ArticleNature chemical biology2017
Electrophilic probes for deciphering substrate recognition by O-GlcNAc transferase.
Article in Nature chemical biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed.
- Dissecting the Mechanisms Underlying Substrate Recognition and Functional Regulation of O-GlcNAc Cycling Enzymes.ACS chemical biology · 2025Review
- O-GlcNAc informatics: advances and trends.Analytical and bioanalytical chemistry · 2025Review
- OGT and OGA: Sweet guardians of the genome.The Journal of biological chemistry · 2024Review
- A cell-permeable probe for the labelling of a bacterial glycosyltransferase and virulence factor.RSC chemical biology · 2024Article
- Motif-dependent binding on the intervening domain regulates O-GlcNAc transferase.Nature chemical biology · 2023Article
- Promiscuous Enzymes for Residue-Specific Peptide and Protein Late-Stage Functionalization.Chembiochem : a European journal of chemical biology · 2023Review
- Systematic analysis of the impact of phosphorylation and O-GlcNAcylation on protein subcellular localization.Cell reports · 2023Article
- A novel binding site on the cryptic intervening domain is a motif-dependent regulator of O-GlcNAc transferase.Research square · 2023Article
- Genetically encoded chemical crosslinking of carbohydrate.Nature chemistry · 2023Article
- Inhibition of O-GlcNAc transferase sensitizes prostate cancer cells to docetaxel.Frontiers in oncology · 2022Article
- Cryo-EM structure provides insights into the dimer arrangement of the O-linked β-N-acetylglucosamine transferase OGT.Nature communications · 2021Article
- Advances in chemical probing of proteinChemical Society reviews · 2021Review
- OGT Protein Interaction Network (OGT-PIN): A Curated Database of Experimentally Identified Interaction Proteins of OGT.International journal of molecular sciences · 2021Article
- Protein Substrates Engage the Lumen of O-GlcNAc Transferase's Tetratricopeptide Repeat Domain in Different Ways.Biochemistry · 2021Article
- Overview of the Assays to ProbeMolecules (Basel, Switzerland) · 2021Review
- C-Terminal Tag Location Hampers in Vitro Profiling of OGT Peptide Substrates by mRNA Display.Chembiochem : a European journal of chemical biology · 2021Article
- Elucidating the protein substrate recognition of O-GlcNAc transferase (OGT) toward O-GlcNAcase (OGA) using a GlcNAc electrophilic probe.International journal of biological macromolecules · 2021Article
- Molecular Interrogation to Crack the Case of O-GlcNAc.Chemistry (Weinheim an der Bergstrasse, Germany) · 2020Review
- Identification of targets of AMPylating Fic enzymes by co-substrate-mediated covalent capture.Nature chemistry · 2020Article
- Targeted covalent inhibition of O-GlcNAc transferase in cells.Chemical communications (Cambridge, England) · 2019Article
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Authors and funding
12 authors.
Funding
Abstract
O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) is an essential human glycosyltransferase that adds O-GlcNAc modifications to numerous proteins. However, little is known about the mechanism with which OGT recognizes various protein substrates. Here we report on GlcNAc electrophilic probes (GEPs) to expedite the characterization of OGT-substrate recognition. Data from mass spectrometry, X-ray crystallization, and biochemical and radiolabeled kinetic assays support the application of GEPs to rapidly report the impacts of OGT mutations on protein substrate or sugar binding and to discover OGT residues crucial for protein recognition. Interestingly, we found that the same residues on the inner surface of the N-terminal domain contribute to OGT interactions with different protein substrates. By tuning reaction conditions, a GEP enables crosslinking of OGT with acceptor substrates in situ, affording a unique method to discover genuine substrates that weakly or transiently interact with OGT. Hence, GEPs provide new strategies to dissect OGT-substrate binding and recognition.
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Registered trials
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