Neddylation positively regulates the ubiquitin E3 ligase activity of parkin

被引:42
|
作者
Um, Ji Won [1 ]
Han, Kyung Ah [1 ]
Im, Eunju [1 ]
Oh, Yohan [1 ]
Lee, Kyule [1 ]
Chung, Kwang Chul [1 ]
机构
[1] Yonsei Univ, Dept Syst Biol, Coll Life Sci & Biotechnol, Seoul 120749, South Korea
基金
新加坡国家研究基金会;
关键词
parkin; ubiquitin E3 ligase; NEDD8; neddylation; Parkinson's disease; LEWY-BODY FORMATION; NEDD8; MODIFICATION; PROTEIN LIGASE; CONJUGATING ENZYMES; S-NITROSYLATION; ALPHA-SYNUCLEIN; DISEASE; PHOSPHORYLATION; DEGRADATION; COMPLEX;
D O I
10.1002/jnr.22828
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
Mutations in the parkin gene underlie a familial form of Parkinson's disease known as autosomal recessive juvenile Parkinsonism (AR-JP). Dysfunction of parkin, a ubiquitin E3 ligase, has been implicated in the accumulation of ubiquitin proteasome system-destined substrates and eventually leads to cell death. However, regulation of parkin enzymatic activity is incompletely understood. Here we investigated whether the ubiquitin E3 ligase activity of parkin could be regulated by neddylation. We found that parkin could be a target of covalent modification with NEDD8, a ubiquitin-like posttranslational modifier. In addition, NEDD8 attachment caused an increase of parkin activity through the increased binding affinity for ubiquitin-conjugating E2 enzyme as well as the enhanced formation of the complex containing parkin and substrates. These findings point to the functional importance of NEDD8 and suggest that neddylation is one to the diverse modes of parkin regulation, potentially linking it to the pathogenesis of AR-JP. (C) 2012 Wiley Periodicals, Inc.
引用
收藏
页码:1030 / 1042
页数:13
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