169073
Constitutive activation of phototransduction by K296E opsin is not a cause of photoreceptor degenerationQ34453852
Possible involvement of the endocannabinoid system in the actions of three clinically used drugs.Q34547367
Stable rhodopsin/arrestin complex leads to retinal degeneration in a transgenic mouse model of autosomal dominant retinitis pigmentosa.Q34581973
Differential interaction of spin-labeled arrestin with inactive and active phosphorhodopsinQ34596638
Toward a unified model of vertebrate rod phototransductionQ34693762
The new face of active receptor bound arrestin attracts new partnersQ35214608
Each rhodopsin molecule binds its own arrestinQ35652316
Determinants of single photon response variabilityQ36411526
Mass spectrometric analysis of the kinetics of in vivo rhodopsin phosphorylationQ36639195
Visual and both non-visual arrestins in their "inactive" conformation bind JNK3 and Mdm2 and relocalize them from the nucleus to the cytoplasmQ36726881
Mechanism of phosphorylation-recognition by visual arrestin and the transition of arrestin into a high affinity binding stateQ73030745
Use of bacteriophage RNA polymerase in RNA synthesisQ73053443
An additional phosphate-binding element in arrestin molecule. Implications for the mechanism of arrestin activationQ73054341
Arrestin with a single amino acid substitution quenches light-activated rhodopsin in a phosphorylation-independent fashionQ73427926
Isolation of isoelectric species of phosphorylated rhodopsinQ73591603
Arrestin: mutagenesis, expression, purification, and functional characterizationQ73591654
Visual arrestin activity may be regulated by self-associationQ78010480
Multiple phosphorylation sites confer reproducibility of the rod's single-photon responsesQ80011647
Arrestin translocation is induced at a critical threshold of visual signaling and is superstoichiometric to bleached rhodopsinQ82372903
The differential engagement of arrestin surface charges by the various functional forms of the receptorQ36737719
Light-dependent redistribution of arrestin in vertebrate rods is an energy-independent process governed by protein-protein interactionsQ37365027
Structure and function of the visual arrestin oligomerQ38304145
Concentration-dependent tetramerization of bovine visual arrestinQ40248090
Mapping the arrestin-receptor interface. Structural elements responsible for receptor specificity of arrestin proteinsQ40628650
The nature of the arrestin x receptor complex determines the ultimate fate of the internalized receptorQ40678127
Agonist-receptor-arrestin, an alternative ternary complex with high agonist affinity.Q41079862
Mechanism of quenching of phototransduction. Binding competition between arrestin and transducin for phosphorhodopsin.Q41099124
Constitutive activation of opsin: interaction of mutants with rhodopsin kinase and arrestinQ41294623
How does arrestin respond to the phosphorylated state of rhodopsin?Q42470664
Visual arrestin interaction with rhodopsin. Sequential multisite binding ensures strict selectivity toward light-activated phosphorylated rhodopsin.Q42623057
Multiple phosphorylation of rhodopsin and the in vivo chemistry underlying rod photoreceptor dark adaptationQ43702730
Transition of arrestin into the active receptor-binding state requires an extended interdomain hingeQ44127981
N-formyl peptide receptor phosphorylation domains differentially regulate arrestin and agonist affinityQ44211079
Light induced shift and binding of S-antigen in retinal rodsQ44722936
Visual pigment phosphorylation but not transducin translocation can contribute to light adaptation in zebrafish conesQ44815991
Rhodopsin phosphorylation in rats exposed to intense lightQ45123488
Dynamics of arrestin-rhodopsin interactions: arrestin and retinal release are directly linked eventsQ45182666
Light dependent phosphorylation of rhodopsin by ATP.Q46123273
Light causes phosphorylation of nonactivated visual pigments in intact mouse rod photoreceptor cellsQ46137947
RGS expression rate-limits recovery of rod photoresponsesQ46175317
Rapid and reproducible deactivation of rhodopsin requires multiple phosphorylation sitesQ46690154
Crystal structure of cone arrestin at 2.3A: evolution of receptor specificity.Q46804865
G-protein-coupled receptors: turn-ons and turn-offsQ47754228
The selectivity of visual arrestin for light-activated phosphorhodopsin is controlled by multiple nonredundant mechanismsQ47982269
Conservation of the phosphate-sensitive elements in the arrestin family of proteinsQ48871433
Targeted construction of phosphorylation-independent beta-arrestin mutants with constitutive activity in cellsQ48922901
Arrestin interactions with G protein-coupled receptors. Direct binding studies of wild type and mutant arrestins with rhodopsin, beta 2-adrenergic, and m2 muscarinic cholinergic receptorsQ50337370
Phosphorylation modulates the affinity of light-activated rhodopsin for G protein and arrestin.Q52078908
Variability in the time course of single photon responses from toad rods: termination of rhodopsin's activity.Q52209745
The formation of stable rhodopsin-arrestin complexes induces apoptosis and photoreceptor cell degeneration.Q52584172
A molecular pathway for light-dependent photoreceptor apoptosis in Drosophila.Q52584174
Visual arrestin binding to rhodopsin. Diverse functional roles of positively charged residues within the phosphorylation-recognition region of arrestin.Q54266642
The role of arrestin and retinoids in the regeneration pathway of rhodopsinQ67901125
Cell-free expression of visual arrestin. Truncation mutagenesis identifies multiple domains involved in rhodopsin interactionQ67907347
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 illuminationQ68905392
Differential immunogold-dextran labeling of bovine and frog rod and cone cells using monoclonal antibodies against bovine rhodopsinQ68957656
Phosphorylation of frog photoreceptor membranes induced by lightQ68997021
Mechanism of rhodopsin kinase activationQ70231775
Light-induced binding of 48-kDa protein to photoreceptor membranes is highly enhanced by phosphorylation of rhodopsinQ70501789
Phosphorylation of non-bleached rhodopsin in intact retinas and living frogsQ71245930
Light-dependent phosphorylation of rhodopsin: number of phosphorylation sitesQ72111974
Rhodopsin phosphorylation and dephosphorylation in vivoQ72315710
Duration and amplitude of the light-induced cGMP hydrolysis in vertebrate photoreceptors are regulated by multiple phosphorylation of rhodopsin and by arrestin bindingQ72422681
Control of rhodopsin multiple phosphorylationQ72767084
P433issue44
P407language of work or nameEnglishQ1860
P921main subjectphosphorylationQ242736
P1104number of pages9
P304page(s)32075-32083
P577publication date2007-09-11
P1433published inJournal of Biological ChemistryQ867727
P1476titleRegulation of arrestin binding by rhodopsin phosphorylation level
P478volume282

Reverse relations

cites work (P2860)
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