Agonist-independent localization of the NOP receptor in detergent-resistant membrane rafts

被引：5
|
作者：
Butour, JL [1 ]
Corbani, M [1 ]
Meunier, JC [1 ]
机构：
[1] CNRS, Unite Neuropharmacol Mol, Inst Pharmacol & Biol Struct, UMR 5089, F-31077 Toulouse 04, France
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2004年 / 325卷 / 03期
关键词：
nociceptin/orphanin FQ; G protein-coupled receptor; green fluorescent protein; detergent-resistant membrane fraction; methyl-beta-cyclodextrin; signal transduction;
D O I：
10.1016/j.bbrc.2004.10.125
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：
A lipid rafts/detergent-resistant membrane (DRM) fraction was prepared from recombinant HEK293 cells stably expressing the human NOP receptor fused to the green fluorescent protein EGFP (hNOPr-EGFP), and probed for the presence and functionality of the fusion protein. Fluorescence detection as well as immunoblotting with an anti-GFP antibody revealed that most of the fusion protein was recovered in the DRM fraction, wherein it mediated efficiently NOP-induced stimulation of GTPgamma(35)S binding. Recovery of hNOPr-EGFP in the DRM fraction was not affected had the cells been acutely or chronically exposed to NOP prior to detergent treatment. Therefore, in HEK cells, the NOP receptor localizes constitutively to DRMs wherein it retains ability to couple with hetero-trimeric G protein. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码：915 / 921
页数：7
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