Effects of α-Synuclein-Associated Post-Translational Modifications in Parkinson's Disease

Songzhe He, Fushun Wang, Kin Lam YUNG, Shiqing ZHANG, Shaogang Qu*

*Corresponding author for this work

Research output: Contribution to journalReview articlepeer-review

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.

Original languageEnglish
Pages (from-to)1061-1071
Number of pages11
JournalACS Chemical Neuroscience
Volume12
Issue number7
DOIs
Publication statusPublished - 7 Apr 2021

Scopus Subject Areas

  • Biochemistry
  • Physiology
  • Cognitive Neuroscience
  • Cell Biology

User-Defined Keywords

  • neurodegenerative diseases
  • Parkinson's disease
  • post-translational modifications
  • protein aggregation
  • protein misfolding
  • α-Synuclein

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