RNF220, an E3 ubiquitin ligase that targets Sin3B for ubiquitination

被引：36

作者：

Kong, Qinghua ^{[1
,2
]}

Zeng, Wanli ^{[1
,2
]}

Wu, Jingyang ^{[1
,2
]}

Hu, Wanling ^{[1
,2
]}

Li, Chaocui ^{[1
]}

Mao, Bingyu ^{[1
]}

机构：

[1] Chinese Acad Sci, Kunming Inst Zool, State Key Lab Genet Resources & Evolut, CAS Max Planck Jr Scientist Grp Dev Biol, Kunming 650223, Peoples R China

[2] Chinese Acad Sci, Grad Univ, Beijing 100049, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2010年 / 393卷 / 04期

基金：

中国国家自然科学基金;

关键词：

RNF220; Sin3B; E3; ligase; Ubiquitination; Degradation; HISTONE DEACETYLASE; GENE-EXPRESSION; DROSOPHILA SIN3; N-COR; COMPLEX; TRANSCRIPTION; COREPRESSOR; REPRESSION; REGULATOR; CHROMATIN;

D O I：

10.1016/j.bbrc.2010.02.066

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：

Modification of proteins by ubiquitination plays important roles in various cellular processes. During this process, the target specificity is determined by ubiquitin ligases. Here we identify RNF220 (RING finger protein 220) as a novel ubiquitin ligase for Sin3B. As a conserved RING protein, RNF220 can bind E2 and mediate auto-ubiquitination of itself. Through a yeast two-hybrid screen, we isolated Sin3B as one of its targets, which is a scaffold protein of the Sin3/HDAC (histone deacetylase) corepressor complex. RNF220 specifically interacts with Sin3B both in vitro and in vivo. Sin3B can be regulated by the ubiquitin-proteasome system. Co-expression of RNF220 promotes the ubiquitination and proteasomal degradation of Sin3B. Taken together, these results reveal a new mechanism for regulating the Sin3/HDAC complex. (C) 2010 Elsevier Inc. All rights reserved.

引用

页码：708 / 713

页数：6

共 29 条

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