Cell Biology

Wrestling with Heat Shock

See allHide authors and affiliations

Science  05 Jun 2009:
Vol. 324, Issue 5932, pp. 1243
DOI: 10.1126/science.324_1243c

Golebiowski et al. have conducted a comprehensive large-scale analysis of protein SUMOylation. Small ubiquitin-like modifier (SUMO) proteins, when covalently attached to target proteins, can alter properties such as the cellular localization, activity, or stability of the targets. By combining an affinity-tagging isolation method with sensitive mass spectrometry detection, the authors obtained a glimpse of 766 proteins that experienced increased or decreased SUMOylation in cells exposed to the stress of heat shock (a temperature increase from 37° to 43°C). Three-quarters of these proteins had not been identified previously as targets of SUMOylation. These proteins provide clues to the extent of the biological processes that are altered by heat shock—from DNA repair and protein folding to cell death and cell cycle control. Furthermore, this regulatory mechanism operates quickly, within 5 min, although reversal of SUMOylation was generally slower, taking up to 2 hours—and for those proteins that underwent deconjugation in response to stress, an even longer recovery time was needed for re-SUMOylation.

Sci. Signal. 2, ra24 (2009).

Navigate This Article