ArticleThe Journal of biological chemistry2011
Lectin domains of polypeptide GalNAc transferases exhibit glycopeptide binding specificity.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed.
- An in vitro approach for simulating divergent Golgi O-glycosylation of tumor-associated MUC1 from normal MUC1.Nature communications · 2026Article
- Multiplexed Detection of Autoantibodies to Glycopeptides Using Microarray.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Rational Design of Dual-Domain Binding Inhibitors forJACS Au · 2024Article
- Pathogenesis of IgA nephropathy: Omics data inform glycomedicine.Nephrology (Carlton, Vic.) · 2024Article
- Targeting host O-linked glycan biosynthesis affects Ebola virus replication efficiency and reveals differential GalNAc-T acceptor site preferences on the Ebola virus glycoprotein.Journal of virology · 2024Article
- An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.Science advances · 2024Article
- Molecular Recognition of GalNAc in Mucin-Type O-Glycosylation.Accounts of chemical research · 2023Review
- Polypeptide N-acetylgalactosamine transferase 3: a post-translational writer on human health.Journal of molecular medicine (Berlin, Germany) · 2022Review
- Atomic and Specificity Details of Mucin 1JACS Au · 2022Article
- Quantitative assessment of successive carbohydrate additions to the clustered O-glycosylation sites of IgA1 by glycosyltransferases.Glycobiology · 2021Article
- Review
- Mucin-Type O-GalNAc Glycosylation in Health and Disease.Advances in experimental medicine and biology · 2021Article
- The Role of APPBiomolecules · 2020Review
- IgA1 hinge-region clustered glycan fidelity is established early during semi-ordered glycosylation by GalNAc-T2.Glycobiology · 2019Article
- Polypeptide GalNAc-Ts: from redundancy to specificity.Current opinion in structural biology · 2019Review
- A strategy for generating cancer-specific monoclonal antibodies to aberrant O-glycoproteins: identification of a novel dysadherin-Tn antibody.Glycobiology · 2019Article
- Structural and Mechanistic Insights into the Catalytic-Domain-Mediated Short-Range Glycosylation Preferences of GalNAc-T4.ACS central science · 2018Article
- The interdomain flexible linker of the polypeptide GalNAc transferases dictates their long-range glycosylation preferences.Nature communications · 2017Article
- Structure and functional impact of seed region variant in MIR-499 gene family in bronchial asthma.Respiratory research · 2017Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
UDP-GalNAc:polypeptide α-N-acetylgalactosaminyltransferases (GalNAc-Ts) constitute a family of up to 20 transferases that initiate mucin-type O-glycosylation. The transferases are structurally composed of catalytic and lectin domains. Two modes have been identified for the selection of glycosylation sites by GalNAc-Ts: confined sequence recognition by the catalytic domain alone, and concerted recognition of acceptor sites and adjacent GalNAc-glycosylated sites by the catalytic and lectin domains, respectively. Thus far, only the catalytic domain has been shown to have peptide sequence specificity, whereas the primary function of the lectin domain is to increase affinity to previously glycosylated substrates. Whether the lectin domain also has peptide sequence selectivity has remained unclear. Using a glycopeptide array with a library of synthetic and recombinant glycopeptides based on sequences of mucins MUC1, MUC2, MUC4, MUC5AC, MUC6, and MUC7 as well as a random glycopeptide bead library, we examined the binding properties of four different lectin domains. The lectin domains of GalNAc-T1, -T2, -T3, and -T4 bound different subsets of small glycopeptides. These results indicate an additional level of complexity in the initiation step of O-glycosylation by GalNAc-Ts.
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