Sodium channel {beta}1 and {beta}3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain

doi:10.1083/jcb.200102086

Published 23 July 2001. doi:10.1083/jcb.200102086

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© The Rockefeller University Press, 0021-9525/2001/7/427 $5.00
The Journal of Cell Biology, Volume 154, Number 2, July 23, 2001 427-434

Article

Sodium channel ß1 and ß3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain

Charlotte F. Ratcliffe¹, Ruth E. Westenbroek¹, Rory Curtis² and William A. Catterall¹

¹ Department of Pharmacology, University of Washington, Seattle, WA 98195
² Millennium Pharmaceuticals, Cambridge, MA 02139

Address correspondence to William A. Catterall, Department of Pharmacology R-189, University of Washington, HSC, Box 357280, F-427, Seattle, WA 98195-7280. Tel.: (206) 543-1925. Fax: (206) 543-3882. E-mail: wcatt{at}u.washington.edu

Sequence homology predicts that the extracellular domain ofthe sodium channel ß1 subunit forms an immunoglobulin(Ig) fold and functions as a cell adhesion molecule. We showhere that ß1 subunits associate with neurofascin,a neuronal cell adhesion molecule that plays a key role in theassembly of nodes of Ranvier. The first Ig-like domain and secondfibronectin type III–like domain of neurofascin mediatethe interaction with the extracellular Ig-like domain of ß1,confirming the proposed function of this domain as a cell adhesionmolecule. ß1 subunits localize to nodes of Ranvierwith neurofascin in sciatic nerve axons, and ß1 andneurofascin are associated as early as postnatal day 5, duringthe period that nodes of Ranvier are forming. This associationof ß1 subunit extracellular domains with neurofascinin developing axons may facilitate recruitment and concentrationof sodium channel complexes at nodes of Ranvier.

Key Words: sodium channel; neurofascin; neural cell adhesion molecules; nodes of Ranvier; protein binding

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