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        Study of G-Protein-Coupled Receptor-Protein Interactions by Bioluminescence Resonance Energy Transfer

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        Complex networks of protein-protein interactions are key determinants of cellular function, including those regulated by G-protein-coupled receptors (GPCRs). Formation of either stable or transitory complexes are involved in regulating all aspects of receptor function, from ligand binding through to signal transduction, desensitization, resensitization and downregulation. Today, 50% of all recently launched drugs are targeted against GPCRs. This particular class of proteins is extremely useful as a drug target because the receptors are partly located outside the cell, simplifying bioavailability and delivery of drugs directed against them. However, being located within the cell membrane causes difficulties for the study of GPCR function and bioluminescence resonance energy transfer (BRET), a naturally occurring phenomenon, represents a newly emerging, powerful tool with which to investigate and monitor dynamic interactions involving this receptor class. BRET is a noninvasive, highly sensitive technique, performed as a simple homogeneous assay, involving the proximity-dependent transfer of energy from an energy donor to acceptor resulting in the emission of light. This technology has several advantages over alternative approaches as the detection occurs within live cells, in real time, and is not restricted to a particular cellular compartment. The use of such biophysical techniques as BRET, will not only increase our understanding of the nature of GPCR regulation and the protein complexes involved, but could also potentially lead to the development of novel therapeutics that modulate these interactions.
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