Agonist-induced dimer dissociation as a macromolecular step in G protein-coupled receptor signaling.

ABSTRACT: G protein-coupled receptors (GPCRs) constitute the largest family of cell surface receptors. They can exist and act as dimers, but the requirement of dimers for agonist-induced signal initiation and structural dynamics remains largely unknown. Frizzled 6 (FZD₆) is a member of Class F GPCRs, which bind WNT proteins to initiate signaling. Here, we show that FZD₆ dimerizes and that the dimer interface of FZD₆ is formed by the transmembrane α-helices four and five. Most importantly, we present the agonist-induced dissociation/re-association of a GPCR dimer through the use of live cell imaging techniques. Further analysis of a dimerization-impaired FZD₆ mutant indicates that dimer dissociation is an integral part of FZD₆ signaling to extrac

SUBMITTER: Petersen J 

PROVIDER: S-EPMC5548745 | biostudies-literature | 2017 Aug

REPOSITORIES: biostudies-literature