SUMO under stress.
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.
Tempé
Denis
D
Institut de Génétique Moléculaire de Montpellier, CNRS, UMR 5535, IFR 122, 1919 Route de Mende, Montpellier F-34293, France.
Piechaczyk
Marc
M
Bossis
Guillaume
G
D000818:Animals; D006801:Humans; D018384:Oxidative Stress; D011499:Protein Processing, Post-Translational; D015398:Signal Transduction / Q000502:physiology; D025841:Small Ubiquitin-Related Modifier Proteins / Q000378:metabolism*
D025841:Small Ubiquitin-Related Modifier Proteins