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Activity‐based probes for the ubiquitin conjugation–deconjugation machinery: new chemistries, new tools, and new insights

Identifieur interne : 000851 ( Ncbi/Checkpoint ); précédent : 000850; suivant : 000852

Activity‐based probes for the ubiquitin conjugation–deconjugation machinery: new chemistries, new tools, and new insights

Auteurs : David S. Hewings ; John A. Flygare ; Matthew Bogyo ; Ingrid E. Wertz

Source :

The Febs Journal [ 1742-464X ] ; 2017.

RBID : PMC:7163952

Abstract

The reversible post‐translational modification of proteins by ubiquitin and ubiquitin‐like proteins regulates almost all cellular processes, by affecting protein degradation, localization, and complex formation. Deubiquitinases (DUBs) are proteases that remove ubiquitin modifications or cleave ubiquitin chains. Most DUBs are cysteine proteases, which makes them well suited for study by activity‐based probes. These DUB probes report on deubiquitinase activity by reacting covalently with the active site in an enzyme‐catalyzed manner. They have proven to be important tools to study DUB selectivity and proteolytic activity in different settings, to identify novel DUBs, and to characterize deubiquitinase inhibitors. Inspired by the efficacy of activity‐based probes for DUBs, several groups have recently reported probes for the ubiquitin conjugation machinery (E1, E2, and E3 enzymes). Many of these enzymes, while not proteases, also posses active site cysteine residues and can be targeted by covalent probes. In this review, we will discuss how features of the probe (cysteine‐reactive group, recognition element, and reporter tag) affect reactivity and suitability for certain experimental applications. We will also review the diverse applications of the current probes, and discuss the need for new probe types to study emerging aspects of ubiquitin biology.

Url:

http://www.ncbi.nlm.nih.gov/pmc/articles/PMC7163952

DOI: 10.1111/febs.14039
PubMed: 28196299
PubMed Central: 7163952

Affiliations:

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PMC:7163952

Le document en format XML

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Activity‐based probes for the ubiquitin conjugation–deconjugation machinery: new chemistries, new tools, and new insights

Activity‐based probes for the ubiquitin conjugation–deconjugation machinery: new chemistries, new tools, and new insights

Source :

Abstract

Links toward previous steps (curation, corpus...)

Links to Exploration step

Le document en format XML

Pour manipuler ce document sous Unix (Dilib)

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Pour générer des pages wiki