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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


  • Poliak S
  • Salomon D
  • Elhanany H
  • Sabanay H
  • Kiernan B
  • Pevny L
  • Stewart CL
  • Xu X
  • Chiu SY
  • Shrager P
  • Furley AJ
  • Peles E


The Journal of cell biology

Publication Data

September 15, 2003

Associated Grants

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

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