Functional Map of Arrestin Binding to Phosphorylated Opsin, with and Without Agonist

Overview

Journal Sci Rep

Specialty Science

Date 2016 Jun 29

PMID 27350090

Citations 19

Authors

Christian Peterhans

Ciara C M Lally

Martin K Ostermaier

Martha E Sommer

Jorg Standfuss

Affiliations

Soon will be listed here.

Abstract

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 agonist-bound form (Meta II-P). Disruption of the polar core or displacement of the C-tail strengthened binding to both receptor forms. In contrast, mutations of phosphate-binding residues (phosphosensors) suggest the phosphorylated receptor C-terminus binds arrestin differently for Meta II-P and Ops-P. Likewise, mutations within the inter-domain interface, variations in the receptor-binding loops and the C-edge of arrestin reveal different binding modes. In summary, our results indicate that arrestin-1 binding to Meta II-P and Ops-P is similarly dependent on arrestin activation, although the complexes formed with these two receptor forms are structurally distinct.

Citing Articles

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