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Gliomedin Mediates Schwann Cell-Axon Interaction and the Molecular Assembly of the Nodes of Ranvier
Open accessAbstract
Accumulation of Na(+) channels at the nodes of Ranvier is a prerequisite for saltatory conduction. In peripheral nerves, clustering of these channels along the axolemma is regulated by myelinating Schwann cells through a yet unknown mechanism. We report the identification of gliomedin, a glial ligand for neurofascin and NrCAM, two axonal immunoglobulin cell adhesion molecules that are associated with Na+ channels at the nodes of Ranvier. Gliomedin is expressed by myelinating Schwann cells and accumulates at the edges of each myelin segment during development, where it aligns with the forming nodes. Eliminating the expression of gliomedin by RNAi, or the addition of a soluble extracellular domain of neurofascin to myelinating cultures, which caused the redistribution of gliomedin along the internodes, abolished node formation. Furthermore, a soluble gliomedin induced nodal-like clusters of Na+ channels in the absence of Schwann cells. We propose that gliomedin provides a glial cue for the formation of peripheral nodes of Ranvier.
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“Finally, the membranes of Schwann cell microvilli contain ligands for axonal cell adhesion molecules and contribute to sodium channel clustering at the nodes of Ranvier (Eshed et al., 2005).”
From SH3TC2, a protein mutant in Charcot–Marie–Tooth neuropathy, links peripheral nerve myelination to endosomal recycling (2010) · cites this paper as Eshed et al., 2005
In the citing paper
“In the PNS nodes, Schwann cell-derived type II transmembrane protein, glyomedin, is concentrated at the Schwann cell microvilli and induces the clustering of Na + channels at the PNS nodes via interaction with NF186 and NrCAM (Eshed et al., 2005).”
From The hyaluronan and proteoglycan link proteins: Organizers of the brain extracellular matrix and key molecules for neuronal function and plasticity (2015) · cites this paper as Eshed et al., 2005
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Metadata
- Authors
- Eshed, Y., Feinberg, K., Poliak, S., Sabanay, H., Sarig-Nadir, O., Spiegel, I., Bermingham, J. R., & Peles, E.
- Affiliations
- Weizmann Institute of Science (IL)
- McLaughlin Research Institute (US)
- Corresponding author
- Peles, Elior
- Venue
- Neuron
- Publisher
- Elsevier BV
- Published
- 2005-07
- Volume
- 47
- Issue
- 2
- Pages
- 215-229
- ISSN
- 0896-6273 (ISSN-L)
- OpenAlex
- W2017281603
- Cited by
- 321
- References
- 70
- Citations by year
- 2026: 4 · 2025: 8 · 2024: 12 · 2023: 8 · 2022: 10 · 2021: 15 · 2020: 13 · 2019: 13 · 2018: 12 · 2017: 16 · 2016: 10 · 2015: 15 · 2014: 27 · 2013: 16 · 2012: 17
- FWCI
- 9.51
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 2974 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Neuron (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Institutes of Health
- National Institute of Neurological Disorders and Stroke (NS50220)
- National Multiple Sclerosis Society (RG3594-A-4)
- Topics
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Nerve injury and regeneration
- Life Sciences › Neuroscience › Developmental Neuroscience › Neurogenesis and neuroplasticity mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Keywords
- Schwann cells, nodes of Ranvier, sodium channel clustering, saltatory conduction, neurofascin, NrCAM, axon-glia interaction, myelination, peripheral nervous system development, myelin
- MeSH terms
- Ezrin, Age Factors, Amino Acid Sequence, Animals, Axons, Cell Compartmentation, Cells, Cultured, Chlorocebus aethiops, Cloning, Molecular, Cytoskeletal Proteins, Myelin Basic Protein, Fluorescent Antibody Technique, Ganglia, Spinal, Humans, Membrane Proteins, Microfilament Proteins, S100 Proteins, Phosphoproteins, Protein Binding, Ranvier's Nodes, Schwann Cells, Sciatic Nerve, Spectrin, Transfection, Blotting, Northern, Blotting, Western, Sodium Channels, Cell Adhesion Molecules, Cell Adhesion Molecules, Neuronal, Microscopy, Immunoelectron, Neurofilament Proteins, Protein Structure, Tertiary, Ankyrins, Receptors, Peptide, Gene Expression Regulation, Developmental, Myelin-Associated Glycoprotein, Macromolecular Substances, Rats, Claudins
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