ArticleThe Journal of biological chemistry2011
Fibronectin type III-like domains of neurofascin-186 protein mediate gliomedin binding and its clustering at the developing nodes of Ranvier.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed.
- Identification of GLDNInternational journal of oral science · 2026Article
- Unveiling proteomic and peptide-level modifications in cerebrospinal fluid and plasma in normal cognitive aging.Communications medicine · 2025Article
- Anti-pan-neurofascin antibodies induce subclass-related complement activation and nodo-paranodal damage.Brain : a journal of neurology · 2023Article
- Concussion leads to widespread axonal sodium channel loss and disruption of the node of Ranvier.Acta neuropathologica · 2022Article
- Lethal Congenital Contracture Syndrome 11: A Case Report and Literature Review.Journal of clinical medicine · 2022Article
- Article
- Mechanisms of node of Ranvier assembly.Nature reviews. Neuroscience · 2021Review
- Impact of Neurofascin on Chronic Inflammatory Demyelinating PolyneuropathyFrontiers in molecular neuroscience · 2021Review
- Latrophilin's Social Protein Network.Frontiers in neuroscience · 2019Review
- Article
- Autoantibodies Against the Node of Ranvier in Seropositive Chronic Inflammatory Demyelinating Polyneuropathy: Diagnostic, Pathogenic, and Therapeutic Relevance.Frontiers in immunology · 2018Review
- Mutations in GLDN, Encoding Gliomedin, a Critical Component of the Nodes of Ranvier, Are Responsible for Lethal Arthrogryposis.American journal of human genetics · 2016Article
- Mechanisms of sodium channel clustering and its influence on axonal impulse conduction.Cellular and molecular life sciences : CMLS · 2016Review
- The Nodes of Ranvier: Molecular Assembly and Maintenance.Cold Spring Harbor perspectives in biology · 2015Review
- The olfactomedin domain from gliomedin is a β-propeller with unique structural properties.The Journal of biological chemistry · 2015Article
- Perlecan is recruited by dystroglycan to nodes of Ranvier and binds the clustering molecule gliomedin.The Journal of cell biology · 2015Article
- Inhibitory axons are targeted in hippocampal cell culture by anti-Caspr2 autoantibodies associated with limbic encephalitis.Frontiers in cellular neuroscience · 2015Article
- Molecular Details of Olfactomedin Domains Provide Pathway to Structure-Function Studies.PloS one · 2015Article
- Expression, purification, crystallization and preliminary X-ray crystallographic analysis of the extracellular olfactomedin domain of gliomedin.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Long-term maintenance of Na+ channels at nodes of Ranvier depends on glial contact mediated by gliomedin and NrCAM.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
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4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The cell adhesion molecules (CAMs) of the immunoglobulin superfamily (Ig-CAMs) play a crucial role in the organization of the node of Ranvier in myelinated axons. In the peripheral nervous system, Gliomedin (Gldn) secreted by Schwann cell microvilli binds NgCAM-related CAM (NrCAM) and Neurofascin-186 (NF186) and direct the nodal clustering of voltage-gated sodium channels (Nav). NF186 is the single axonal Gldn partner to ensure Nav clustering at nodes, whereas NrCAM is only required in glial cells (Feinberg, K., Eshed-Eisenbach, Y., Frechter, S., Amor, V., Salomon, D., Sabanay, H., Dupree, J. L., Grumet, M., Brophy, P. J., Shrager, P., and Peles, E. (2010) Neuron 65, 490-502). The olfactomedin domain of Gldn is implicated in the interaction with nodal Ig-CAMs. However, the interacting modules of NrCAM or NF186 involved in Gldn association are unknown. Here, we report that fibronectin type III-like (FnIII) domains of both Ig-CAMs mediate their interaction with Gldn in pulldown and cell binding assays. Using surface plasmon resonance assays, we determined that NrCAM and NF186 display similar affinity constant for their association with Gldn (K(D) of 0.9 and 5.7 nm, respectively). We characterized the FnIII domains 1 and 2 of NF186 as interacting modules that ensure association with Gldn. We found that the soluble FnIII domains of NF186 (FnIII-Fc) bind on Schwann cells and inhibit Gldn and Nav clustering at heminodes, the precursors of mature nodes in myelinating cultures. Our study reveals the unexpected importance of FnIII domains of Ig-CAMs in the organization of nodes of Ranvier in peripheral axons. Thus, NF186 utilizes distinct modules to organize the multimeric nodal complex.
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