Heterophilic interactions of sodium channel beta1 subunits with axonal and glial cell adhesion molecules.

@article{McEwen2004HeterophilicIO,
  title={Heterophilic interactions of sodium channel beta1 subunits with axonal and glial cell adhesion molecules.},
  author={Dyke P. McEwen and Lori L Isom},
  journal={The Journal of biological chemistry},
  year={2004},
  volume={279 50},
  pages={52744-52}
}
Voltage-gated sodium channels localize at high density in axon initial segments and nodes of Ranvier in myelinated axons. Sodium channels consist of a pore-forming alpha subunit and at least one beta subunit. beta1 is a member of the immunoglobulin superfamily of cell adhesion molecules and interacts homophilically and heterophilically with contactin and Nf186. In this study, we characterized beta1 interactions with contactin and Nf186 in greater detail and investigated interactions of beta1… CONTINUE READING