Deubiquitinating enzymes: Their functions and substrate specificity

Tatiana A. Soboleva, Rohan T. Baker*

*Corresponding author for this work

    Research output: Contribution to journalReview articlepeer-review

    51 Citations (Scopus)

    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.

    Original languageEnglish
    Pages (from-to)191-200
    Number of pages10
    JournalCurrent Protein and Peptide Science
    Volume5
    Issue number3
    DOIs
    Publication statusPublished - Jun 2004

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