Post-translational modifications of Parkinson's disease-related proteins: Phosphorylation, SUMOylation and Ubiquitination

Biochim Biophys Acta Mol Basis Dis. 2019 Aug 1;1865(8):2001-2007. doi: 10.1016/j.bbadis.2018.10.025. Epub 2018 Nov 6.

Abstract

Parkinson's disease (PD) is a neurodegenerative disorder characterized by loss of dopaminergic neurons in the nigrostriatal pathway. The etiology of PD remains unclear and most cases are sporadic, however genetic mutations in more than 20 proteins have been shown to cause inherited forms of PD. Many of these proteins are linked to mitochondrial function, defects in which are a central characteristic of PD. Post-translational modifications (PTMs) allow rapid and reversible control over protein function. Largely focussing on mitochondrial dysfunction in PD, here we review findings on the PTMs phosphorylation, SUMOylation and ubiquitination that have been shown to affect PD-related proteins.

Keywords: Parkinson's disease; Phosphorylation; Post-translational modifications; SUMOylation; Ubiquitination.

Publication types

  • Review

MeSH terms

  • Animals
  • Humans
  • Parkinson Disease / metabolism*
  • Phosphorylation
  • Protein Processing, Post-Translational*
  • Proteins / analysis
  • Proteins / metabolism*
  • Proteolysis
  • Sumoylation
  • Ubiquitination

Substances

  • Proteins