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Sodium channel β1 and β3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain

Open access
Ratcliffe, Charlotte F., Westenbroek, Ruth E., Curtis, Rory, Catterall, William A.·2001·The Journal of Cell Biology

Abstract

Sequence homology predicts that the extracellular domain of the sodium channel β1 subunit forms an immunoglobulin (Ig) fold and functions as a cell adhesion molecule. We show here that β1 subunits associate with neurofascin, a neuronal cell adhesion molecule that plays a key role in the assembly of nodes of Ranvier. The first Ig-like domain and second fibronectin type III–like domain of neurofascin mediate the interaction with the extracellular Ig-like domain of β1, confirming the proposed function of this domain as a cell adhesion molecule. β1 subunits localize to nodes of Ranvier with neurofascin in sciatic nerve axons, and β1 and neurofascin are associated as early as postnatal day 5, during the period that nodes of Ranvier are forming. This association of β1 subunit extracellular domains with neurofascin in developing axons may facilitate recruitment and concentration of sodium channel complexes at nodes of Ranvier.

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Metadata

Authors
Ratcliffe, C. F., Westenbroek, R. E., Curtis, R., & Catterall, W. A.
Venue
The Journal of Cell Biology
Published
2001-07-23
Volume
154
Issue
2
Pages
427-434
ISSN
  • 0021-9525 (ISSN-L)
  • 1540-8140
OpenAlex
W2057888827
Cited by
173
References
2
FWCI
4.23
Type
journal article
Language
en
Open access
bronze

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CoChat. (2026). Citation check: Sodium channel β1 and β3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain. https://app.cochat.ai/papers/10.1083/jcb.200102086
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Ratcliffe, C. F., Westenbroek, R. E., Curtis, R., & Catterall, W. A. (2001). Sodium channel β1 and β3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain. The Journal of Cell Biology. https://doi.org/10.1083/jcb.200102086

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Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.