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AIMS Molecular Science

2015, Volume 2, Issue 4: 382-410. doi: 10.3934/molsci.2015.4.382
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SUMO modulation of protein aggregation and degradation

  • 1.
    Laboratory of Synaptic Plasticity, EBRI Rita Levi-Montalcini Foundation, Via del Fosso di Fiorano 64/65, Rome 00143, Italy;
  • 2.
    Department of Physiology and Pharmacology, Sapienza University of Rome, Rome, 00185, Italy;
  • 3.
    Tanz Centre for Research in Neurodegenerative Diseases, University of Toronto, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada;
  • 4.
    Department of Pathology and Cell Biology and Taub Institute for Research on Alzheimer's Disease and the Aging Brain, Columbia University, 630 W 168th St., New York, NY 10032, USA;
  • 5.
    Department of Medical Biophysics, University of Toronto, 60 Leonard Avenue, Toronto, Ontario M5T 2S8, Canada
  • 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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