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DeSUMOylating isopeptidase: a second class of SUMO protease
Author(s) -
Shin Eun Ju,
Shin Hyun Mi,
Nam Eori,
Kim Won Seog,
Kim JiHoon,
Oh ByungHa,
Yun Yungdae
Publication year - 2012
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2012.3
Subject(s) - protease , biology , microbiology and biotechnology , class (philosophy) , enzyme , biochemistry , computer science , artificial intelligence
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.