Tools for functional dissection of site-specific O-GlcNAcylation

Andrii Gorelik, Daan van Aalten (Lead / Corresponding author)

Research output: Contribution to journalArticle

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.
Original languageEnglish
Number of pages12
JournalRSC Chemical Biology
Early online date12 Jun 2020
DOIs
Publication statusE-pub ahead of print - 12 Jun 2020

Fingerprint Dive into the research topics of 'Tools for functional dissection of site-specific <i>O</i>-GlcNAcylation'. Together they form a unique fingerprint.

  • Projects

    Cite this