Wrestling with stress: roles of protein SUMOylation and deSUMOylation in cell stress response

Chun Guo, Jeremy M Henley

Research output: Contribution to journalArticle (Academic Journal)peer-review

83 Citations (Scopus)


How cell fate is determined following extreme stress is a core question in cell biology. This is particularly important in the brain where neuronal death following ischemic stroke is a major cause of disability. Over the last few years it has emerged that the SUMOylation status of an increasing number of substrate proteins plays a crucial role in cellular responses to environmental and metabolic stress. SUMOylation is a post-translational modification in which the 97-residue protein, SUMO (Small Ubiquitin-related MOdifier) is covalently attached to specific lysine residues in a target protein. Despite being covalent, it is a highly transient modification because of the actions of deSUMOylation enzymes, so SUMO conjugation acts as a rapidly reversible switch that can promote or inhibit protein interactions with the substrate protein. Overall, it appears that increased SUMOylation represents a cellular protective response. Here we discuss recent progress toward understanding the mechanisms, pathways, and roles of SUMOylation during and after severe metabolic stress.

Original languageEnglish
Pages (from-to)71-7
Number of pages7
JournalIUBMB Life
Issue number2
Publication statusPublished - Feb 2014

Bibliographical note

© 2014 International Union of Biochemistry and Molecular Biology.


  • Cell Death
  • Cell Survival
  • Humans
  • Protein Processing, Post-Translational
  • Protein Transport
  • SUMO-1 Protein
  • Signal Transduction
  • Stress, Physiological
  • Sumoylation


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