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• W1978553600 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." @default.
• W1978553600 created "2016-06-24" @default.
• W1978553600 creator A5021183543 @default.
• W1978553600 creator A5081123077 @default.
• W1978553600 date "2002-01-21" @default.
• W1978553600 modified "2023-10-03" @default.
• W1978553600 title "βIV-spectrin regulates sodium channel clustering through ankyrin-G at axon initial segments and nodes of Ranvier" @default.
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• W1978553600 doi "https://doi.org/10.1083/jcb.200110003" @default.
• W1978553600 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2199236" @default.
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• W1978553600 hasPublicationYear "2002" @default.
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