Ubiquitin-Specific Protease 25 Functions in Endoplasmic Reticulum-Associated Degradation

被引：57

作者：

Blount, Jessica R. ^{[1
,2
]}

Burr, Aaron A. ^{[1
,2
,3
]}

Denuc, Amanda ^{[4
]}

Marfany, Gemma ^{[4
]}

Todi, Sokol V. ^{[1
,2
,3
]}

机构：

[1] Wayne State Univ, Sch Med, Dept Pharmacol, Detroit, MI 48201 USA

[2] Wayne State Univ, Sch Med, Dept Neurol, Detroit, MI 48201 USA

[3] Wayne State Univ, Sch Med, Grad Program Canc Biol, Detroit, MI USA

[4] Univ Barcelona, Fac Med, Dept Genet, Barcelona 7, Spain

来源：

PLOS ONE | 2012年 / 7卷 / 05期

基金：

美国国家卫生研究院;

关键词：

POLYGLUTAMINE DISEASE PROTEIN; DEUBIQUITINATING ENZYME ATAXIN-3; QUALITY-CONTROL; USP25; ERAD; RETROTRANSLOCATION; GENERATION; MUTATIONS; TURNOVER; VCP/P97;

D O I：

10.1371/journal.pone.0036542

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Endoplasmic Reticulum (ER)-associated degradation (ERAD) discards abnormal proteins synthesized in the ER. Through coordinated actions of ERAD components, misfolded/anomalous proteins are recognized, ubiquitinated, extracted from the ER and ultimately delivered to the proteasome for degradation. It is not well understood how ubiquitination of ERAD substrates is regulated. Here, we present evidence that the deubiquitinating enzyme Ubiquitin-Specific Protease 25 (USP25) is involved in ERAD. Our data support a model where USP25 counteracts ubiquitination of ERAD substrates by the ubiquitin ligase HRD1, rescuing them from degradation by the proteasome.

引用

页数：9

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