Review Special Issues

SUMO modulation of protein aggregation and degradation

  • Received: 14 July 2015 Accepted: 30 August 2015 Published: 08 September 2015
  • Small ubiquitin-like modifier (SUMO) conjugation and binding to target proteins regulate a wide variety of cellular pathways. The functional aspects of SUMOylation include changes in protein-protein interactions, intracellular trafficking as well as protein aggregation and degradation. SUMO has also been linked to specialized cellular pathways such as neuronal development and synaptic transmission. In addition, SUMOylation is associated with neurological diseases associated with abnormal protein accumulations. SUMOylation of the amyloid and tau proteins involved in Alzheimer's disease and other tauopathies may contribute to changes in protein solubility and proteolytic processing. Similar events have been reported for α-synuclein aggregates found in Parkinson's disease, polyglutamine disorders such as Huntington's disease as well as protein aggregates found in amyotrophic lateral sclerosis (ALS). This review provides a detailed overview of the impact SUMOylation has on the etiology and pathology of these related neurological diseases.

    Citation: Marco Feligioni, Serena Marcelli, Erin Knock, Urooba Nadeem, Ottavio Arancio, Paul E. Fraser. SUMO modulation of protein aggregation and degradation[J]. AIMS Molecular Science, 2015, 2(4): 382-410. doi: 10.3934/molsci.2015.4.382

    Related Papers:

  • Small ubiquitin-like modifier (SUMO) conjugation and binding to target proteins regulate a wide variety of cellular pathways. The functional aspects of SUMOylation include changes in protein-protein interactions, intracellular trafficking as well as protein aggregation and degradation. SUMO has also been linked to specialized cellular pathways such as neuronal development and synaptic transmission. In addition, SUMOylation is associated with neurological diseases associated with abnormal protein accumulations. SUMOylation of the amyloid and tau proteins involved in Alzheimer's disease and other tauopathies may contribute to changes in protein solubility and proteolytic processing. Similar events have been reported for α-synuclein aggregates found in Parkinson's disease, polyglutamine disorders such as Huntington's disease as well as protein aggregates found in amyotrophic lateral sclerosis (ALS). This review provides a detailed overview of the impact SUMOylation has on the etiology and pathology of these related neurological diseases.


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