PPPDE1 is a novel deubiquitinase belonging to a cysteine isopeptidase family

被引：20

作者：

Xie, Xingwang ^{[1
,2
]}

Wang, Xueyan ^{[1
]}

Jiang, Dong ^{[3
]}

Wang, Jianghua ^{[1
]}

Fei, Ran ^{[1
]}

Cong, Xu ^{[1
]}

Wei, Lai ^{[1
]}

Wang, Yu ^{[2
]}

Chen, Hongsong ^{[1
]}

机构：

[1] Peking Univ, Hepatol Inst, Beijing Key Lab Hepatitis & Immunotherapy Liver D, Peking Univ Peoples Hosp, Beijing 100044, Peoples R China

[2] Chinese Ctr Dis Control & Prevent, Beijing 102206, Peoples R China

[3] Capital Med Univ, Beijing Ditan Hosp, Inst Infect Dis, Beijing Key Lab Emerging Infect Dis, Beijing 100015, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2017年 / 488卷 / 02期

基金：

北京市自然科学基金; 中国国家自然科学基金;

关键词：

Cysteine isopeptidase; Deubiquitinase; DUBs; PPPDE1; RPS7; UBIQUITINATION; PROTEIN; CYLD; P53; ACTIVATION;

D O I：

10.1016/j.bbrc.2017.04.161

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：

Ubiquitinlation of proteins is prevalent and important in both normal and pathological cellular processes. Deubiquitinating enzymes (DUBs) can remove the ubiquitin tags on substrate proteins and dynamically regulate the ubiquitination process. The PPPDE family proteins were predicted to be a novel class of deubiquitinating peptidase, but this has not yet been experimentally proved. Here we validated the deubiquitinating activity of PPPDE1 and revealed its isopeptidase activity against ubiquitin conjugated through Lys 48 and Lys 63. We also identified ribosomal protein S7, RPS7, as a substrate protein of PPPDE1. Moreover, PPPDE1 could mediate the ubiquitin chain editing of RPS7, deubiquitinating Lys 48 linked ubiquitination, and finally stabilize RPS7 proteins. Taken together, we report that PPPDE1 is a novel deubiquitinase that belongs to a cysteine isopeptidase family. (C) 2017 Elsevier Inc. All rights reserved.

引用

页码：291 / 296

页数：6

共 33 条

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