Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson's diseaseopen access
- Authors
- Yoo, Hajung; Lee, Jeongmin; Kim, Bokwang; Moon, Heechang; Jeong, Huisu; Lee, Kyungmi; Song, Woo Jeung; Hur, Junho K.; Oh, Yohan
- Issue Date
- Jul-2022
- Publisher
- KOREAN SOCIETY BIOCHEMISTRY & MOLECULAR BIOLOGY
- Keywords
- Alpha-synuclein; Parkinson’s disease; Post-translational modification; Protein aggregation
- Citation
- BMB REPORTS, v.55, no.7, pp.323 - 335
- Indexed
- SCIE
SCOPUS
KCI
- Journal Title
- BMB REPORTS
- Volume
- 55
- Number
- 7
- Start Page
- 323
- End Page
- 335
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/171582
- DOI
- 10.5483/BMBRep.2022.55.7.073
- ISSN
- 1976-6696
- Abstract
- Together with neuronal loss, the existence of insoluble inclusions of alpha-synuclein (alpha-syn) in the brain is widely accepted as a hallmark of synucleinopathies including Parkinson's disease (PD), multiple system atrophy, and dementia with Lewy body. Because the alpha-syn aggregates are deeply involved in the pathogenesis, there have been many attempts to demonstrate the mechanism of the aggregation and its potential causative factors including post-translational modifications (PTMs). Although no concrete conclusions have been made based on the previous study results, growing evidence suggests that modifications such as phosphorylation and ubiquitination can alter alpha-syn characteristics to have certain effects on the aggregation process in PD; either facilitating or inhibiting fibrillization. In the present work, we reviewed studies showing the significant impacts of PTMs on alpha-syn aggregation. Furthermore, the PTMs modulating alpha-syn aggregation-induced cell death have been discussed.
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