Sumoylation: implications for neurodegenerative diseases

Dina Anderson, Camila A. Zanella, Jeremy Henley, Helena Cimarosti

Research output: Chapter in Book/Report/Conference proceedingChapter in a book

43 Citations (Scopus)


The covalent posttranslational modifications of proteins are critical events in signaling cascades that enable cells to efficiently, rapidly and reversibly respond to extracellular stimuli. This is especially important in the CNS where the processes affecting synaptic communication between neurons are highly complex and very tightly regulated. Sumoylation regulates the function and fate of a diverse array of proteins and participates in the complex cell signaling pathways required for cell survival. One of the most complex signaling pathways is synaptic transmission.
Correct synaptic function is critical to the working of the brain and its alteration through synaptic plasticity mediates learning, mental disorders and stroke. The investigation of neuronal sumoylation is a new and exciting field and the functional and pathophysiological implications are far-reaching. Sumoylation has already been implicated in a diverse array of neurological disorders. Here we provide an overview of current literature highlighting recent insights into the role of sumoylation in neurodegeneration. In addition we present a brief assessment of drug discovery in the analogous ubiquitin system and extrapolate on the potential for development of novel therapies that might target SUMO-associated mechanisms of neurodegenerative disease.
Original languageEnglish
Title of host publicationSUMO regulation of cellular processes
Number of pages21
ISBN (Electronic)9783319500447
Publication statusPublished - 15 Feb 2017

Publication series

NameAdvances in experimental medicine and biology
ISSN (Print)0065-2598


  • Alzheimer’s disease
  • Amyotrophic lateral sclerosis
  • Ischemia
  • Neuronal intranuclear inclusion disease
  • Parkinson's disease
  • Polyglutamine diseases
  • Drug targets


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