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

• Tipo: Artigo em Revista Científica Internacional
• Data: 2012

Autores

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

Revista

Título: Biochimica et Biophysica Acta - Molecular Cell Research

Vol. 1823

Páginas: 1958-1966

ISSN: 0167-4889

Editora: Elsevier

Indexação

ISI Web of Knowledge - 37 Citações

Scopus - 37 Citações

Classificação Científica

FOS: Ciências exactas e naturais > Ciências biológicas

Outras Informações

ID Authenticus: 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.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 9