期刊
IUBMB LIFE
卷 66, 期 2, 页码 71-77出版社
WILEY
DOI: 10.1002/iub.1244
关键词
cell death; cell stress; proteases; SUMO; SENP; cell survival; posttranslational modification
资金
- European Research Council
- MRC
- BBSRC
- Biotechnology and Biological Sciences Research Council [BB/K014366/1] Funding Source: researchfish
- Medical Research Council [G0601810, MR/L003791/1] Funding Source: researchfish
- BBSRC [BB/K014366/1] Funding Source: UKRI
- MRC [G0601810, MR/L003791/1] Funding Source: UKRI
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. (c) 2014 IUBMB Life, 66(2):71-77, 2014
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