ArticleInternational journal of biological macromolecules2021
Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe.
Article in International journal of biological macromolecules, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 18 citations in OpenAlex.
- O-GlcNAcylation: A molecular switch linking brain health to neurodegeneration.Neural regeneration research · 2026Article
- Dissecting the Mechanisms Underlying Substrate Recognition and Functional Regulation of O-GlcNAc Cycling Enzymes.ACS chemical biology · 2025Review
- Berberine treatment inhibits ferroptosis in NIT-1 murine pancreatic cell line via inhibiting OGT expression levels.Scientific reports · 2025Article
- Photoactivatable O-GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent-Exposed TPR Domain Interactions.Chembiochem : a European journal of chemical biology · 2025Article
- The non-catalytic domains of O-GlcNAc cycling enzymes present new opportunities for function-specific control.Current opinion in chemical biology · 2024Review
- CanPharmaceuticals (Basel, Switzerland) · 2024Review
- Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase.Nature chemical biology · 2023Article
- Cryo-EM structure of human O-GlcNAcylation enzyme pair OGT-OGA complex.Nature communications · 2023Article
- A novel binding site on the cryptic intervening domain is a motif-dependent regulator of O-GlcNAc transferase.Research square · 2023Article
- Review
- Tools, tactics and objectives to interrogate cellular roles of O-GlcNAc in disease.Nature chemical biology · 2022Review
- Truncation of the TPR domain of OGT alters substrate and glycosite selection.Analytical and bioanalytical chemistry · 2021Article
- Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.Biochemistry · 2021Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The essential human O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) is the sole enzyme responsible for modifying thousands of intracellular proteins with the monosaccharide O-GlcNAc. This unique modification plays crucial roles in human health and disease, but the substrate recognition of OGT remains poorly understood. Intriguingly, the only human enzyme reported to remove this modification, O-GlcNAcase (OGA), is O-GlcNAc modified. Here, we exploited a GlcNAc electrophilic probe (GEP1A) to rapidly screen OGT mutants in a fluorescence assay that can discriminate between altered OGT-sugar and -protein substrate binding to help elucidate the binding mode of OGT toward OGA protein substrate. Since OGT tetratricopeptide repeat (TPR) domain plays a key role in OGT-OGA binding, we screened 30 OGT TPR mutants, which revealed 15 "ladder like" asparagine or aspartate residues spanning TPRs 3-7 and 10-13.5 that affect OGA O-GlcNAcylation. By applying a truncated OGA construct, we found that OGA's N-terminal region or pseudo histone acetyltransferase domain is not required for its O-GlcNAcylation, suggesting OGT functionally interacts with OGA through its catalytic and/or stalk domains. This work represents the first effort to systemically investigate each OGT TPR and our findings will facilitate the development of new strategies to investigate the role of substrate-specific O-GlcNAcylation.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.