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Zinc-finger UBPs: regulators of deubiquitylation.

Abstract : 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.
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https://www.hal.inserm.fr/inserm-00311071
Contributor : Maité Peney <>
Submitted on : Tuesday, August 12, 2008 - 4:32:20 PM
Last modification on : Thursday, April 23, 2020 - 2:26:26 PM

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Jacques Bonnet, Christophe Romier, László Tora, Didier Devys. Zinc-finger UBPs: regulators of deubiquitylation.. Trends in Biochemical Sciences, Elsevier, 2008, 33 (8), pp.369-75. ⟨10.1016/j.tibs.2008.05.005⟩. ⟨inserm-00311071⟩

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