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dc.contributor.authorVijayakumaran, Shamini
dc.contributor.authorWong, Mathew B
dc.contributor.authorAntony, Helma
dc.contributor.authorPountney, Dean L
dc.date.accessioned2018-01-12T12:31:24Z
dc.date.available2018-01-12T12:31:24Z
dc.date.issued2015
dc.identifier.issn2218-273X
dc.identifier.doi10.3390/biom5031697
dc.identifier.urihttp://hdl.handle.net/10072/141774
dc.description.abstractα-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.
dc.description.peerreviewedYes
dc.languageEnglish
dc.language.isoeng
dc.publisherM D P I AG
dc.relation.ispartofpagefrom1697
dc.relation.ispartofpageto1716
dc.relation.ispartofissue3
dc.relation.ispartofjournalBiomolecules
dc.relation.ispartofvolume5
dc.subject.fieldofresearchMedical Biochemistry and Metabolomics not elsewhere classified
dc.subject.fieldofresearchBiochemistry and Cell Biology
dc.subject.fieldofresearchcode110199
dc.subject.fieldofresearchcode0601
dc.titleDirect and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity
dc.typeJournal article
dc.type.descriptionC1 - Articles
dc.type.codeC - Journal Articles
dcterms.licensehttps://creativecommons.org/licenses/by/4.0/
dc.description.versionVersion of Record (VoR)
gro.facultyGriffith Health, School of Medical Science
gro.rights.copyright© 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).
gro.hasfulltextFull Text
gro.griffith.authorPountney, Dean L.
gro.griffith.authorWong, Mathew B.
gro.griffith.authorVijayakumaran, Shamini
gro.griffith.authorAntony, Helma


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