Abstract
Initially identified as monomers, G protein-coupled receptors (GPCRs) can also form functional dimers that act as distinct signalling hubs for the integration of cellular signalling. We previously found that the angiotensin II (Ang II) type 1 receptor (AT1R) and the prostaglandin F2α (PGF2α) receptor (FP), both important in the control of smooth muscle contractility, form such a functional heterodimeric complex in HEK 293 and vascular smooth muscle cells (Goupil et al., J Biol Chem 290:3137–3148, 2015; Sleno et al., J Biol Chem 292:12139–12152, 2017). In addition to canonical G protein coupling, GPCRs recruit and engage β-arrestin-dependent pathways. Using BRET-based biosensors, we demonstrate how to assess recruitment of β-arrestin-1 and -2 to AT1R and the AT1R/FP dimer in response to Ang II. Surprisingly, β-arrestin-1 and -2 were recruited to the dimer, in response to PGF2α as well, even though FP alone cannot recruit either β-arrestin-1 and -2.
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Acknowledgments
This work was supported by funding from the Canadian Institutes for Health Research and the Ferring Foundation. We also thank Dr. Nicolas Audet (McGill University, Montréal) for useful discussions regarding statistical analysis.
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Fillion, D., Devost, D., Hébert, T.E. (2019). Measuring Recruitment of β-Arrestin to G Protein-Coupled Heterodimers Using Bioluminescence Resonance Energy Transfer. In: Scott, M., Laporte, S. (eds) Beta-Arrestins. Methods in Molecular Biology, vol 1957. Humana Press, New York, NY. https://doi.org/10.1007/978-1-4939-9158-7_5
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DOI: https://doi.org/10.1007/978-1-4939-9158-7_5
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