ArticleAngewandte Chemie (International ed. in English)2025
A Genetically Encoded Assay System to Quantify O-GlcNAc Transferase (OGT) Activity in Live Cells.
Article in Angewandte Chemie (International ed. in English), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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Who cites it
2 citing papers in PubMed.
- Chemical biology tools for the O-GlcNAc modification: Determining systems-level functions and druggability.Current opinion in chemical biology · 2026Review
- A Genetically Encoded Assay System to Quantify O-GlcNAc Transferase (OGT) Activity in Live Cells.Angewandte Chemie (International ed. in English) · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
Abstract
O-GlcNAc transferase (OGT) catalyzes O-GlcNAcylation of many nucleocytoplasmic proteins and plays important roles in regulating diverse cellular functions. Dysregulation of OGT is implicated in various diseases, including cancers and neurodegeneration. Despite its vital roles, little is known about how this enzyme is regulated within cells in part because no current assays directly report on its activity within cells. Here we describe a genetically encoded reporter of cellular OGT glycosyltransferase activity by exploiting the transferase-dependent proteolytic activity of OGT on host cell factor-1 (HCF-1). The reporter comprises sites at which OGT cleaves HCF-1, which are flanked by two different fluorescent proteins that are linked to either nuclear export or import sequences. OGT-catalyzed cleavage of this construct leads to separation and independent localization of these two fluorescent proteins. By quantifying their nuclear and cytoplasmic distributions, OGT activity can be measured. We validated this OGT cellular activity reporter (CAR) system using known modulators of the O-GlcNAc pathway and assessed the effects of several metabolites on OGT activity. Analyses of the dose- and time-dependent effects of these OGT modulators illustrate the sensitivity and precision of this OGT-CAR strategy. We envision this OGT-CAR system will aid in discovering and characterizing modifiers of OGT activity.
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Registered trials
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