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Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by degrading Bcl-xL, PNAS, 115(12):E2762-E2771,5 Mar 2018
2018-03-07 | 【     】【打印】【关闭

Proc Natl Acad Sci U S A,115(12):E2762-E2771,5 Mar 2018,DOI: 10.1073/pnas.1716439115

Transmembrane E3 ligase RNF183 mediates ER stress-induced apoptosis by degrading Bcl-xL

Yanfang Wu, Xia Li, Junying Jia, Yanpeng Zhang, Jing Li, Zhengmao Zhu, Huaqing Wang, Jie Tang and Junjie Hu

Abstract

The accumulation of unfolded proteins in the endoplasmic reticulum (ER) is a pathological condition observed in many diseases, including cancer, diabetes, and neurodegenerative diseases. Failure to relieve the cellular stress via adaptive mechanisms of the unfolded protein response (UPR) activates apoptotic cell death. We demonstrate that a membrane-anchored RING finger protein, RNF183, is specifically induced by prolonged ER stress. RNF183 is regulated by IRE1, mainly through miR-7. As an E3 ligase, RNF183 ubiquitinates Bcl-xL, causing its degradation and subsequent apoptosis. Our findings imply that manipulation of RNF183 activity may help control cell fate in pathological conditions and suggest that the close contact between the ER and mitochondria plays a key role in cellular signaling.

文章链接:http://www.pnas.org/content/early/2018/03/01/1716439115

相关报道:http://www.ibp.cas.cn/kyjz/zxdt/201803/t20180308_4970998.html

 

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