Effects of α-Synuclein-associated post-translational modifications in Parkinson’s disease

Songzhe HE, Fushun WANG, Kin Lam Ken YUNG, Shiqing ZHANG, Shaogang QU

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37 Citations (Scopus)

Abstract

α-Synuclein (α-syn), a small highly conserved presynaptic protein containing 140 amino acids, is thought to be the main pathological hallmark in related neurodegenerative disorders. Although the normal function of α-syn is closely involved in the regulation of vesicular neurotransmission in these diseases, the underlying mechanisms of post-translational modifications (PTMs) of α-syn in the pathogenesis of Parkinson's disease (PD) have not been fully characterized. The pathological accumulation of misfolded α-syn has a critical role in PD pathogenesis. Recent studies of factors contributing to α-syn-associated aggregation and misfolding have expanded our understanding of the PD disease process. In this Review, we summarize the structure and physiological function of α-syn, and we further highlight the major PTMs (namely phosphorylation, ubiquitination, nitration, acetylation, truncation, SUMOylation, and O-GlcNAcylation) of α-syn and the effects of these modifications on α-syn aggregation, which may elucidate mechanisms for PD pathogenesis and lay a theoretical foundation for clinical treatment of PD. Copyright © 2021 American Chemical Society.

Original languageEnglish
Pages (from-to)1061-1071
JournalACS Chemical Neuroscience
Volume12
Issue number7
Early online dateMar 2021
DOIs
Publication statusPublished - Apr 2021

Citation

He, S., Wang, F., Yung, K. K. L., Zhang, S., & Qu, S. (2021). Effects of α-Synuclein-associated post-translational modifications in Parkinson’s disease. ACS Chemical Neuroscience, 12(7), 1061-1071. https://doi.org/10.1021/acschemneuro.1c00028

Keywords

  • α-Synuclein
  • Parkinson’s disease
  • Protein misfolding
  • Protein aggregation
  • Post-translational modifications
  • Neurodegenerative diseases

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