Tools for functional dissection of site-specific O-GlcNAcylation

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

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    20 Citations (Scopus)
    113 Downloads (Pure)


    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
    Pages (from-to)98-109
    Number of pages12
    JournalRSC Chemical Biology
    Issue number3
    Early online date12 Jun 2020
    Publication statusPublished - 1 Aug 2020


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