Abstract
Bioluminescence resonance energy transfer (BRET) is a natural phenomenon that has been successfully applied for the study of protein–protein interactions, including opioid receptor oligomers. The discovery of opioid receptor homomers and heteromers has brought to the finding of new functions and new way of signaling and trafficking; therefore, opioid receptor oligomers may be considered as novel drug targets. Fusing receptors of interest with Renilla luciferase and with a fluorescent protein (such as EYFP), it is possible to study opioid receptor dimerization using BRET.
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References
Bacart J, Corbel C, Jockers R et al (2008) The BRET technology and its application to screening assays. Biotechnol J 3:311–324
Lohse MJ, Nuber S, Hoffmann C (2012) Fluorescence/bioluminescence resonance energy transfer techniques to study G-protein-coupled receptor activation and signaling. Pharmacol Rev 64:299–336
Ferré S, Navarro G, Casadó V et al (2010) G protein-coupled receptor heteromers as new targets for drug development. Prog Mol Biol Transl Sci 91:41–52
Hart RC, Stempel KE, Boyer PD et al (1978) Mechanism of the enzyme-catalyzed bioluminescent oxidation of coelenteratetype luciferin. Biochem Biophys Res Commun 81:980–986
Wilson T, Hastings JW (1998) Bioluminescence. Annu Rev Cell Dev Biol 14:197–230
Ayoub MA, Pfleger KD (2010) Recent advances in bioluminescence resonance energy transfer technologies to study GPCR heteromerization. Curr Opin Pharmacol 10:44–52
Pfleger KD, Dromey JR, Dalrymple MB et al (2006) Extended bioluminescence resonance energy transfer (eBRET) for monitoring prolonged protein–protein interactions in live cells. Cell Signal 18:1664–1670
Pfleger KD (2009) Analysis of protein–protein interactions using bioluminescence resonance energy transfer. Methods Mol Biol 574: 173–183
Pfleger KD, Eidne KA (2003) New technologies: bioluminescence resonance energy transfer (BRET) for the detection of real time interactions involving G-protein coupled receptors. Pituitary 6:141–151
Wang D, Sun X, Bohn LM et al (2005) Opioid receptor homo- and heterodimerization in living cells by quantitative bioluminescence resonance energy transfer. Mol Pharmacol 67: 2173–2184
Gomes I, Filipovska J, Jordan BA et al (2002) Oligomerization of opioid receptors. Methods 27:358–365
George SR, Fan T, Xie Z et al (2000) Oligomerization of mu- and delta-opioid receptors. Generation of novel functional properties. J Biol Chem 275:26128–26135
van Rijn RM, Whistler JL, Waldhoer M (2010) Opioid-receptor-heteromer-specific trafficking and pharmacology. Curr Opin Pharmacol 10: 73–79
Pan YX, Bolan E, Pasternak GW (2002) Dimerization of morphine and orphanin FQ/nociceptin receptors: generation of a novel opioid receptor subtype. Biochem Biophys Res Commun 297:659–663
McVey M, Ramsay D, Kellett E 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 surface, which is not regulated by receptor occupancy. J Biol Chem 276:14092–14099
Rios C, Gomes I, Devi LA (2006) mu opioid and CB1 cannabinoid receptor interactions: reciprocal inhibition of receptor signaling and neuritogenesis. Br J Pharmacol 148:387–395
Kocan M, See HB, Seeber RM et al (2008) Demonstration of improvements to the bioluminescence resonance energy transfer (BRET) technology for the monitoring of G protein-coupled receptors in live cells. J Biomol Screen 13:888–898
Li Y, Chen J, Bai B et al (2012) Heterodimerization of human apelin and kappa opioid receptors: roles in signal transduction. Cell Signal 24:991–1001
Li F, Yu J, Zhang Z et al (2012) Buffer enhanced bioluminescence resonance energy transfer sensor based on Gaussia luciferase for in vitro detection of protease. Anal Chim Acta 724:104–110
Couturier C, Deprez B (2012) Setting up a bioluminescence resonance energy transfer high throughput screening assay to search for protein/protein interaction inhibitors in mammalian cells. Front Endocrinol (Lausanne) 3:1–13
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Baiula, M. (2015). Monitoring Opioid Receptor Dimerization in Living Cells by Bioluminescence Resonance Energy Transfer (BRET). In: Spampinato, S. (eds) Opioid Receptors. Methods in Molecular Biology, vol 1230. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-1708-2_8
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DOI: https://doi.org/10.1007/978-1-4939-1708-2_8
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