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 4 2020
Accepted
20 5 2020
First published
12 6 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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