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- W2911335091 abstract "O-Linked N-acetylglucosamine (O-GlcNAc) is an abundant posttranslational monosaccaride-modification found on Ser or Thr residues of intracellular proteins in most eukaryotes. The dynamic nature of O-GlcNAc has enabled researchers to modulate the stoichiometry of O-GlcNAc on proteins in order to investigate its function. Cell permeable small moleculars have proven invaluable tools to increase O-GlcNAc levels. Herein, using in vitro substrate screening, we identified GlcNAcF3 as an OGT-accepted but OGA-resistant sugar mimic. Cellular experiments with cell-permeable peracetylated-GlcNAcF3 (Ac4GlcNAcF3) displayed that Ac4GlcNAcF3 was a potent tool to increase O-GlcNAc levels in several cell lines. Further, NIH3T3 cells interfered with OGT (siOGT) showed significant decreasing of O-GlcNAc levels with Ac4GlcNAcF3 treatment, indicating O-GlcNAcF3 was an OGT-dependent modification. In addition, cellular toxic assay confirmed O-GlcNAcF3 production has no significant effect on cell proliferation or viability. Thus, Ac4GlcNAcF3 represents a safe and dual regulator for both OGT and OGA, which will benefit the study of O-GlcNAc." @default.
- W2911335091 created "2019-02-21" @default.
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- W2911335091 date "2019-03-01" @default.
- W2911335091 modified "2023-10-16" @default.
- W2911335091 title "Ac4GlcNAcF3, an OGT-tolerated but OGA-resistant regulator for O-GlcNAcylation" @default.
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- W2911335091 doi "https://doi.org/10.1016/j.bmcl.2019.01.021" @default.
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