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

Research output: Contribution to journalMeeting abstract

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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 Our unpublished studies suggest that hP2Y1 and hP2Y12 heterodimerise; therefore, the aim of this study was to investigate the functional relevance of receptor interaction,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.
Original languageEnglish
Pages (from-to)3049
Number of pages1
JournalBritish Journal of Pharmacology
Volume176
Issue number16
Early online date9 Jul 2019
DOIs
Publication statusPublished - 1 Aug 2019
EventPharmacology 2018 - QEII Centre, London, United Kingdom
Duration: 18 Dec 201820 Dec 2018
https://www.bps.ac.uk/news-events/events/2018/december/pharmacology-2018

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Purinergic P2Y1 Receptors
Purinergic P2Y12 Receptors

Keywords

  • P2Y1 receptors
  • P2Y12 receptors
  • G‐protein coupled receptors (GPCRs)
  • heterodimersation

Cite this

@article{e7a711c3b1df4bbaa17a4d70db7fee97,
title = "P2Y1 and P2Y12 receptor heterodimerisation: from recombinant systems to native detection",
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 Our unpublished studies suggest that hP2Y1 and hP2Y12 heterodimerise; therefore, the aim of this study was to investigate the functional relevance of receptor interaction,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.",
keywords = "P2Y1 receptors, P2Y12 receptors, G‐protein coupled receptors (GPCRs), heterodimersation",
author = "M.A. Safar and R. Wood and M.R. Cunningham and C. Kennedy",
note = "Abstract number: OC053.",
year = "2019",
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day = "1",
doi = "10.1111/bph.14681",
language = "English",
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P2Y1 and P2Y12 receptor heterodimerisation : from recombinant systems to native detection. / Safar, M.A.; Wood, R.; Cunningham, M.R.; Kennedy, C.

In: British Journal of Pharmacology, Vol. 176, No. 16, 01.08.2019, p. 3049.

Research output: Contribution to journalMeeting abstract

TY - JOUR

T1 - P2Y1 and P2Y12 receptor heterodimerisation

T2 - from recombinant systems to native detection

AU - Safar, M.A.

AU - Wood, R.

AU - Cunningham, M.R.

AU - Kennedy, C.

N1 - Abstract number: OC053.

PY - 2019/8/1

Y1 - 2019/8/1

N2 - 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.

AB - 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.

KW - P2Y1 receptors

KW - P2Y12 receptors

KW - G‐protein coupled receptors (GPCRs)

KW - heterodimersation

UR - https://bpspubs.onlinelibrary.wiley.com/doi/abs/10.1111/bph.14681

U2 - 10.1111/bph.14681

DO - 10.1111/bph.14681

M3 - Meeting abstract

VL - 176

SP - 3049

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

SN - 0007-1188

IS - 16

ER -