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  • Title: Measuring Recruitment of β-Arrestin to G Protein-Coupled Heterodimers Using Bioluminescence Resonance Energy Transfer.
    Author: Fillion D, Devost D, Hébert TE.
    Journal: Methods Mol Biol; 2019; 1957():83-91. PubMed ID: 30919348.
    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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