Molecular basis of association of receptor activity-modifying protein 3 with the family B G protein-coupled secretin receptor.

ABSTRACT: The three receptor activity-modifying proteins (RAMPs) have been recognized as being important for the trafficking and function of a subset of family B G protein-coupled receptors, although the structural basis for this has not been well established. In the current work, we use morphological fluorescence techniques, bioluminescence resonance energy transfer, and bimolecular fluorescence complementation to demonstrate that the secretin receptor associates specifically with RAMP3, but not with RAMP1 or RAMP2. We use truncation constructs, peptide competition experiments, and chimeric secretin-GLP1 receptor constructs to establish that this association is structurally specific, dependent on the intramembranous region of the RAMP and TM6 and TM7 of this receptor. There were no observed changes

SUBMITTER: Harikumar KG 

PROVIDER: S-EPMC2790544 | biostudies-literature | 2009 Dec

REPOSITORIES: biostudies-literature