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  • Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity

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    VijayakumaranPUB2152.pdf (548.7Kb)
    Author(s)
    Vijayakumaran, Shamini
    Wong, Mathew B
    Antony, Helma
    Pountney, Dean L
    Griffith University Author(s)
    Pountney, Dean L.
    Wong, Mathew B.
    Vijayakumaran, Shamini
    Antony, Helma
    Year published
    2015
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    Abstract
    α-Synuclein inclusion bodies are a pathological hallmark of several neurodegenerative diseases, including Parkinson’s disease, and contain aggregated α-synuclein and a variety of recruited factors, including protein chaperones, proteasome components, ubiquitin and the small ubiquitin-like modifier, SUMO-1. Cell culture and animal model studies suggest that misfolded, aggregated α-synuclein is actively translocated via the cytoskeletal system to a region of the cell where other factors that help to lessen the toxic effects can also be recruited. SUMO-1 covalently conjugates to various intracellular target proteins in a way ...
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    α-Synuclein inclusion bodies are a pathological hallmark of several neurodegenerative diseases, including Parkinson’s disease, and contain aggregated α-synuclein and a variety of recruited factors, including protein chaperones, proteasome components, ubiquitin and the small ubiquitin-like modifier, SUMO-1. Cell culture and animal model studies suggest that misfolded, aggregated α-synuclein is actively translocated via the cytoskeletal system to a region of the cell where other factors that help to lessen the toxic effects can also be recruited. SUMO-1 covalently conjugates to various intracellular target proteins in a way analogous to ubiquitination to alter cellular distribution, function and metabolism and also plays an important role in a growing list of cellular pathways, including exosome secretion and apoptosis. Furthermore, SUMO-1 modified proteins have recently been linked to cell stress responses, such as oxidative stress response and heat shock response, with increased SUMOylation being neuroprotective in some cases. Several recent studies have linked SUMOylation to the ubiquitin-proteasome system, while other evidence implicates the lysosomal pathway. Other reports depict a direct mechanism whereby sumoylation reduced the aggregation tendency of α-synuclein, and reduced the toxicity. However, the precise role of SUMO-1 in neurodegeneration remains unclear. In this review, we explore the potential direct or indirect role(s) of SUMO-1 in the cellular response to misfolded α-synuclein in neurodegenerative disorders.
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    Journal Title
    Biomolecules
    Volume
    5
    Issue
    3
    DOI
    https://doi.org/10.3390/biom5031697
    Copyright Statement
    © 2015 by the authors; licensee MDPI, Basel, Switzerland. This is an open access article distributed under the Creative Commons Attribution License which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. (CC BY 4.0).
    Subject
    Medical Biochemistry and Metabolomics not elsewhere classified
    Biochemistry and Cell Biology
    Publication URI
    http://hdl.handle.net/10072/141774
    Collection
    • Journal articles

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