Human Polycomb protein 2 promotes alpha-synuclein aggregate formation through covalent SUMOylation
- Authors
- Oh, Yohan; Kim, Yong Man; Mouradian, M. M; Chung, Kwang Chul
- Issue Date
- Mar-2011
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- alpha-Synuclein; Cell death; hPc2; Parkinson' s disease; Protein aggregation; SUMOylation
- Citation
- BRAIN RESEARCH, v.1381, pp.78 - 89
- Indexed
- SCIE
SCOPUS
- Journal Title
- BRAIN RESEARCH
- Volume
- 1381
- Start Page
- 78
- End Page
- 89
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/168810
- DOI
- 10.1016/j.brainres.2011.01.039
- ISSN
- 0006-8993
- Abstract
- 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.
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