SUMOylation in α-Synuclein Homeostasis and Pathology

Frontiers in Aging Neuroscience
Mor Savyon, Simone Engelender

Abstract

The accumulation and aggregation of α-synuclein are central to Parkinson's disease (PD), yet the molecular mechanisms responsible for these events are not fully understood. Post-translational modifications of α-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 α-synuclein accumulation, aggregation and toxicity, and its possible implication in neurodegeneration that underlies PD.

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Citations

Jul 3, 2021·International Journal of Molecular Sciences·Antonella CardinaleBarbara Picconi
Jul 28, 2021·NPJ Parkinson's Disease·Luis M A OliveiraTiago F Outeiro

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Methods Mentioned

BETA
ubiquitination
acetylation
transgenic
GTPase
immunoprecipitation
confocal microscopy
immunoprecipitations
nuclear translocation
super-resolution microscopy

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Alpha-Synuclein Aggregation (MDS)

Alpha-synucleins are small proteins that are believed to restrict the mobility of synpatic vesicles and inhibit neurotransmitter release. Aggregation of these proteins have been linked to several types of neurodegenerative diseases including dementia with Lewy bodies and Parkinson's disease. Here is the latest research on α-synuclein aggregation.

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