Bioluminescence resonance energy transfer (BRET) for the real-time detection of protein-protein interactions

Pfleger, K.D. & Eidne, K.A. Illuminating insights into protein-protein interactions using bioluminescence resonance energy transfer (BRET). Nat. Methods 3, 165–174 (2006).

Milligan, G. & Bouvier, M. Methods to monitor the quaternary structure of G-protein–coupled receptors. FEBS J. 272, 2914–2925 (2005).

Boute, N., Jockers, R. & Issad, T. The use of resonance energy transfer in high-throughput screening: BRET versus FRET. Trends Pharmacol. Sci. 23, 351–354 (2002).

Pfleger, K.D.G. & Eidne, K.A. New technologies: bioluminescence resonance energy transfer (BRET) for the detection of real time interactions involving G-protein coupled receptors. Pituitary 6, 141–151 (2003).

Wu, P. & Brand, L. Resonance energy transfer: methods and applications. Anal. Biochem. 218, 1–13 (1994).

Xu, Y., Piston, D.W. & Johnson, C.H. A bioluminescence resonance energy transfer (BRET) system: application to interacting circadian clock proteins. Proc. Natl. Acad. Sci. USA 96, 151–156 (1999).

Subramanian, C. et al. The Arabidopsis repressor of light signaling, COP1, is regulated by nuclear exclusion: mutational analysis by bioluminescence resonance energy transfer. Proc. Natl. Acad. Sci. USA 101, 6798–6802 (2004).

Angers, S. et al. Detection of beta 2-adrenergic receptor dimerization in living cells using bioluminescence resonance energy transfer (BRET). Proc. Natl. Acad. Sci. USA 97, 3684–3689 (2000).

Kroeger, K.M., Hanyaloglu, A.C., Seeber, R.M., Miles, L.E. & Eidne, K.A. Constitutive and agonist-dependent homo-oligomerization of the thyrotropin-releasing hormone receptor. Detection in living cells using bioluminescence resonance energy transfer. J. Biol. Chem. 276, 12736–12743 (2001).

Pfleger, K.D.G. & Eidne, K.A. Monitoring the formation of dynamic G-protein-coupled receptor-protein complexes in living cells. Biochem. J. 385, 625–637 (2005).

Scaffidi, A.K. et al. α(v)β(3) Integrin interacts with the transforming growth factor β (TGFβ) type II receptor to potentiate the proliferative effects of TGFβ1 in living human lung fibroblasts. J. Biol. Chem. 279, 37726–37733 (2004).

Brown, R.J. et al. Model for growth hormone receptor activation based on subunit rotation within a receptor dimer. Nat. Struct. Mol. Biol. 12, 814–821 (2005).

Michelini, E., Mirasoli, M., Karp, M., Virta, M. & Roda, A. Development of a bioluminescence resonance energy-transfer assay for estrogen-like compound in vivo monitoring. Anal. Chem. 76, 7069–7076 (2004).

Garside, H. et al. Glucocorticoid ligands specify different interactions with NF-kappaB by allosteric effects on the glucocorticoid receptor DNA binding domain. J. Biol. Chem. 279, 50050–50059 (2004).

de Virgilio, M., Kiosses, W.B. & Shattil, S.J. Proximal, selective, and dynamic interactions between integrin alphaIIbbeta3 and protein tyrosine kinases in living cells. J. Cell. Biol. 165, 305–311 (2004).

Yung, T.M., Sato, S. & Satoh, M.S. Poly(ADP-ribosyl)ation as a DNA damage-induced post-translational modification regulating poly(ADP-ribose) polymerase-1-topoisomerase I interaction. J. Biol. Chem. 279, 39686–39696 (2004).

Trevaskis, J. et al. Src homology 3-domain growth factor receptor-bound 2-like (endophilin) interacting protein 1, a novel neuronal protein that regulates energy balance. Endocrinology 146, 3757–3764 (2005).

Germain-Desprez, D., Bazinet, M., Bouvier, M. & Aubry, M. Oligomerization of transcriptional intermediary factor 1 regulators and interaction with ZNF74 nuclear matrix protein revealed by bioluminescence resonance energy transfer in living cells. J. Biol. Chem. 278, 22367–22373 (2003).

Terrillon, S. et al. Oxytocin and vasopressin V1a and V2 receptors from constitutive homo- and heterodimers during biosynthesis. Mol. Endocrinol. 17, 677–691 (2003).

Mercier, J.F., Salahpour, A., Angers, S., Breit, A. & Bouvier, M. Quantitative assessment of β1- and β2-adrenergic receptor homo- and heterodimerization by bioluminescence resonance energy transfer. J. Biol. Chem. 277, 44925–44931 (2002).

Ayoub, M.A. et al. Monitoring of ligand-independent dimerization and ligand-induced conformational changes of melatonin receptors in living cells by bioluminescence resonance energy transfer. J. Biol. Chem. 277, 21522–21528 (2002).

Hamdan, F.F., Audet, M., Garneau, P., Pelletier, J. & Bouvier, M. High-throughput screening of G protein-coupled receptor antagonists using a bioluminescence resonance energy transfer 1–based β-arrestin2 recruitment assay. J. Biomol. Screen. 10, 463–475 (2005).

Pfleger, K.D. et al. Extended bioluminescence resonance energy transfer (eBRET) for monitoring prolonged protein-protein interactions in live cells. Cell. Signal; Advance online publication 21 February 2006 (doi: 10.1016/j.cellsig.2006.01.004).

De, A. & Gambhir, S.S. Noninvasive imaging of protein-protein interactions from live cells and living subjects using bioluminescence resonance energy transfer. FASEB J. 19, 2017–2019 (2005).