Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10870411 | FEBS Letters | 2014 | 6 Pages |
Abstract
Accumulation of voltage-gated sodium channel Nav1 at the axon initial segment (AIS), results from a direct interaction with ankyrin G. This interaction is regulated in vitro by the protein kinase CK2, which is also highly enriched at the AIS. Here, using phosphospecific antibodies and inhibition/depletion approaches, we showed that Nav1 channels are phosphorylated in vivo in their ankyrin-binding motif. Moreover, we observed that CK2 accumulation at the AIS depends on expression of Nav1 channels, with which CK2 forms tight complexes. Thus, the CK2-Nav1 interaction is likely to initiate an important regulatory mechanism to finely control Nav1 phosphorylation and, consequently, neuronal excitability.
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Authors
Y.E. Hien, A. Montersino, F. Castets, C. Leterrier, O. Filhol, H. Vacher, B. Dargent,