Format

Send to

Choose Destination
See comment in PubMed Commons below
Front Endocrinol (Lausanne). 2012 Jun 22;3:82. doi: 10.3389/fendo.2012.00082. eCollection 2012.

Receptor-G protein interaction studied by bioluminescence resonance energy transfer: lessons from protease-activated receptor 1.

Author information

1
Department of Molecular Pharmacology, Institute of Functional Genomics, CNRS UMR5203, Universities Montpellier 1 and 2 Montpellier, France. mayoub@ksu.edu.sa

Abstract

Since its development, the bioluminescence resonance energy transfer (BRET) approach has been extensively applied to study G protein-coupled receptors (GPCRs) in real-time and in live cells. One of the major aspects of GPCRs investigated in considerable details is their physical coupling to the heterotrimeric G proteins. As a result, new concepts have emerged, but few questions are still a matter of debate illustrating the complexity of GPCR-G protein interactions and coupling. Here, we summarized the recent advances on our understanding of GPCR-G protein coupling based on BRET approaches and supported by other FRET-based studies. We essentially focused on our recent studies in which we addressed the concept of preassembly vs. the agonist-dependent interaction between the protease-activated receptor 1 (PAR1) and its cognate G proteins. We discussed the concept of agonist-induced conformational changes within the preassembled PAR1-G protein complexes as well as the critical question how the multiple coupling of PAR1 with two different G proteins, Gαi1 and Gα12, but also β-arrestin 1, can be regulated.

KEYWORDS:

BRET; G proteins; PAR1; preassembly; precoupling; protein interactions

PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for Frontiers Media SA Icon for PubMed Central
    Loading ...
    Support Center