Structural studies of phosphorylation-dependent interactions between the V2R receptor and arrestin-2.

ABSTRACT: Arrestins recognize different receptor phosphorylation patterns and convert this information to selective arrestin functions to expand the functional diversity of the G protein-coupled receptor (GPCR) superfamilies. However, the principles governing arrestin-phospho-receptor interactions, as well as the contribution of each single phospho-interaction to selective arrestin structural and functional states, are undefined. Here, we determined the crystal structures of arrestin2 in complex with four different phosphopeptides derived from the vasopressin receptor-2 (V2R) C-tail. A comparison of these four crystal structures with previously solved Arrestin2 structures demonstrated that a single phospho-interaction change results in measurable conformational changes at remote sites in the complex

SUBMITTER: He QT 

PROVIDER: S-EPMC8062632 | biostudies-literature | 2021 Apr

REPOSITORIES: biostudies-literature