» Articles » PMID: 25183007

Heterologous Regulation of Mu-opioid (MOP) Receptor Mobility in the Membrane of SH-SY5Y Cells

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2014 Sep 4
PMID 25183007
Citations 7
Authors
Affiliations
Soon will be listed here.
Abstract

The dynamic organization of G protein-coupled receptors in the plasma membrane is suspected of playing a role in their function. The regulation of the diffusion mode of the mu-opioid (MOP) receptor was previously shown to be agonist-specific. Here we investigate the regulation of MOP receptor diffusion by heterologous activation of other G protein-coupled receptors and characterize the dynamic properties of the MOP receptor within the heterodimer MOP/neuropeptide FF (NPFF2) receptor. The data show that the dynamics and signaling of the MOP receptor in SH-SY5Y cells are modified by the activation of α2-adrenergic and NPFF2 receptors, but not by the activation of receptors not described to interact with the opioid receptor. By combining, for the first time, fluorescence recovery after photobleaching at variable radius experiments with bimolecular fluorescence complementation, we show that the MOP/NPFF2 heterodimer adopts a specific diffusion behavior that corresponds to a mix of the dynamic properties of both MOP and NPFF2 receptors. Altogether, the data suggest that heterologous regulation is accompanied by a specific organization of receptors in the membrane.

Citing Articles

Luminescence- and Fluorescence-Based Complementation Assays to Screen for GPCR Oligomerization: Current State of the Art.

Wouters E, Vasudevan L, Crans R, Saini D, Stove C Int J Mol Sci. 2019; 20(12).

PMID: 31213021 PMC: 6627893. DOI: 10.3390/ijms20122958.


Temporal dependence of shifts in mu opioid receptor mobility at the cell surface after agonist binding observed by single-particle tracking.

Metz M, Pennock R, Krapf D, Hentges S Sci Rep. 2019; 9(1):7297.

PMID: 31086197 PMC: 6514008. DOI: 10.1038/s41598-019-43657-x.


GFP fluorescence: A few lesser-known nuggets that make it work.

Sarkar P, Chattopadhyay A J Biosci. 2018; 43(3):421-430.

PMID: 30002261


Dynamic lateral organization of opioid receptors (kappa, mu and mu ) in the plasma membrane at the nanoscale level.

Rogacki M, Golfetto O, Tobin S, Li T, Biswas S, Jorand R Traffic. 2018; .

PMID: 29808515 PMC: 6120469. DOI: 10.1111/tra.12582.


Methods used to study the oligomeric structure of G-protein-coupled receptors.

Guo H, An S, Ward R, Yang Y, Liu Y, Guo X Biosci Rep. 2017; 37(2).

PMID: 28062602 PMC: 5398257. DOI: 10.1042/BSR20160547.


References
1.
Chabot-Dore A, Schuster D, Stone L, Wilcox G . Analgesic synergy between opioid and α2 -adrenoceptors. Br J Pharmacol. 2014; 172(2):388-402. PMC: 4292955. DOI: 10.1111/bph.12695. View

2.
Berglund M, Schober D, Esterman M, Gehlert D . Neuropeptide Y Y4 receptor homodimers dissociate upon agonist stimulation. J Pharmacol Exp Ther. 2003; 307(3):1120-6. DOI: 10.1124/jpet.103.055673. View

3.
Calizo R, Scarlata S . Discrepancy between fluorescence correlation spectroscopy and fluorescence recovery after photobleaching diffusion measurements of G-protein-coupled receptors. Anal Biochem. 2013; 440(1):40-8. PMC: 3770895. DOI: 10.1016/j.ab.2013.04.033. View

4.
Mollereau C, Mazarguil H, Zajac J, Roumy M . Neuropeptide FF (NPFF) analogs functionally antagonize opioid activities in NPFF2 receptor-transfected SH-SY5Y neuroblastoma cells. Mol Pharmacol. 2004; 67(3):965-75. DOI: 10.1124/mol.104.004614. View

5.
Rozenfeld R, Devi L . Receptor heteromerization and drug discovery. Trends Pharmacol Sci. 2010; 31(3):124-30. PMC: 2834828. DOI: 10.1016/j.tips.2009.11.008. View