Journal
FRONTIERS IN AGING NEUROSCIENCE
Volume 12, Issue -, Pages -Publisher
FRONTIERS MEDIA SA
DOI: 10.3389/fnagi.2020.00167
Keywords
Parkinson's disease; alpha-synuclein; post-translational modifications; SUMOylation; ubiquitination; protein aggregation
Categories
Funding
- Israel Academy of Sciences
- Allen and Jewel Prince Center for Neurodegenerative Disorders of the Brain
- Technion Research Funds
- Dears Foundation for Neurodegenerative Diseases
- Isidore C. and Penny W. Myers Fund for Parkinson's Research
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The accumulation and aggregation of alpha-synuclein are central to Parkinson's disease (PD), yet the molecular mechanisms responsible for these events are not fully understood. Post-translational modifications of alpha-synuclein regulate several of its properties, including degradation, interaction with proteins and membranes, aggregation and toxicity. SUMOylation is a post-translational modification involved in various nuclear and extranuclear processes, such as subcellular protein targeting, mitochondrial fission and synaptic plasticity. Protein SUMOylation increases in response to several stressful situations, from viral infections to trauma. In this framework, an increasing amount of evidence has implicated SUMOylation in several neurodegenerative diseases, including PD. This review will discuss recent findings in the role of SUMOylation as a regulator of alpha-synuclein accumulation, aggregation and toxicity, and its possible implication in neurodegeneration that underlies PD.
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