Light resonance energy transfer-based methods in the study of G protein-coupled receptor oligomerization.
Since most of the functions in cells are mediated by multimeric protein complexes, the determination of protein-protein interactions is an important step in the study of cellular mechanisms. Traditionally, after screening for possible target interactors by means of a yeast two-hybrid screen, several methods are used to validate the initial result before carrying out functional experiments. Nowadays, non-invasive fluorescence-based methods like Bioluminescence Resonance Energy Transfer (BRET) and Fluorescence Resonance Energy Transfer (FRET) are widely used in the study of protein-protein interactions in living cells. In the present review, we address the individual strengths and weaknesses of both RET approaches, providing information on their possible future use in the study of G protein-coupled receptor oligomerization.
Gandía
Jorge
J
Unitat de Farmacologia, Departament de Patologia i Terapèutica Experimental, Facultat de Medicina, Universitat de Barcelona, Spain.
Lluís
Carme
C
Ferré
Sergi
S
Franco
Rafael
R
Ciruela
Francisco
F
D000818:Animals; D019281:Dimerization; D031541:Fluorescence Resonance Energy Transfer / Q000379:methods*; D006801:Humans; D008027:Light; D008164:Luminescent Proteins / Q000737:chemistry / Q000378:metabolism; D008954:Models, Biological; D011485:Protein Binding; D043562:Receptors, G-Protein-Coupled / Q000032:analysis* / Q000737:chemistry / Q000378:metabolism*
D008164:Luminescent Proteins; D043562:Receptors, G-Protein-Coupled