ArticleJournal of the American Chemical Society2018
O-GlcNAc Transferase Recognizes Protein Substrates Using an Asparagine Ladder in the Tetratricopeptide Repeat (TPR) Superhelix.
Article in Journal of the American Chemical Society, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.
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Who cites it
54 citing papers in PubMed.
- Pathogenic O-GlcNAc dyshomeostasis is associated with cortical malformations and hyperactivity.eLife · 2026Article
- Revealing and Exploiting the Biochemistry ofBiochemistry · 2026Review
- OGT mediates O-GlcNAcylation of MEIS2 and affects palatal osteogenic development.International journal of oral science · 2026Article
- Understanding O-GlcNAc transferase (OGT): Every amino acid matters.The Journal of biological chemistry · 2025Review
- Protein O-GlcNAcylation in reproductive biology and the impact of metabolic disease.Human reproduction update · 2025Review
- O-linked β-N-acetylglucosamine (O-GlcNAc) modification: Emerging pathogenesis and a therapeutic target of diabetic nephropathy.Diabetic medicine : a journal of the British Diabetic Association · 2025Review
- Photoactivatable O-GlcNAc Transferase Library Enables Covalent Chemical Capture of Solvent-Exposed TPR Domain Interactions.Chembiochem : a European journal of chemical biology · 2025Article
- Article
- Identification of a Polypeptide Inhibitor ofJournal of the American Chemical Society · 2024Article
- O-GlcNAc transferase congenital disorder of glycosylation (OGT-CDG): Potential mechanistic targets revealed by evaluating the OGT interactome.The Journal of biological chemistry · 2024Review
- The non-catalytic domains of O-GlcNAc cycling enzymes present new opportunities for function-specific control.Current opinion in chemical biology · 2024Review
- Dissecting OGT's TPR domain to identify determinants of cellular function.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules.Journal of the American Chemical Society · 2024Article
- OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 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
- Phage display uncovers a sequence motif that drives polypeptide binding to a conserved regulatory exosite of O-GlcNAc transferase.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- An O-GlcNAc transferase pathogenic variant linked to intellectual disability affects pluripotent stem cell self-renewal.Disease models & mechanisms · 2023Article
- Extracellular arginine availability modulates eIF2α O-GlcNAcylation and heme oxygenase 1 translation for cellular homeostasis.Journal of biomedical science · 2023Article
- Chemoproteomic profiling of O-GlcNAcylated proteins and identification of O-GlcNAc transferases in rice.Plant biotechnology journal · 2023Article
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Authors and funding
6 authors.
Funding
Abstract
The essential mammalian enzyme O-GlcNAc Transferase (OGT) is uniquely responsible for transferring N-acetylglucosamine to over a thousand nuclear and cytoplasmic proteins, yet there is no known consensus sequence and it remains unclear how OGT recognizes its substrates. To address this question, we developed a protein microarray assay that chemoenzymatically labels de novo sites of glycosylation with biotin, allowing us to simultaneously assess OGT activity across >6000 human proteins. With this assay we examined the contribution to substrate selection of a conserved asparagine ladder within the lumen of OGT's superhelical tetratricopeptide repeat (TPR) domain. When five asparagines were mutated, OGT retained significant activity against short peptides, but showed limited limited glycosylation of protein substrates on the microarray. O-GlcNAcylation of protein substrates in cell extracts was also greatly attenuated. We conclude that OGT recognizes the majority of its substrates by binding them to the asparagine ladder in the TPR lumen proximal to the catalytic domain.
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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.