Deubiquitinating Enzymes: Their Functions and Substrate Specificity

Citations Over TimeTop 10% of 2004 papers

Abstract

Conjugation of one or more molecules of ubiquitin to target proteins can signify one of several fates, including degradation by the 26S proteasome, or trafficking via the secretory or endocytic pathways. Whereas much attention in recent years has focussed on the mechanisms of forming these different ubiquitin conjugates, far less is known about the removal of ubiquitin, which is performed by deubiquitinating enzymes (DUBs). While it has been appreciated for some 10 years that DUBs constitute large gene families in eukaryotes, and known for much longer that ubiquitination is a reversible process, information on the exact role of DUBs has been slow in coming. This review will attempt to summarise results from the last few years that shows that DUBs are an essential regulatory step of both protein degradation by the proteasome, and of other ubiquitin-dependent processes, by virtue of their ability to regulate protein ubiquitination in a target-specific manner.

Related Papers

• → Proteasome subunit Rpn13 is a novel ubiquitin receptor(2008)654 cited
• → Multiple Associated Proteins Regulate Proteasome Structure and Function(2002)640 cited
• → The Ubiquitin Conjugating Enzyme: An Important Ubiquitin Transfer Platform in Ubiquitin-Proteasome System(2020)165 cited
• → Deubiquitinating Enzymes: Their Functions and Substrate Specificity(2004)59 cited
• → Ubiquitin-Proteasome System for Controlling Cellular Protein Levels(2006)