Heat shock induces a massive but differential inactivation of SUMO-specific proteases

• Type: Article in International Scientific Journal
• Date: 2012

Authors

Manuel P Pinto (Author) Other; Andreia F Carvalho (Author) Other; Claudia P Grou (Author) Other; Jose E Rodriguez Borges (Author) FCUP; Clara Sa Miranda (Author) Other; Jorge E Azevedo (Author) ICBAS

Journal

Title: Biochimica et Biophysica Acta - Molecular Cell Research

Vol. 1823

Pages: 1958-1966

ISSN: 0167-4889

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 37 Citations

Scopus - 37 Citations

Scientific classification

FOS: Natural sciences > Biological sciences

Other information

Authenticus ID: P-002-4Y8

DOI: 10.1016/j.bbamcr.2012.07.010

Abstract (EN): 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 9