期刊
NEUROSCIENCE LETTERS
卷 466, 期 3, 页码 154-158出版社
ELSEVIER IRELAND LTD
DOI: 10.1016/j.neulet.2009.09.048
关键词
Mu opioid receptor; RanBPM; Internalization; Scaffold protein; beta Arrestin; Yeast two-hybrid screen
资金
- National Institutes of Health [DA016346]
- Bower, Bennet, & Bennet Endowed Chair Research Award
- American Foundation for Pharmaceutical Education New Investigator Program
- University of Nebraska Medical Center
Mu opioid receptors (MOP) are transducers of the pharmacological effects of many opioid drugs, including analgesia and tolerance/dependence. Previously, we observed increased MOP signaling during postnati development that was not associated with increased MOP or G protein expression. A yeast two-hybrid screen of a human brain cDNA library using the MOP C-terminus as bait identified RanBPM as a potential MOP-interacting protein. RanBPM has been recognized as a multi-functional scaffold protein that interacts with a variety of signaling receptors/proteins. Co-immunoprecipitation studies in HEK29 cells indicated that RanBPM constitutively associates with MOP. Functionally, RanBPM had no effect on MOP-mediated inhibition of adenylyl cyclase, yet reduced agonist-induced endocytosis of MOP Mechanistically, RanBPM interfered with beta arrestin2-GFP translocation stimulated by MOP but not alpha(1B) adrenergic receptor activation, indicating selectivity of action. Our findings suggest that RanBPM is novel MOP-interacting protein that negatively regulates receptor internalization without altering MC signaling through adenylyl cyclase. (C) 2009 Elsevier Ireland Ltd. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据