During the last decade, SUMOylation has emerged as a central regulatory post-translational modification in the control of the fate and function of proteins. However, how SUMOylation is regulated itself has just started to be delineated. It appears now that SUMO (small ubiquitin-related modifier) conjugation/deconjugation equilibrium is affected by various environmental stresses, including osmotic, hypoxic, heat, oxidative and genotoxic stresses. This regulation occurs either at the level of individual targets, through an interplay between stress-induced phosphorylation and SUMOylation, or via modulation of the conjugation/deconjugation machinery abundance or activity. The present review gives an overview of the connections between stress and SUMOylation, the underlying molecular mechanisms and their effects on cellular functions.
SUMO under stress
Tempe, D.; Piechaczyk, M.; Bossis, G.
Biochem Soc Trans
2008-10 / vol 36 / pages 874-8
Humans; Animals; Signal Transduction/physiology; *Protein Processing, Post-Translational; Small Ubiquitin-Related Modifier Proteins/*metabolism; *Oxidative Stress