期刊
BRAIN RESEARCH
卷 1381, 期 -, 页码 78-89出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/j.brainres.2011.01.039
关键词
alpha-Synuclein; Cell death; hPc2; Parkinson's disease; Protein aggregation; SUMOylation
资金
- Ministry of Education, Science and Technology (MEST), Republic of Korea [2009K-001251]
- National Research Foundation of Korea (NRF) [2010-0018916]
- Ministry for Health, Welfare & Family Affairs, Republic of Korea [A092004]
- MEST [2010-0001668]
Parkinson's disease (PD) manifests from the impairment of motor systems due to the specific loss of dopaminergic neurons and the appearance of intracellular filamentous inclusions called Lewy bodies (LBs). alpha-Synuclein, a major component of LBs, is known to contribute to the pathogenesis of PD. Although alpha-synuclein is known to be a target of diverse posttranslational modifications, the contribution of alpha-synuclein SUMOylation and its functional consequences have not yet been fully characterized. Here, we demonstrate that human Polycomb protein 2 (hPc2) binds to alpha-synuclein and may function as a SUMO E3 ligase to promote the SUMOylation of alpha-synuclein. In addition, hPc2 promotes the SUMOylation of alpha-synuclein in the presence of MG-132-induced proteasome inhibition, which consequently promotes alpha-synuclein aggregate formation. Furthermore, the increased formation of intracellular alpha-synuclein aggregates, which predominantly contain SUMOylated alpha-synuclein, significantly reduces the death of fibroblast cells in response to staurosporine. In summary, the results from this study demonstrate that the hPc2-induced SUMOylation of alpha-synuclein could function as a cytoprotector by increasing alpha-synuclein aggregate formation within fibroblast cells. (C) 2011 Elsevier B.V. All rights reserved.
作者
我是这篇论文的作者
点击您的名字以认领此论文并将其添加到您的个人资料中。
推荐
暂无数据