Journal
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR CELL RESEARCH
Volume 1823, Issue 10, Pages 1958-1966Publisher
ELSEVIER SCIENCE BV
DOI: 10.1016/j.bbamcr.2012.07.010
Keywords
SUMO-specific protease; SENP; SUMO; Heat shock; Activity-based probe
Categories
Funding
- Fundacao para a Ciencia e Tecnologia
- Fundo Europeu de Desenvolvimento Regional (FEDER) through COMPETE-Programa Operacional Factores de Competitividade (POFC) in the context of QREN, Portugal [PEst-C/SAU/LA0002/2011]
- Programa Operacional Potencial Humano (POPH) do QREN
- Fundo Social Europeu (FSE)
- POPH-QREN-Tipologia 4.2-Promocao do Emprego Cientifico
- Fundo Social Europeu
- MCTES
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Covalent conjugation of the small ubiquitin-like modifier (SUMO) to proteins is a highly dynamic and reversible process. Cells maintain a fine-tuned balance between SUMO conjugation and deconjugation. In response to stress stimuli such as heat shock, this balance is altered resulting in a dramatic increase in the levels of SUMO conjugates. Whether this reflects an activation of the conjugation cascade, a decrease in the activity of SUMO-specific proteases (SENPs), or both, remains unknown. Here, we show that from the five human SENPs detected in HeLa cells (SENP1/2/3/6/7) the activities of all but one (SENP6) were largely diminished after 30 min of heat shock. The decreased activity is not due to changes in their steady-state levels. Rather, in vitro experiments suggest that these SENPs are intrinsically heat-sensitive, a property most likely emerging from their catalytic domains. Heat shock inactivation seems to be a specific property of SENPs because numerous members of the related deubiquitinase family of cysteine proteases are not affected by this stress condition. Overall, our results suggest that SENPs are particularly sensitive to heat shock, a property that may be important for the adaptation of cells to this stress condition. (C) 2012 Elsevier B.V. All rights reserved.
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