The Role of Arrestin-1 Middle Loop in Rhodopsin Binding

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dc.contributor.authorVishnivetskiy, Sergey A.
dc.contributor.authorHuh, Elizabeth K.
dc.contributor.authorKarnam, Preethi C.
dc.contributor.authorOviedo, Samantha
dc.contributor.authorGurevich, Eugenia V.
dc.contributor.authorGurevich, Vsevolod V.
dc.date.accessioned2022-11-24T14:43:45Z
dc.date.available2022-11-24T14:43:45Z
dc.date.issued2022-11-11
dc.date.updated2022-11-24T14:43:46Z
dc.description.abstractArrestins preferentially bind active phosphorylated G protein-coupled receptors (GPCRs). The middle loop, highly conserved in all arrestin subtypes, is localized in the central crest on the GPCR-binding side. Upon receptor binding, it directly interacts with bound GPCR and demonstrates the largest movement of any arrestin element in the structures of the complexes. Comprehensive mutagenesis of the middle loop of rhodopsin-specific arrestin-1 suggests that it primarily serves as a suppressor of binding to non-preferred forms of the receptor. Several mutations in the middle loop increase the binding to unphosphorylated light-activated rhodopsin severalfold, which makes them candidates for improving enhanced phosphorylation-independent arrestins. The data also suggest that enhanced forms of arrestin do not bind GPCRs exactly like the wild-type protein. Thus, the structures of the arrestin-receptor complexes, in all of which different enhanced arrestin mutants and reengineered receptors were used, must be interpreted with caution.
dc.description.departmentChemistry
dc.identifierdoi: 10.3390/ijms232213887
dc.identifier.citationInternational Journal of Molecular Sciences 23 (22): 13887 (2022)
dc.identifier.urihttps://hdl.handle.net/20.500.12588/1418
dc.rightsAttribution 4.0 United States
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.subjectarrestin
dc.subjectGPCR
dc.subjectmutagenesis
dc.subjectprotein-protein interactions
dc.subjectreceptor binding
dc.subjectselectivity
dc.titleThe Role of Arrestin-1 Middle Loop in Rhodopsin Binding
dc.typeArticle

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