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

Mohammed Akli Ayoub, Abdulrahman Al-Senaidy, Jean Philippe Pin

Research output: Contribution to journalArticlepeer-review

22 Citations (Scopus)

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.

Original languageEnglish
Article numberArticle 82
JournalFrontiers in Endocrinology
Volume3
Issue numberJUN
DOIs
Publication statusPublished - 2012
Externally publishedYes

Keywords

  • Bret
  • G proteins
  • Par1
  • Preassembly
  • Precoupling
  • Protein interactions

ASJC Scopus subject areas

  • Endocrinology, Diabetes and Metabolism

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