ArticleProceedings of the National Academy of Sciences of the United States of America2025
O-GalNAc glycans are enriched in neuronal tracts and regulate nodes of Ranvier.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Deletion of Core 1 β3GalT-specific molecular chaperone (Cosmc) in murine intestinal epithelia leads to major alterations in glycocalyx and tumorigenesis.The Journal of biological chemistry · 2026Article
- ASGR2 and CLEC12A as Prognostically Relevant C-Type Lectin Hubs in Glioblastoma.International journal of molecular sciences · 2026Article
- GalNAc-T13 maintains neurite architecture and memory retention via O-GalNAc glycosylation of seizure protein 6.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Disrupted O-GalNAc glycosylation as a mechanism and biomarker ofbioRxiv : the preprint server for biology · 2026Article
- Glycosylation disorders in pediatric epilepsy: pathophysiology, imaging and precision therapy.Frontiers in neurology · 2026Review
- Review
- Abnormal O-glycan sialylation in the mPFC contributes to depressive-like behaviors in male mice.Science advances · 2025Article
- Neuromuscular Defects in aBiomolecules · 2025Article
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Authors and funding
4 authors.
Funding
Abstract
Protein O-glycosylation is a critical modification in the brain, as genetic variants in the pathway are associated with common and severe neuropsychiatric phenotypes. However, little is known about the most abundant O-glycans in the mammalian brain, which are N-acetylgalactosamine (O-GalNAc) linked. Here, we determined the spatial localization, protein carriers, and cellular function of O-GalNAc glycans in the mouse brain. We observed striking spatial enrichment of O-GalNAc glycans in neuronal tracts, and specifically at nodes of Ranvier, specialized structures involved in signal propagation in the brain. Glycoproteomic analysis revealed that more than half of the identified O-GalNAc glycans were present on chondroitin sulfate proteoglycans termed lecticans, and display both domain enrichment and regional heterogeneity. Inhibition of O-GalNAc synthesis in neurons reduced binding of Siglec-4, a known regulator of neurite growth, and shortened the length of nodes of Ranvier. This work establishes a function of O-GalNAc glycans in the brain and will inform future studies on their role in development and disease.
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