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pubmed-article:10624965pubmed:abstractTextRapid 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.lld:pubmed
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pubmed-article:10624965pubmed:dateRevised2007-11-14lld:pubmed
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pubmed-article:10624965pubmed:articleTitleCaspr2, a new member of the neurexin superfamily, is localized at the juxtaparanodes of myelinated axons and associates with K+ channels.lld:pubmed
pubmed-article:10624965pubmed:affiliationDepartment of Molecular Cell Biology, The Weizmann Institute of Science, Rehovot, Israel.lld:pubmed
pubmed-article:10624965pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:10624965pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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