Zinc-finger UBPs: regulators of deubiquitylation.
Fiche publication
Date publication
août 2008
Auteurs
Membres identifiés du Cancéropôle Est :
Dr TORA Laszlo
Tous les auteurs :
Bonnet J, Romier C, Tora L, Devys D
Lien Pubmed
Résumé
Deubiquitylating enzymes have key regulatory roles in multiple cellular processes by mediating ubiquitin removal and processing. The ubiquitin-specific processing proteases (USPs) represent the largest subclass of deubiquitylases. Recently, several USPs that recognize the monoubiquitylated histones H2A and/or H2B have been identified. Among these enzymes, three USPs contain a zinc-finger ubiquitin-specific protease (ZnF-UBP) domain, indicating that this domain plays a crucial part in regulating their activity. To address the putative function of this domain, we systematically analysed and aligned yeast and human ZnF-UBP-containing proteins. By complementing our analysis with structural and functional data, we present a classification of the different ZnF-UBP-containing proteins and a model for their regulation.
Référence
Trends Biochem Sci. 2008 Aug;33(8):369-75