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• W2617686703 startingPage "12496" @default.
• W2617686703 abstract "Arrestins specifically bind active and phosphorylated forms of their cognate G protein–coupled receptors, blocking G protein coupling and often redirecting the signaling to alternative pathways. High-affinity receptor binding is accompanied by two major structural changes in arrestin: release of the C-tail and rotation of the two domains relative to each other. The first requires detachment of the arrestin C-tail from the body of the molecule, whereas the second requires disruption of the network of charge-charge interactions at the interdomain interface, termed the polar core. These events can be facilitated by mutations destabilizing the polar core or the anchoring of the C-tail that yield “preactivated” arrestins that bind phosphorylated and unphosphorylated receptors with high affinity. Here we explored the functional role in arrestin activation of the three native cysteines in the N domain, which are conserved in all arrestin subtypes. Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations. Thus, these three conserved cysteines play a role in the domain rotation but not in the C-tail release. Arrestins specifically bind active and phosphorylated forms of their cognate G protein–coupled receptors, blocking G protein coupling and often redirecting the signaling to alternative pathways. High-affinity receptor binding is accompanied by two major structural changes in arrestin: release of the C-tail and rotation of the two domains relative to each other. The first requires detachment of the arrestin C-tail from the body of the molecule, whereas the second requires disruption of the network of charge-charge interactions at the interdomain interface, termed the polar core. These events can be facilitated by mutations destabilizing the polar core or the anchoring of the C-tail that yield “preactivated” arrestins that bind phosphorylated and unphosphorylated receptors with high affinity. Here we explored the functional role in arrestin activation of the three native cysteines in the N domain, which are conserved in all arrestin subtypes. Using visual arrestin-1 and rhodopsin as a model, we found that substitution of these cysteines with serine, alanine, or valine virtually eliminates the effects of the activating polar core mutations on the binding to unphosphorylated rhodopsin while only slightly reducing the effects of the C-tail mutations. Thus, these three conserved cysteines play a role in the domain rotation but not in the C-tail release." @default.
• W2617686703 created "2017-06-05" @default.
• W2617686703 creator A5011089158 @default.
• W2617686703 creator A5041615081 @default.
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• W2617686703 date "2017-07-01" @default.
• W2617686703 modified "2023-10-16" @default.
• W2617686703 title "Functional role of the three conserved cysteines in the N domain of visual arrestin-1" @default.
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• W2617686703 doi "https://doi.org/10.1074/jbc.m117.790386" @default.
• W2617686703 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/5535024" @default.
• W2617686703 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/28536260" @default.
• W2617686703 hasPublicationYear "2017" @default.
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