Arrestin Allows All-Trans-Retinal to Enter the Ligand Binding Pocket of Phosphorylated Opsin
نویسندگان
چکیده
منابع مشابه
Functional map of arrestin binding to phosphorylated opsin, with and without agonist
Arrestins desensitize G protein-coupled receptors (GPCRs) and act as mediators of signalling. Here we investigated the interactions of arrestin-1 with two functionally distinct forms of the dim-light photoreceptor rhodopsin. Using unbiased scanning mutagenesis we probed the individual contribution of each arrestin residue to the interaction with the phosphorylated apo-receptor (Ops-P) and the a...
متن کاملCorrigendum: Functional map of arrestin binding to phosphorylated opsin, with and without agonist
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متن کاملErratum: Distinct loops in arrestin differentially regulate ligand binding within the GPCR opsin
G-protein-coupled receptors are universally regulated by arrestin binding. Here we show that rod arrestin induces uptake of the agonist all-trans-retinal [corrected] in only half the population of phosphorylated opsin in the native membrane. Agonist uptake blocks subsequent entry of the inverse agonist 11-cis-retinal (that is, regeneration of rhodopsin), but regeneration is not blocked in the o...
متن کاملA rhodopsin exhibiting binding ability to agonist all-trans-retinal.
Rhodopsins are the members of the family of G protein-coupled receptors that have diverged from ligand-binding receptors into photoreceptive pigments. Vertebrate rhodopsins are able to bind the inverse agonist 11-cis-retinal but are unable to bind the agonist all-trans-retinal, indicating that vertebrate rhodopsin changed its binding ability during the course of molecular evolution. Here, we sh...
متن کاملArrestin residues involved in the functional binding of arrestin to phosphorylated, photolyzed rhodopsin.
PURPOSE The purpose of our study was to determine whether arrestin residues previously predicted by computational modeling to interact with an aspartic acid substituted rhodopsin tail are actually involved in interactions with phospho-residues on the rhodopsin cytoplasmic tail. METHODS We generated arrestin mutants with altered charges at predicted positions. These mutants were then tested fo...
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ژورنال
عنوان ژورنال: Biophysical Journal
سال: 2012
ISSN: 0006-3495
DOI: 10.1016/j.bpj.2011.11.2824