Contactin associates with Na+ channels and increases their functional expression

Katie Kazarinova-Noyes, Jyoti Dhar Malhotra, Dyke P. McEwen, Laura N. Mattei, Erik O. Berglund, Barbara Ranscht, S. Rock Levinson, Melitta Schachner, Peter Shrager, Lori L. Isom, Zhi Cheng Xiao

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162 Scopus citations


Contactin (also known as F3, F11) is a surface glycoprotein that has significant homology with the β2 subunit of voltage-gated Na+ channels. Contactin and Na- channels can be reciprocally coimmunoprecipitated from brain homogenates, indicating association within a complex. Cells cotransfected with Na+ channel Nav1.2α and β1 subunits and contactin have threefold to fourfold higher peak Na+ currents than cells with Nav1.2α alone, Nav1.2/β1, Nav1.2/contactin, or Nav1.2/β1/β2. These cells also have a correspondingly higher saxitoxin binding, suggesting an increased Na+ channel surface membrane density. Coimmunoprecipitation of different subunits from cell lines shows that contactin interacts specifically with the β1 subunit. In the PNS, immunocytochemical studies show a transient colocalization of contactin and Na+ channels at new nodes of Ranvier forming during remyelination. In the CNS, there is a particularly high level of colocalization of Na+ channels and contactin at nodes both during development and in the adult. Contactin may thus significantly influence the functional expression and distribution of Na+ channels in neurons.

Original languageEnglish (US)
Pages (from-to)7517-7525
Number of pages9
JournalJournal of Neuroscience
Issue number19
StatePublished - Oct 1 2001
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Neuroscience(all)


  • Axon
  • Cluster
  • Contactin
  • Na channel
  • Node of Ranvier
  • β subunit


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