Issue 3, 2020

Tools for functional dissection of site-specific O-GlcNAcylation

Abstract

Protein O-GlcNAcylation is an abundant post-translational modification of intracellular proteins with the monosaccharide N-acetylglucosamine covalently tethered to serines and threonines. Modification of proteins with O-GlcNAc is required for metazoan embryo development and maintains cellular homeostasis through effects on transcription, signalling and stress response. While disruption of O-GlcNAc homeostasis can have detrimental impact on cell physiology and cause various diseases, little is known about the functions of individual O-GlcNAc sites. Most of the sites are modified sub-stoichiometrically which is a major challenge to the dissection of O-GlcNAc function. Here, we discuss the application, advantages and limitations of the currently available tools and technologies utilised to dissect the function of O-GlcNAc on individual proteins and sites in vitro and in vivo. Additionally, we provide a perspective on future developments required to decipher the protein- and site-specific roles of this essential sugar modification.

Graphical abstract: Tools for functional dissection of site-specific O-GlcNAcylation

Article information

Article type
Review Article
Submitted
25 apr 2020
Accepted
20 maj 2020
First published
12 jun 2020
This article is Open Access
Creative Commons BY license

RSC Chem. Biol., 2020,1, 98-109

Tools for functional dissection of site-specific O-GlcNAcylation

A. Gorelik and D. M. F. van Aalten, RSC Chem. Biol., 2020, 1, 98 DOI: 10.1039/D0CB00052C

This article is licensed under a Creative Commons Attribution 3.0 Unported Licence. You can use material from this article in other publications without requesting further permissions from the RSC, provided that the correct acknowledgement is given.

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