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 language | English |
|---|---|
| Pages (from-to) | 2001-2007 |
| Number of pages | 7 |
| Journal | Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease |
| Volume | 1865 |
| Issue number | 8 |
| Early online date | 6 Nov 2018 |
| DOIs | |
| Publication status | Published - 1 Aug 2019 |
Keywords
- Parkinson's disease
- Phosphorylation
- Post-translational modifications
- SUMOylation
- Ubiquitination
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