期刊
ELIFE
卷 6, 期 -, 页码 -出版社
ELIFE SCIENCES PUBLICATIONS LTD
DOI: 10.7554/eLife.21392
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资金
- Wellcome
- Medical Research Council
- National Institutes of Health [NS044916, NS069688, NS050220]
- Dr. Miriam and Sheldon G. Adelson Medical Research Foundation
- United States-Israel Binational Science Foundation
- Israel Science Foundation
- Wellcome Trust [107008/Z/15/Z] Funding Source: Wellcome Trust
- Medical Research Council [MR/L011379/1] Funding Source: researchfish
- Wellcome Trust [107008/Z/15/Z] Funding Source: researchfish
- MRC [MR/L011379/1] Funding Source: UKRI
A high density of Na+ channels at nodes of Ranvier is necessary for rapid and efficient action potential propagation in myelinated axons. Na+ channel clustering is thought to depend on two axonal cell adhesion molecules that mediate interactions between the axon and myelinating glia at the nodal gap (i.e., NF186) and the paranodal junction (i.e., Caspr). Here we show that while Na+ channels cluster at nodes in the absence of NF186, they fail to do so in double conditional knockout mice lacking both NF186 and the paranodal cell adhesion molecule Caspr, demonstrating that a paranodal junction-dependent mechanism can cluster Na+ channels at nodes. Furthermore, we show that paranode-dependent clustering of nodal Na+ channels requires axonal beta II spectrin which is concentrated at paranodes. Our results reveal that the paranodal junction-dependent mechanism of Na+ channel clustering is mediated by the spectrin-based paranodal axonal cytoskeleton.
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