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Light resonance energy transfer‐based methods in the study of G protein‐coupled receptor oligomerization
Author(s) -
Gandía Jorge,
Lluís Carme,
Ferré Sergi,
Franco Rafael,
Ciruela Francisco
Publication year - 2008
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.20682
Subject(s) - förster resonance energy transfer , energy transfer , bioluminescence , protein–protein interaction , resonance (particle physics) , bimolecular fluorescence complementation , fluorescence , biophysics , yeast , biology , microbiology and biotechnology , computational biology , chemistry , biochemistry , physics , chemical physics , particle physics , quantum mechanics
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. BioEssays 30:82–89, 2008. © 2007 Wiley Periodicals, Inc.