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

Citation
Cf. Ratcliffe et al., Sodium channel beta 1 and beta 3 subunits associate with neurofascin through their extracellular immunoglobulin-like domain, J CELL BIOL, 154(2), 2001, pp. 427-434
Citations number
32
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Cell & Developmental Biology
Journal title
JOURNAL OF CELL BIOLOGY
ISSN journal
0021-9525 → ACNP
Volume
154
Issue
2
Year of publication
2001
Pages
427 - 434
Database
ISI
SICI code
0021-9525(20010723)154:2<427:SCB1AB>2.0.ZU;2-L
Abstract
Sequence homology predicts that the extracellular domain of the sodium chan nel beta1 subunit forms an immunoglobulin (Ig) fold and functions as a cell adhesion molecule. We show here that beta1 subunits associate with neurofa scin, a neuronal cell adhesion molecule that plays a key role in the assemb ly of nodes of Ranvier. The first Ig-like domain and second fibronectin typ e III-like domain of neurofascin mediate the interaction with the extracell ular Ig-like domain of beta1, confirming the proposed function of this doma in as a cell adhesion molecule. beta1 subunits localize to nodes of Ranvier with neurofascin in sciatic nerve axons, and beta1 and neurofascin are ass ociated as early as postnatal day 5, during the period that nodes of Ranvie r are forming. This association of beta1 subunit extracellular domains with neurofascin in developing axons may facilitate recruitment and concentrati on of sodium channel complexes at nodes of Ranvier.