Jump to main content
Jump to site search

Issue 15, 2016
Previous Article Next Article

Chemical and semisynthetic approaches to study and target deubiquitinases

Author affiliations

Abstract

Ubiquitination is a key posttranslational modification, which affects numerous biological processes and is reversed by a class of enzymes known as deubiquitinases (DUBs). This family of enzymes cleaves mono-ubiquitin or poly-ubiquitin chains from a target protein through different mechanisms and mode of interactions with their substrates. Studying the role of DUBs in health and diseases has been a major goal for many laboratories both in academia and in industry. However, the field has been challenged by the difficulties in obtaining native substrates and novel reagents using traditional enzymatic and molecular biology approaches. Recent advancements in the synthesis and semisynthesis of proteins made it possible to prepare several unique ubiquitin conjugates to study various aspects of DUBs such as their specificities and structures. Moreover, these approaches enable the preparation of novel activity based probes and assays to monitor DUB activities in vitro and in cellular contexts. Efforts made to bring new chemical entities for the selective inhibition of DUBs based on these tools are also highlighted with selected examples.

Graphical abstract: Chemical and semisynthetic approaches to study and target deubiquitinases

Back to tab navigation

Publication details

The article was received on 01 Feb 2016 and first published on 06 Apr 2016


Article type: Review Article
DOI: 10.1039/C6CS00083E
Chem. Soc. Rev., 2016,45, 4171-4198
  • Open access: Creative Commons BY license
  •   Request permissions

    Chemical and semisynthetic approaches to study and target deubiquitinases

    P. Gopinath, S. Ohayon, M. Nawatha and A. Brik, Chem. Soc. Rev., 2016, 45, 4171
    DOI: 10.1039/C6CS00083E

    This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. Material from this article can be used in other publications provided that the correct acknowledgement is given with the reproduced material.

    Reproduced material should be attributed as follows:

    • For reproduction of material from NJC:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the Centre National de la Recherche Scientifique (CNRS) and the RSC.
    • For reproduction of material from PCCP:
      [Original citation] - Published by the PCCP Owner Societies.
    • For reproduction of material from PPS:
      [Original citation] - Published by The Royal Society of Chemistry (RSC) on behalf of the European Society for Photobiology, the European Photochemistry Association, and RSC.
    • For reproduction of material from all other RSC journals:
      [Original citation] - Published by The Royal Society of Chemistry.

    Information about reproducing material from RSC articles with different licences is available on our Permission Requests page.

Search articles by author

Spotlight

Advertisements