Wrestling with stress: roles of protein SUMOylation and deSUMOylation in cell stress response.
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.
School of Biochemistry, Medical Sciences Building, University of Bristol, University Walk, Bristol, BS8 1TD, UK.
Chun
C
Guo
Jeremy M
JM
Henley
D016923:Cell Death / Q000235:genetics; D002470:Cell Survival / Q000235:genetics; D006801:Humans; D011499:Protein Processing, Post-Translational; D021381:Protein Transport / Q000235:genetics; D025842:SUMO-1 Protein / Q000235:genetics* / Q000378:metabolism; D015398:Signal Transduction / Q000235:genetics*; D013312:Stress, Physiological / Q000235:genetics*; D058207:Sumoylation / Q000235:genetics*
D025842:SUMO-1 Protein
SENP; SUMO; cell death; cell stress; cell survival; posttranslational modification; proteases