Cited by 321Nerve injury and regenerationNeurogenesis and neuroplasticity mechanismsIon channel regulation and function

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Gliomedin Mediates Schwann Cell-Axon Interaction and the Molecular Assembly of the Nodes of Ranvier

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Eshed, Yael, Feinberg, Konstantin, Poliak, Sebastian, Sabanay, Helena, Sarig-Nadir, Offra, Spiegel, Ivo, Bermingham, John R., Peles, Elior·2005·Neuron

DOI 10.1016/j.neuron.2005.06.026

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Abstract

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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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
ORCID: Feinberg, Konstantin
Spiegel, Ivo
Bermingham, John R.
Peles, Elior
Venue: Neuron
Publisher: Elsevier BV
Published: 2005-07
Volume: 47
Issue: 2
Pages: 215-229
ISSN: 0896-6273 (ISSN-L)
DOI: 10.1016/j.neuron.2005.06.026
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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Gliomedin Mediates Schwann Cell-Axon Interaction and the Molecular Assembly of the Nodes of Ranvier

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