Bioluminescent resonance energy transfer

Percherancier Y, Berchiche YA, Slight 1, Volkmer-Engert R, Tamamura H, Fujii N, Bouvier M, Heveker N (2005) Bioluminescence resonance energy transfer reveals hgand-induced conformational changes in CXCR4 homo- and heterodimers. J Biol Chem 280 9895-9903... 

James, J. R., Oliveira, M. I., Carmo, A. M., Iaboni, A. and Davis, S. J. (2006). A rigorous experimental framework for detecting protein oligomerization using bioluminescence resonance energy transfer. Nat. Methods 3, 1001-6. 

Coulon, V., Audet, M., Homburger, V., Bockaert, J., Fagni, L., Bouvier, M. and Perroy, J. (2008). Subcellular imaging of dynamic protein interactions by bioluminescence resonance energy transfer. Biophys. J. 94,1001-9. 

Xu, X., Soutto, M., Xie, Q., Servick, S., Subramanian, C., von Arnim, A. G. and Johnson, C. H. (2007). Imaging protein interactions with bioluminescence resonance energy transfer (BRET) in plant and mammalian cells and tissues. Proc. Natl. Acad. Sci. USA 104, 10264-9. 

Cheng, Z. J. and Miller, L. J. (2001) Agonist-dependent dissociation of oligomeric complexes of G protein-coupled cholecystokinin receptors demonstrated in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276,48040-48047. 

Mercier, J. F., Salahpour, A., Angers, S., Breit, A., and Bouvier, M. (2002) Quantitative assessment of beta 1 and beta 2-adrenergic receptor homo and hetero-dimerization by bioluminescence resonance energy transfer. J. Biol. Chem. 277,44925 14931. 

Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. USA 97, 3684-3689. 

Yamakawa Y, Ueda H, Kitayama A et al (2002) Rapid homogeneous immunoassay of peptides based on bioluminescence resonance energy transfer from firefly luciferase. J Biosci Bioeng 93 537-542... 

Alvarez-Curto E, Pediani JD, Milligan G (2010) Applications of fluorescence and bioluminescence resonance energy transfer to drug discovery at G protein coupled receptors. Anal Bioanal Chem 398 167-180... 

Xu, Y., Piston, D.W. and Johnson, C.H. (1999). A bioluminescence resonance energy transfer (BRET) system application to interacting circadian clock proteins. Proceedings of the National Academy of Sciences, USA, 96, 151-156. 

McVey M, Ramsay D, Kellett E, Rees S, Wilson S, et al. 2001. Monitoring receptor oligomerization using time-resolved fluorescence resonance energy transfer and bioluminescence resonance energy transfer. The human delta-opioid receptor displays constitutive oligomerization at the cell... 

Like FRET, bioluminescence resonance energy transfer (BRET) is based on non-radiative energy transfer between a donor and an acceptor. However, in BRET, the donor is a luminescent molecule, excited by the enzyme Renilla Luciferase (Rluc), and not a fluorescent molecule. The BRET acceptor can be a fluorescent protein like green fluorescent protein (GFP) or YFR If the enzyme and the fluorescent protein are in close proximity (d < 10 nm), an energy transfer will occur between the Rluc substrate (coelanterazine) and the fluorescent protein, leading to emission from the later. 

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