Post-translational modifications of Parkinson's disease-related proteins: Phosphorylation,SUMOylation and Ubiquitination |
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Authors: | Stella C. Junqueira Eduarda G.Z. Centeno Kevin A. Wilkinson Helena Cimarosti |
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Affiliation: | 1. Department of Pharmacology, Federal University of Santa Catarina, Florianopolis, Brazil;2. School of Biochemistry, Centre for Synaptic Plasticity, University of Bristol, Bristol, UK |
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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. |
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Keywords: | Correspondence to: K. A. Wilkinson, School of Biochemistry, Centre for Synaptic Plasticity, Biomedical Sciences Building, University of Bristol, Bristol BS8 1TD, UK. Parkinson's disease Phosphorylation Post-translational modifications SUMOylation Ubiquitination |
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