Zinc-finger UBPs: regulators of deubiquitylation.

Jacques Bonnet, Christophe Romier, László Tora, Didier Devys

Department of Functional Genomics, Institut de Génétique et de Biologie Moléculaire et Cellulaire, CNRS UMR 7104, INSERM U 596, Université Louis Pasteur de Strasbourg, ILLKIRCH Cedex, CU de Strasbourg, France.

Trends in biochemical sciences 2008 Aug

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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.

Citation

Jacques Bonnet, Christophe Romier, László Tora, Didier Devys. Zinc-finger UBPs: regulators of deubiquitylation. Trends in biochemical sciences. 2008 Aug;33(8):369-75