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Caspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels.

Authors: Poliak, S  Gollan, L  Martinez, R  Custer, A  Einheber, S  Salzer, JL  Trimmer, JS  Shrager, P  Peles, E 
Citation: Poliak S, etal., Neuron. 1999 Dec;24(4):1037-47.
Pubmed: (View Article at PubMed) PMID:10624965

Rapid conduction in myelinated axons depends on the generation of specialized subcellular domains to which different sets of ion channels are localized. Here, we describe the identification of Caspr2, a mammalian homolog of Drosophila Neurexin IV (Nrx-IV), and show that this neurexin-like protein and the closely related molecule Caspr/Paranodin demarcate distinct subdomains in myelinated axons. While contactin-associated protein (Caspr) is present at the paranodal junctions, Caspr2 is precisely colocalized with Shaker-like K+ channels in the juxtaparanodal region. We further show that Caspr2 specifically associates with Kv1.1, Kv1.2, and their Kvbeta2 subunit. This association involves the C-terminal sequence of Caspr2, which contains a putative PDZ binding site. These results suggest a role for Caspr family members in the local differentiation of the axon into distinct functional subdomains.

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RGD Object Information
RGD ID: 8554062
Created: 2014-05-08
Species: All species
Last Modified: 2014-05-08
Status: ACTIVE



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