Next Article in Journal
Pre-mRNA Splicing in Plants: In Vivo Functions of RNA-Binding Proteins Implicated in the Splicing Process
Next Article in Special Issue
Αlpha-Synuclein as a Mediator in the Interplay between Aging and Parkinson’s Disease
Previous Article in Journal
Galectin Binding to Neo-Glycoproteins: LacDiNAc Conjugated BSA as Ligand for Human Galectin-3
Previous Article in Special Issue
Toxic Oligomeric Alpha-Synuclein Variants Present in Human Parkinson’s Disease Brains Are Differentially Generated in Mammalian Cell Models
Article Menu

Export Article

Open AccessReview
Biomolecules 2015, 5(3), 1697-1716; doi:10.3390/biom5031697

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

Menzies Health Institute Queensland, School of Medical Science, Griffith University, Gold Coast, Queensland 4222, Australia
*
Author to whom correspondence should be addressed.
Academic Editor: Stephan N. Witt
Received: 28 May 2015 / Revised: 3 July 2015 / Accepted: 9 July 2015 / Published: 24 July 2015
View Full-Text   |   Download PDF [2675 KB, uploaded 24 July 2015]   |  

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 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. View Full-Text
Keywords: alpha-synuclein; Parkinson’s disease; SUMO; multiple system atrophy; neurodegeneration; autophagy alpha-synuclein; Parkinson’s disease; SUMO; multiple system atrophy; neurodegeneration; autophagy
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).

Scifeed alert for new publications

Never miss any articles matching your research from any publisher
  • Get alerts for new papers matching your research
  • Find out the new papers from selected authors
  • Updated daily for 49'000+ journals and 6000+ publishers
  • Define your Scifeed now

SciFeed Share & Cite This Article

MDPI and ACS Style

Vijayakumaran, S.; Wong, M.B.; Antony, H.; Pountney, D.L. Direct and/or Indirect Roles for SUMO in Modulating Alpha-Synuclein Toxicity. Biomolecules 2015, 5, 1697-1716.

Show more citation formats Show less citations formats

Related Articles

Article Metrics

Article Access Statistics

1

Comments

[Return to top]
Biomolecules EISSN 2218-273X Published by MDPI AG, Basel, Switzerland RSS E-Mail Table of Contents Alert
Back to Top