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Article Dans Une Revue Biochemical Journal Année : 2009

Characterization of SENP7, a SUMO-2/3-specific isopeptidase

Marie-Claude Geoffroy
Ellis G. Jaffray
  • Fonction : Auteur
Ronald T. Hay
  • Fonction : Auteur

Résumé

The modification of proteins by SUMO (small ubiquitinrelated modifier) plays important roles in regulating the activity, stability and cellular localization of target proteins. Similar to ubiquitination, SUMO modification is a dynamic process that can be reversed by SENPs [SUMO-1/sentrin/SMT3 (suppressor of mif two 3 homologue 1)-specific peptidases]. To date, six SENPs have been discovered in humans, although knowledge of their regulation, specificity and biological functions is limited. In the present study, we report that SENP7 has a restricted substrate specificity, being unable to process SUMO precursors and displaying paralogue-specific isopeptidase activity. The C-terminal catalytic domain of SENP7 efficiently depolymerized poly-SUMO-2 chains but had undetectable activity against poly-SUMO-1 chains. SENP7 also displayed isopeptidase activity against di-SUMO-2-and SUMO-2-modified RanGAP1 (Ran GTPase-activating protein 1) but had limited activity against SUMO-1-modified RanGAP1. In vivo, full-length SENP7 was localized to the nucleoplasm and preferentially reduced the accumulation of high-molecular-mass conjugates of SUMO-2 and SUMO-3 compared with SUMO-1. Small interfering RNAmediated ablation of SENP7 expression led to the accumulation of high-molecular-mass SUMO-2 species and to the accumulation of promyelocytic leukaemia protein in subnuclear bodies. These findings suggest that SENP7 acts as a SUMO-2/3-specific protease that is likely to regulate the metabolism of poly-SUMO-2/3 rather than SUMO-1 conjugation in vivo.

Dates et versions

hal-03082511 , version 1 (18-10-2022)

Identifiants

Citer

Lin Nan Shen, Marie-Claude Geoffroy, Ellis G. Jaffray, Ronald T. Hay. Characterization of SENP7, a SUMO-2/3-specific isopeptidase. Biochemical Journal, 2009, 421 (2), pp.223 - 230. ⟨10.1042/bj20090246⟩. ⟨hal-03082511⟩

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