Résumé
G protein-coupled receptors (GPCRs) are the largest family of cellular surface receptors and play a key role controlling a diverse array of developmental and physiological processes. Therefore, GPCRs constitute the targets of many modern therapeutics. Interestingly, GPCRs can interact (i.e., oligomerize) with other cell surface receptors and ion channels, thus leading to a fine-tuning modulation of physiological functions. In line with this, GPCR oligomerization has gained interest during the last years, since drugs targeting these molecular entities could open new GPCR-based pharmacotherapeutic avenues. Accordingly, different techniques assessing the occurrence of GPCR oligomerization in native tissue have emerged (i.e., immunoelectron microscopy, proximity ligation assay, etc.). From them, one of the most reliable approaches consists of using GPCR-fluorescent ligands engaging into a heteromerization-dependent time-resolved fluorescence resonance energy transfer (TR-FRET) process. Here, we review this methodology to reveal receptor-receptor interactions in brain tissue.