Interaction of voltage-gated sodium channel Nav1.6 (SCN8A) with microtubule-associated protein Map1b.

ABSTRACT: The mechanism by which voltage-gated sodium channels are trafficked to the surface of neurons is not well understood. Our previous work implicated the cytoplasmic N terminus of the sodium channel Na(v)1.6 in this process. We report that the N terminus plus the first transmembrane segment (residues 1-153) is sufficient to direct a reporter to the cell surface. To identify proteins that interact with the 117-residue N-terminal domain, we carried out a yeast two-hybrid screen of a mouse brain cDNA library. Three clones containing overlapping portions of the light chain of microtubule-associated protein Map1b (Mtap1b) were recovered from the screen. Interaction between endogenous Na(v)1.6 channels and Map1b in mouse brain was confirmed by co-immunoprecipitation. Map1b did not interact with the

SUBMITTER: O'Brien JE 

PROVIDER: S-EPMC3365756 | biostudies-literature | 2012 May

REPOSITORIES: biostudies-literature