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. 2023 May 10;8:196. doi: 10.1038/s41392-023-01442-3

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© The Author(s) 2023

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 1 — The effect of glucose on OGT and O-GlcNAcylation. GlcNAc is an O-β-N-acetylglucosamine moiety attached to a nuclear protein, cytoplasmic protein serine, or threonine residue. The addition of GlcNAc to proteins is catalyzed by OGT, while its removal is catalyzed by OGA. Currently, several pathways have been proposed that implicate O-GlcNAcylated proteins in the link between tumorigenesis and hyperglycemia. O-GlcNAcylation stabilizes SP1, β-catenin and YAP proteins promoting expression of target genes and transcriptional activity of NF-kB pathway. O-GlcNAc O-β-N-acetylglucosamine, OGT O-GlcNAc transferase, OGA O-GlcNAcase, SP1 Specificity protein 1, YAP Yes-associated protein