Proteasome inhibition induces alpha-synuclein SUMOylation and aggregate formation
- Authors
- Kim, Yong Man; Jang, Won Hee; Quezado, Martha M; Oh, Yohan; Chung, Kwang Chul; Junn, Eunsung; Mouradian, M. M
- Issue Date
- Aug-2011
- Publisher
- ELSEVIER SCIENCE BV
- Keywords
- Parkinson' s disease; Dementia with Lewy Bodies; alpha-Synuclein; SUMOylation; Protein aggregation; Proteasome
- Citation
- JOURNAL OF THE NEUROLOGICAL SCIENCES, v.307, no.1-2, pp.157 - 161
- Indexed
- SCIE
SCOPUS
- Journal Title
- JOURNAL OF THE NEUROLOGICAL SCIENCES
- Volume
- 307
- Number
- 1-2
- Start Page
- 157
- End Page
- 161
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/167751
- DOI
- 10.1016/j.jns.2011.04.015
- ISSN
- 0022-510X
- Abstract
- Parkinson's disease (PD) and Dementia with Lewy Bodies (DLB) are characterized pathologically by intraneuronal inclusions called Lewy bodies (LBs) and Lewy neurites. A major component of these inclusions is the protein a-synuclein, which is natively unfolded but forms oligomers and insoluble fibrillar aggregates under pathological conditions. Although alpha-synuclein is known to undergo several posttranslational modifications, the contribution of SUMOylation to alpha-synuclein aggregation and the pathogenesis of alpha-synucleinopathies have not been elucidated. Here, we provide evidence that aggregates and inclusions formed as a result of impaired proteasome activity contain SUMOylated alpha-synuclein. Additionally, SUMO1 is present in the halo of LBs colocalizing with alpha-synuclein in the brains of PD and DLB patients. Interestingly. SUMOylation does not affect the ubiquitination of alpha-synuclein. These findings suggest that proteasomal dysfunction results in the accumulation of SUMOylated alpha-synuclein and subsequently its aggregation, pointing to the contribution of this posttranslational modification to the pathogenesis of inclusion formation in alpha-synucleinopathies.
- Files in This Item
-
Go to Link
- Appears in
Collections - 서울 의생명공학전문대학원 > 서울 의생명과학과 > 1. Journal Articles
Items in ScholarWorks are protected by copyright, with all rights reserved, unless otherwise indicated.