ArticleScience advances2024
An unusual dual sugar-binding lectin domain controls the substrate specificity of a mucin-type O-glycosyltransferase.
Article in Science advances, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 13 citations in OpenAlex.
- Social rank modulates empathic pain via Galntl6Molecular psychiatry · 2026Article
- Minimal Computational Framework for Systematic Identification of Antimicrobial Targets.bioRxiv : the preprint server for biology · 2026Article
- The Critical Role of GALNTs-Regulated O-GalNAc Glycosylation in Cancer Malignancy.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Review
- An in vitro approach for simulating divergent Golgi O-glycosylation of tumor-associated MUC1 from normal MUC1.Nature communications · 2026Article
- O-glycosylation in Cancer: Emerging Paradigms and Prospects for Precision Oncology.International journal of biological sciences · 2026Review
- A single catalytic domain residue regulates the substrate specificity of a mucin-type O-glycosyltransferase in salivary gland function.bioRxiv : the preprint server for biology · 2025Article
- Decoding the complex substrate specificities of GalNAc-Ts.Glycobiology · 2025Review
- Glycosylation in kidney diseases.Precision clinical medicine · 2025Review
- Rational Design of Dual-Domain Binding Inhibitors forJACS Au · 2024Article
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Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
N-acetylgalactosaminyl-transferases (GalNAc-Ts) initiate mucin-type O-glycosylation, an abundant and complex posttranslational modification that regulates host-microbe interactions, tissue development, and metabolism. GalNAc-Ts contain a lectin domain consisting of three homologous repeats (α, β, and γ), where α and β can potentially interact with O-GalNAc on substrates to enhance activity toward a nearby acceptor Thr/Ser. The ubiquitous isoenzyme GalNAc-T1 modulates heart development, immunity, and SARS-CoV-2 infectivity, but its substrates are largely unknown. Here, we show that both α and β in GalNAc-T1 uniquely orchestrate the O-glycosylation of various glycopeptide substrates. The α repeat directs O-glycosylation to acceptor sites carboxyl-terminal to an existing GalNAc, while the β repeat directs O-glycosylation to amino-terminal sites. In addition, GalNAc-T1 incorporates α and β into various substrate binding modes to cooperatively increase the specificity toward an acceptor site located between two existing O-glycans. Our studies highlight a unique mechanism by which dual lectin repeats expand substrate specificity and provide crucial information for identifying the biological substrates of GalNAc-T1.
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Registered trials
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