DeSUMOylating isopeptidase: a second class of SUMO protease

EMBO Rep. 2012 Apr;13(4):339-46. doi: 10.1038/embor.2012.3.

Abstract

The modification of proteins by small ubiquitin-like modifier (SUMO) is crucial for the regulation of diverse cellular processes. Protein SUMOylation is reversed by isopeptidases, collectively known as deSUMOylases. Only one family of SUMO-specific proteases has been described so far: the sentrin-specific proteases (SENP). Here, we identify and characterize a new deSUMOylase, which we have named DeSI-1 (DeSumoylating Isopeptidase 1). We describe BZEL—a new transcriptional repressor—as substrate of DeSI-1. DeSI-1 catalyses the deSUMOylation, but not the deubiquitination, of BZEL. Furthermore, the SENP substrates PML and ΔNp63 are not deSUMOylated by DeSI-1, suggesting that SENP and DeSI enzymes recognize different sets of substrates. Together, these data identify a second class of SUMO proteases.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Carbon-Nitrogen Lyases / chemistry
  • Carbon-Nitrogen Lyases / metabolism*
  • Cell Line
  • Endopeptidases / metabolism
  • Humans
  • Mice
  • Molecular Sequence Data
  • Protein Processing, Post-Translational
  • Recombinant Proteins / metabolism
  • Repressor Proteins / metabolism
  • Small Ubiquitin-Related Modifier Proteins / metabolism*
  • Substrate Specificity
  • Sumoylation*
  • Transcription, Genetic

Substances

  • Recombinant Proteins
  • Repressor Proteins
  • Small Ubiquitin-Related Modifier Proteins
  • Endopeptidases
  • Carbon-Nitrogen Lyases
  • deSumoylating Isopeptidase 1, mouse
  • isopeptidase