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Juxtaparanodal clustering of Shaker-like K+ channels in myelinated axons depends on Caspr2 and TAG-1.

In myelinated axons, K+ channels are concealed under the myelin sheath in the juxtaparanodal region, where they are associated with Caspr2, a member of the neurexin superfamily. Deletion of Caspr2 in mice by gene targeting revealed that it is required to maintain K+ channels at this location. Furthermore, we show that the localization of Caspr2 and clustering of K+ channels at the juxtaparanodal region depends on the presence of TAG-1, an immunoglobulin-like cell adhesion molecule that binds Caspr2. These results demonstrate that Caspr2 and TAG-1 form a scaffold that is necessary to maintain K+ channels at the juxtaparanodal region, suggesting that axon-glia interactions mediated by these proteins allow myelinating glial cells to organize ion channels in the underlying axonal membrane.

Pubmed ID: 12963709 RIS Download

Mesh terms: Animals | Axons | Cell Adhesion Molecules, Neuronal | Cell Communication | Contactin 2 | Gene Targeting | Membrane Proteins | Mice | Mice, Knockout | Microscopy, Electron | Mutation | Nerve Fibers, Myelinated | Nerve Tissue Proteins | Neural Conduction | Neuroglia | Potassium Channels | Ranvier's Nodes | Shaker Superfamily of Potassium Channels

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Associated grants

  • Agency: NINDS NIH HHS, Id: R01 NS017965
  • Agency: NINDS NIH HHS, Id: NS17965
  • Agency: PHS HHS, Id: R01-23375

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