Targeted Control of Protein O-GlcNAcylation in Living Cells

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ID: 329674
2026
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Abstract
Abstract O-linked N-acetylglucosamine glycosylation (O-GlcNAcylation) regulates many intracellular proteins, but linking a cellular phenotype to O-GlcNAcylation of a specific substrate remains difficult. Global perturbation of O-GlcNAc transferase (OGT) or O-GlcNAcase (OGA) changes many proteins at once and therefore provides limited information about individual substrates. Protein-selective approaches address this problem by directing OGT or OGA activity toward chosen proteins in living cells. Here, we review small-molecule recruiters, nanobody-based systems, inducible recruitment strategies, RNA aptamers, and complementary site-level approaches. We compare what each method can establish and the controls needed for interpretation, with particular attention to target engagement, target-protein O-GlcNAcylation, site assignment, selectivity, and functional validation. Together, these approaches provide increasingly direct ways to define how O-GlcNAcylation of individual proteins contributes to cellular function.
Reference Key
openalex_W7214206057 Use this key to autocite in the manuscript while using SciMatic Manuscript Manager or Thesis Manager
Authors Tongyang Xu, B. K.W. NG
Journal glycobiology
Year 2026
DOI
10.1093/glycob/cwag081
URL
https://doi.org/10.1093/glycob/cwag081
Keywords Keywords not found

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