Chemical biology tools to study Deubiquitinases and Ubl proteases  

Magdalena Gorka, Helge Magnus Magnussen, Yogesh Kulathu (Lead / Corresponding author)

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Abstract

The reversible attachment of ubiquitin (Ub) and ubiquitin like modifiers (Ubls) to proteins are crucial post-translational modifications (PTMs)for many cellular processes. Not only do cells possess hundreds of ligases to mediate substrate specific modification with Ub and Ubls, but they also have a repertoire of more than 100 dedicated enzymes for the specific removal of ubiquitin (Deubiquitinases or DUBs) and Ubl modifications (Ubl-specific proteases or ULPs). Over the past two decades, there has been significant progress in our understanding of how DUBs and ULPs function ata molecular level and many novel DUBs and ULPs, including several new DUB classes, have been identified. Here, the development of chemical tools that can bind and trap active DUBs has played a key role. Since the introduction of the first activity-based probe for DUBs in 1986, several innovations have led to the development of more sophisticated tools to study DUBs and ULPs. In this review we discuss how chemical biology has led to the development of activity-based probes and substrates that have been invaluable to the study of DUBs and ULPs. We summarise our currently available toolbox, highlight the main achievements and give an outlook of how these tools may be applied to gain a better understanding of the regulatory mechanisms of DUBs and ULPs.
Original languageEnglish
Pages (from-to)86-96
Number of pages11
JournalSeminars in Cell & Developmental Biology
Volume132
Early online date22 Feb 2022
DOIs
Publication statusPublished - Dec 2022

Keywords

  • Activity-based protein profiling
  • Deubiquitinases
  • Posttranslational modification
  • Proteases
  • Signal transduction
  • UBL
  • Ubiquitin

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