USP14 inhibits ER-associated degradation via interaction with IRE1α

被引：40

作者：

Nagai, Atsushi ^{[2
]}

Kadowaki, Hisae ^{[1
,2
]}

Maruyama, Takeshi ^{[1
,2
]}

Takeda, Kohsuke ^{[1
]}

Nishitoh, Hideki ^{[1
,2
]}

Ichijo, Hidenori ^{[1
]}

机构：

[1] Univ Tokyo, Grad Sch Pharmaceut Sci, Lab Cell Signaling, Bunkyo Ku, Tokyo 1130033, Japan

[2] Tokyo Med & Dent Univ, Grad Sch, Ctr Excellence Program Frontier Res Mol Destruct, Bunkyo Ku, Tokyo 1138510, Japan

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2009年 / 379卷 / 04期

关键词：

ER stress; ERAD; IRE1; USP14; UNFOLDED-PROTEIN RESPONSE; ENDOPLASMIC-RETICULUM STRESS; QUALITY-CONTROL; RETRO-TRANSLOCATION; ATAXIA MICE; PROTEASOME; IRE1; KINASE; ACTIVATION; MECHANISMS;

D O I：

10.1016/j.bbrc.2008.12.182

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：

Accumulation of unfolded proteins within the endoplasmic reticulum (ER) lumen induces ER stress. Eukaryotic cells possess the ER quality control systems, the unfolded protein response (UPR), to adapt to ER stress. IRE1 alpha is one of the ER stress receptors and mediates the UPR. Here, we identified ubiquitin specific protease (USP) 14 as a binding partner of IRE1 alpha. USP14 interacted with the cytoplasmic region of IRE1 alpha, and the endogenous interaction between USP14 and IRE1 alpha was inhibited by ER stress. Overexpression of USP14 inhibited the ER-associated degradation (ERAD) pathway, and USP14 depletion by small interfering RNA effectively activated ERAD. These findings suggest that USP14 is a novel player in the UPR by serving as a physiological inhibitor of ERAD under the non-stressed condition. (C) 2009 Elsevier Inc. All rights reserved.

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页码：995 / 1000

页数：6

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