P2Y1 and P2Y12 receptor heterodimerisation : from recombinant systems to native detection

Safar, M.A. and Wood, R. and Cunningham, M.R. and Kennedy, C. (2019) P2Y1 and P2Y12 receptor heterodimerisation : from recombinant systems to native detection. British Journal of Pharmacology, 176 (16). p. 3049. ISSN 1476-5381

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    Abstract

    Purinergic P2Y1 and P2Y12 receptors belong to the class A family of transmembrane G‐protein coupled receptors (GPCRs) and have been demonstrated to exist as homodimers and oligomers and form heterodimers with other GPCRs. P2Y12 and protease‐activated receptor 4 (PAR4) were recently reported to form a heterodimer with implications in receptor trafficking and signalling. Our unpublished studies suggest that hP2Y1 and hP2Y12 heterodimerise; therefore, the aim of this study was to investigate the functional relevance of receptor interaction, firstly in recombinant systems and then natively in microglial cells. hP2Y1 and hP2Y12 receptor heterodimersation impacted ADP‐mediated internalisation when both receptors are overexpressed in tSA201 cells. Co‐localisation studies in BV‐2 cells suggest that the location of receptor interaction may differ depending upon the cell types explored. Further work is under way to investigate these differences.