ArticleEMBO reports2021
CA10 regulates neurexin heparan sulfate addition via a direct binding in the secretory pathway.
Article in EMBO reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers, 1 of them a synthesis that pooled it.
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Who cites it
8 citing papers in PubMed, 1 synthesis or guideline pooled it, 12 citations in OpenAlex.
- Genome-wide meta-analysis conducted in three large biobanks expands the genetic landscape of lumbar disc herniations.Nature communications · 2024Pooled it
- Ternary Neurexin-T178-PTPR complexes represent a pre-synaptic core-module of neuronal synapse organization.Nature communications · 2026Article
- Synaptic Ca2+ channels and neurexins are linked through direct and indirect binding complexes.Scientific reports · 2026Article
- The Glycosaminoglycan-Dependent Interactome of Neurexin-1 in Human Fetal Glial Cells.Proteoglycan research · 2025Article
- Mapping the FGF2 Interactome Identifies a Functional Proteoglycan Coreceptor.ACS chemical biology · 2025Article
- Excavating proteoglycan structure-function relationships: modern approaches to capture the interactions of ancient biomolecules.American journal of physiology. Cell physiology · 2022Review
- CA10 regulates neurexin heparan sulfate addition via a direct binding in the secretory pathway.EMBO reports · 2021Article
- Expanding the Chondroitin Sulfate Glycoproteome - But How Far?Frontiers in cell and developmental biology · 2021Review
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Neurexins are presynaptic adhesion molecules that shape the molecular composition of synapses. Diversification of neurexins in numerous isoforms is believed to confer synapse-specific properties by engaging with distinct ligands. For example, a subset of neurexin molecules carry a heparan sulfate (HS) glycosaminoglycan that controls ligand binding, but how this post-translational modification is controlled is not known. Here, we observe that CA10, a ligand to neurexin in the secretory pathway, regulates neurexin-HS formation. CA10 is exclusively found on non-HS neurexin and CA10 expressed in neurons is sufficient to suppress HS addition and attenuate ligand binding and synapse formation induced by ligands known to recruit HS. This effect is mediated by a direct interaction in the secretory pathway that blocks the primary step of HS biosynthesis: xylosylation of the serine residue. NMR reveals that CA10 engages residues on either side of the serine that can be HS-modified, suggesting that CA10 sterically blocks xylosyltransferase access in Golgi. These results suggest a mechanism for the regulation of HS on neurexins and exemplify a new mechanism to regulate site-specific glycosylations.
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Registered trials
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