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

被引：15

作者：

Carayon, Kevin ^{[1
]}

Mouledous, Lionel ^{[1
]}

Combedazou, Anne ^{[1
]}

Mazeres, Serge ^{[1
]}

Haanappel, Evert ^{[1
]}

Salome, Laurence ^{[1
]}

Mollereau, Catherine ^{[1
]}

机构：

[1] Univ Toulouse, CNRS, UMR5089, Inst Pharmacol & Biol Struct, F-31077 Toulouse, France

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 2014年 / 289卷 / 41期

关键词：

PROTEIN-COUPLED RECEPTOR; FLUORESCENCE CORRELATION SPECTROSCOPY; HUMAN NEUROBLASTOMA SH-SY5Y; CONDITIONED PLACE PREFERENCE; RAT DORSAL RAPHE; NEUROPEPTIDE-FF; FUNCTIONAL INTERACTIONS; FRAP EXPERIMENTS; PLASMA-MEMBRANE; LIVING CELLS;

D O I：

10.1074/jbc.M114.588558

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 alpha(2)-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 photo-bleaching 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.

引用

页码：28697 / 28706

页数：10