Phosphorylation-induced conformation of β₂-adrenoceptor related to arrestin recruitment revealed by NMR.

ABSTRACT: The C-terminal region of G-protein-coupled receptors (GPCRs), stimulated by agonist binding, is phosphorylated by GPCR kinases, and the phosphorylated GPCRs bind to arrestin, leading to the cellular responses. To understand the mechanism underlying the formation of the phosphorylated GPCR-arrestin complex, we performed NMR analyses of the phosphorylated β₂-adrenoceptor (β₂AR) and the phosphorylated β₂AR-β-arrestin 1 complex, in the lipid bilayers of nanodisc. Here we show that the phosphorylated C-terminal region adheres to either the intracellular side of the transmembrane region or lipids, and that the phosphorylation of the C-terminal region allosterically alters the conformation around M215^5.54 and M279^6.41, located on transemembra

SUBMITTER: Shiraishi Y 

PROVIDER: S-EPMC5768704 | biostudies-literature | 2018 Jan

REPOSITORIES: biostudies-literature