Apelin receptor homodimer-oligomers revealed by single-molecule imaging and novel G protein-dependent signaling.

ABSTRACT: The apelin receptor (APJ) belongs to family A of the G protein-coupled receptors (GPCRs) and is a potential pharmacotherapeutic target for heart failure, hypertension, and other cardiovascular diseases. There is evidence APJ heterodimerizes with other GPCRs; however, the existence of APJ homodimers and oligomers remains to be investigated. Here, we measured APJ monomer-homodimer-oligomer interconversion by monitoring APJ dynamically on cells and compared their proportions, spatial arrangement, and mobility using total internal reflection fluorescence microscopy, resonance energy transfer, and proximity biotinylation. In cells with <0.3 receptor particles/μm², approximately 60% of APJ molecules were present as dimers or oligomers. APJ dimers were present on the cell surface in a

SUBMITTER: Cai X 

PROVIDER: S-EPMC5238433 | biostudies-literature | 2017 Jan

REPOSITORIES: biostudies-literature