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βIV-Spectrin Regulates Sodium Channel Clustering through Ankyrin-G at Axon Initial Segments and Nodes of Ranvier

Masayuki Komada and Philippe Soriano
The Journal of Cell Biology
Vol. 156, No. 2 (Jan. 21, 2002), pp. 337-348
Stable URL: http://www.jstor.org/stable/1620859
Page Count: 12
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βIV-Spectrin Regulates Sodium Channel Clustering through Ankyrin-G at Axon Initial Segments and Nodes of Ranvier
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Abstract

β-Spectrin and ankyrin are major components of the membrane cytoskeleton. We have generated mice carrying a null mutation in the βIV-spectrin gene using gene trapping in embryonic stem cells. Mice homozygous for the mutation exhibit tremors and contraction of hindlimbs. βIV-spectrin expression is mostly restricted to neurons, where it colocalizes with and binds to ankyrin-G at axon initial segments (AISs) and nodes of Ranvier (NR). In βIV-spectrin-null neurons, neither ankyrin-G nor voltage-gated sodium channels (VGSC) are correctly clustered at these sites, suggesting that impaired action potential caused by mislocalization of VGSC leads to the phenotype. Conversely, in ankyrin-G-null neurons, βIV-spectrin is not localized to these sites. These results indicate that βIV-spectrin and ankyrin-G mutually stabilize the membrane protein cluster and the linked membrane cytoskeleton at AIS and NR.

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