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

Stella C Junqueira, Eduarda G Z Centeno, Kevin Wilkinson, Helena I Cimarosti

Research output: Contribution to journalArticle (Academic Journal)peer-review

14 Citations (Scopus)
132 Downloads (Pure)

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.

Original languageEnglish
Pages (from-to)2001-2007
Number of pages7
JournalBiochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Volume1865
Issue number8
Early online date6 Nov 2018
DOIs
Publication statusPublished - 1 Aug 2019

Keywords

  • Parkinson's disease
  • Phosphorylation
  • Post-translational modifications
  • SUMOylation
  • Ubiquitination

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