Genetic Code Expansion Approaches to Decipher the Ubiquitin Code


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Date

2024-10-23

Publication Type

Review Article

ETH Bibliography

yes

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Data

Abstract

The covalent attachment of Ub (ubiquitin) to target proteins (ubiquitylation) represents one of the most versatile PTMs (post-translational modifications) in eukaryotic cells. Substrate modifications range from a single Ub moiety being attached to a target protein to complex Ub chains that can also contain Ubls (Ub-like proteins). Ubiquitylation plays pivotal roles in most aspects of eukaryotic biology, and cells dedicate an orchestrated arsenal of enzymes to install, translate, and reverse these modifications. The entirety of this complex system is coined the Ub code. Deciphering the Ub code is challenging due to the difficulty in reconstituting enzymatic machineries and generating defined Ub/Ubl-protein conjugates. This Review provides a comprehensive overview of recent advances in using GCE (genetic code expansion) techniques to study the Ub code. We highlight strategies to site-specifically ubiquitylate target proteins and discuss their advantages and disadvantages, as well as their various applications. Additionally, we review the potential of small chemical PTMs targeting Ub/Ubls and present GCE-based approaches to study this additional layer of complexity. Furthermore, we explore methods that rely on GCE to develop tools to probe interactors of the Ub system and offer insights into how future GCE-based tools could help unravel the complexity of the Ub code.

Publication status

published

Editor

Book title

Volume

124 (20)

Pages / Article No.

11544 - 11584

Publisher

American Chemical Society

Event

Edition / version

Methods

Software

Geographic location

Date collected

Date created

Subject

Organisational unit

09740 - Lang, Kathrin / Lang, Kathrin check_circle

Notes

Funding

101003289 - Development of a chemical biology toolbox for deciphering the ubiquitin code (EC)

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