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The organization of Rhodopsin-family G protein-coupled receptors (GPCRs) at the cell surface is controversial. Support both for and against the existence of dimers has been obtained in studies of mostly individual receptors. Here, we use a large-scale comparative study to examine the stoichiometric signatures of 60 receptors expressed by a single human cell line. Using bioluminescence resonance energy transfer- and single-molecule microscopy-based assays, we found that a relatively small fraction of Rhodopsin-family GPCRs behaved as dimers and that these receptors otherwise appear to be monomeric. Overall, the analysis predicted that fewer than 20% of ∼700 Rhodopsin-family receptors form dimers. The clustered distribution of the dimers in our sample and a striking correlation between receptor organization and GPCR family size that we also uncover each suggest that receptor stoichiometry might have profoundly influenced GPCR expansion and diversification.

Original publication

DOI

10.1016/j.celrep.2017.08.072

Type

Journal article

Journal

Cell Rep

Publication Date

12/09/2017

Volume

20

Pages

2654 - 2665

Keywords

BRET, G protein-coupled receptors, evolution, single-molecule imaging, stoichiometry, Fluorescence Resonance Energy Transfer, HEK293 Cells, Humans, Protein Multimerization, Protein Structure, Quaternary, Protein Structure, Secondary, Receptors, G-Protein-Coupled, Rhodopsin