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J. Biol. Chem., Vol. 279, Issue 50, 52744-52752, December 10, 2004
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Heterophilic Interactions of Sodium Channel 
1 Subunits with Axonal and Glial Cell Adhesion Molecules*
From the Department of Pharmacology, University of Michigan, Ann Arbor, Michigan 48109-0632
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 
subunit and at least one 
subunit. 1 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 1 interactions with contactin and Nf186 in greater detail and investigated interactions of 1 with NrCAM, Nf155, and sodium channel 2 and 3 subunits. Using Fc fusion proteins and immunocytochemical techniques, we show that 1 interacts with the fibronectin-like domains of contactin. 1 also interacts with NrCAM, Nf155, sodium channel 2, and Nf186 but not with sodium channel 3. The interaction of the extracellular domains of 1 and 2 requires the region 169TEEEGKTDGEGNA181 located in the intracellular domain of 2. Interaction of 1 with Nf186 results in increased Nav1.2 cell surface density over alone, similar to that shown previously for contactin and 2. We propose that 1 is the critical communication link between sodium channels, nodal cell adhesion molecules, and ankyrinG.
Received for publication, May 28, 2004 , and in revised form, August 4, 2004.
* This work was supported in part by National Institutes of Health (NIH) Grant R01MH59980 (to L. L. I.) and by a subcontract from NIH Grant R01NS17965-17 from Dr. Peter Shrager at the University of Rochester (to L. L. I.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
Supported by National Research Service Award Predoctoral Fellowship NS43067.
To whom correspondence should be addressed: Dept. of Pharmacology, University of Michigan, 1150 W. Medical Center Dr., 1301 MSRB III, Ann Arbor, MI 48109-0632. Tel.: 734-936-3050; Fax: 734-763-4450; E-mail: lisom{at}umich.edu.
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