Quaternary structure of a G-protein-coupled receptor heterotetramer in complex with Gi and Gs.

ABSTRACT:

Background

G-protein-coupled receptors (GPCRs), in the form of monomers or homodimers that bind heterotrimeric G proteins, are fundamental in the transfer of extracellular stimuli to intracellular signaling pathways. Different GPCRs may also interact to form heteromers that are novel signaling units. Despite the exponential growth in the number of solved GPCR crystal structures, the structural properties of heteromers remain unknown.

Results

We used single-particle tracking experiments in cells expressing functional adenosine A1-A2A receptors fused to fluorescent proteins to show the loss of Brownian movement of the A1 receptor in the presence of the A2A receptor, and a preponderance of cell surface 2:2 receptor heteromers (dimer of dimers). Using computer modeling, aided by

SUBMITTER: Navarro G 

PROVIDER: S-EPMC4822319 | biostudies-literature | 2016 Apr

REPOSITORIES: biostudies-literature