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KMID : 0624620220550070323
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BMB Reports
2022 Volume.55 No. 7 p.323 ~ p.335
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Role of post-translational modifications on the alpha-synuclein aggregation-related pathogenesis of Parkinson’s disease
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Yoo Ha-Jung
Lee Jeong-Min
Kim Bo-Kwang
Moon Hee-Chang
Jeong Hui-Su
Lee Kyung-Mi
Song Woo-Jeung
Hur Jun-Ho K.
Oh Yo-Han
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Abstract
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Together with neuronal loss, the existence of insoluble inclusions of alpha-synuclein (α-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 α-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 α-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 α-syn aggregation. Furthermore, the PTMs modulating α-syn aggregation-induced cell death have been discussed.
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KEYWORD
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Alpha-synuclein, Parkinson’s disease, Post-translational modification, Protein aggregation
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