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DeSUMOylating enzymes—SENPs
Author(s) -
Drag Marcin,
Salvesen Guy S.
Publication year - 2008
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.113
Subject(s) - deubiquitinating enzyme , ubiquitin , nedd8 , proteases , sumo enzymes , enzyme , biochemistry , function (biology) , chemistry , biology , microbiology and biotechnology , ubiquitin ligase , gene
Modification of proteins by ubiquitin and SUMO ( s mall u biquitin‐like mo difiers) is a dynamic and reversible process. Similar to the ubiquitin pathway, where the action of deubiquitinating enzymes removes ubiquitin from ubiquitin‐adducts, SUMO is also removed intact from its substrates by proteases belonging to the sen trin‐specific p roteases (SENPs) family. In addition to their isopeptidase activity, SENPs also execute another essential function as endopeptidases by removing the short C‐terminal extension from immature SUMOs. The defining characteristics of SENPs are their predicted conserved molecular scaffold—defined as members of peptidase Clan CE, conserved catalytic mechanism, and their reported activity on SUMO or Nedd8 conjugated proteins (or the respective precursors). We discuss recent progress on the human SENPs and their substrates. © 2008 IUBMB IUBMB Life, 60(11): 734–742, 2008