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

M.A. Safar; R. Wood; M.R. Cunningham; C. Kennedy

doi:10.1111/bph.14681

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 Our unpublished studies suggest that hP2Y1 and hP2Y12 heterodimerise; therefore, the aim of this study was to investigate the functional relevance of receptor interaction,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 language	English
Pages (from-to)	3049
Number of pages	1
Journal	British Journal of Pharmacology
Volume	176
Issue number	16
Early online date	9 Jul 2019
DOIs	https://doi.org/10.1111/bph.14681
Publication status	Published - 1 Aug 2019
Event	Pharmacology 2018 - QEII Centre, London, United Kingdom Duration: 18 Dec 2018 → 20 Dec 2018 https://www.bps.ac.uk/news-events/events/2018/december/pharmacology-2018

Keywords

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

Access to Document

10.1111/bph.14681

Safar-etal-BJP-2019-P2Y1-and-P2Y12-receptor-heterodimerisation-from-recombinant-systems-to-native-detectionAccepted author manuscript, 294 KB

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 Our unpublished studies suggest that hP2Y1 and hP2Y12 heterodimerise; therefore, the aim of this study was to investigate the functional relevance of receptor interaction,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. ; Pharmacology 2018 ; Conference date: 18-12-2018 Through 20-12-2018",

year = "2019",

month = aug,

day = "1",

doi = "10.1111/bph.14681",

language = "English",

volume = "176",

pages = "3049",

journal = "British Journal of Pharmacology",

issn = "0007-1188",

number = "16",

url = "https://www.bps.ac.uk/news-events/events/2018/december/pharmacology-2018",

}

TY - JOUR

T1 - P2Y1 and P2Y12 receptor heterodimerisation

T2 - Pharmacology 2018

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 - Conference abstract

SN - 0007-1188

VL - 176

SP - 3049

JO - British Journal of Pharmacology

JF - British Journal of Pharmacology

IS - 16

Y2 - 18 December 2018 through 20 December 2018

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Cite this