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CK2 accumulation at the axon initial segment depends on sodium channel Nav1
Author(s) -
Hien Y.E.,
Montersino A.,
Castets F.,
Leterrier C.,
Filhol O.,
Vacher H.,
Dargent B.
Publication year - 2014
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2014.07.032
Subject(s) - nav1 , ankyrin , sodium channel , microbiology and biotechnology , phosphorylation , ankyrin repeat , chemistry , axon , in vitro , biophysics , in vivo , kinase , biology , biochemistry , sodium , genetics , organic chemistry , gene
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.