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Mass spectrometry techniques for studying the ubiquitin system

Lookup NU author(s): Rachel Heap, Megan Gant, Frederic Lamoliatte, Dr Julien Peltier, Professor Matthias TrostORCiD


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© 2017 The Author(s). Post-translational control of proteins through covalent attachment of ubiquitin plays important roles in all eukaryotic cell functions. The ubiquitin system in humans consists of 2 E1, 35 E2 and >600 E3 ubiquitin ligases as well as hundreds of deubiquitylases, which reverse ubiquitin attachment. Moreover, there are hundreds of proteins with ubiquitin- binding domains that bind one of the eight possible polyubiquitin chains. Dysfunction of the ubiquitin system is associated with many diseases such as cancer, autoimmunity and neurodegeneration, demonstrating the importance of ubiquitylation. Therefore, enzymes of the ubiquitin system are considered highly attractive drug targets. In recent years, mass spectrometry (MS)-based techniques have become increasingly important in the deciphering of the ubiquitin system. This short review addresses the state-of-the-art MS techniques for the identification of ubiquitylated proteins and their ubiquitylation sites. We also discuss the identification and quantitation of ubiquitin chain topologies and highlight how the activity of enzymes in the ubiquitin pathway can be measured. Finally, we present current MS tools that can be used for drug discovery in the ubiquitin space.

Publication metadata

Author(s): Heap RE, Gant MS, Lamoliatte F, Peltier J, Trost M

Publication type: Review

Publication status: Published

Journal: Biochemical Society Transactions

Year: 2017

Volume: 45

Issue: 5

Pages: 1137-1148

Print publication date: 01/10/2017

Online publication date: 22/09/2017

Acceptance date: 10/08/2017

ISSN (print): 0300-5127

ISSN (electronic): 1470-8752

Publisher: Portland Press Ltd


DOI: 10.1042/BST20170091