ArticleThe Journal of biological chemistry2026
Enzymatic basis of branching and extension of O-Man glycans for keratan sulfate biosynthesis.
Article in The Journal of biological chemistry, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Keratan Sulfate: An Electroconductive Glycosaminoglycan at the Interface of Sensory Perception and Neural Signaling.Journal of neuroscience research · 2026Review
- Branching of O-mannose glycans regulates node of Ranvier organization and saltatory conduction.Communications biology · 2026Article
- B3GNT7 regulates mucin glycosylation and protects against colitis and infection.bioRxiv : the preprint server for biology · 2026Article
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Authors and funding
8 authors.
Funding
Abstract
O-Mannose (Man) glycans are branched specifically in the brain by a dedicated glycosyltransferase, N-acetylglucosaminyltransferase IX (GnT-IX, also known as MGAT5B). Such branching of O-Man glycans was reported to be involved in diseases, including demyelination and glioma, but the enzymatic mechanisms by which O-Man glycan is specifically recognized by GnT-IX and how branched O-Man glycans are subsequently elongated by other enzymes in the brain have remained unclear. To shed light on these issues, we here first compared the structural model of GnT-IX complexed with its O-Man substrate with the crystal structure of the homologous N-glycan branching enzyme GnT-V (also known as MGAT5). Several residues in GnT-IX were predicted to be critical to recognition of the O-Man substrate, and an enzyme assay revealed that R304 in GnT-IX is crucial for the specificity toward O-Man glycans. We further investigated the role of O-Man branching for subsequent elongation in the brain and found that the level of keratan sulfate (KS) in O-Man glycans was significantly reduced in GnT-IX-knockout (KO) mouse brain, suggesting that O-Man branching promotes KS biosynthesis. Mechanistically, our enzymatic assays of the KS biosynthetic enzymes demonstrated that B4GALT1, B4GALT4, and CHST1 exhibited significantly higher activity toward branched O-Man glycans than toward their linear counterparts. These results imply that branching of O-Man glycans by GnT-IX provides the scaffold for efficient subsequent glycan elongation. Our findings deepen our understanding of the complex biosynthetic pathway of O-Man glycans in the brain.
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