Protein kinase C enhances human sodium channel hNav1.7 resurgent currents via a serine residue in the domain III–IV linker | Zendy

Tan Zhi-Yong | Zendy; Priest Birgit T. | Zendy; Krajewski Jeffrey L. | Zendy; Knopp Kelly L. | Zendy; Nisenbaum Eric S. | Zendy; Cummins Theodore R. | Zendy

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Protein kinase C enhances human sodium channel hNav1.7 resurgent currents via a serine residue in the domain III–IV linker

Author(s) -

Tan Zhi-Yong,

Priest Birgit T.,

Krajewski Jeffrey L.,

Knopp Kelly L.,

Nisenbaum Eric S.,

Cummins Theodore R.

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.2014.09.011

Subject(s) - phosphorylation , serine , protein kinase c , sodium channel , kinase , linker , chemistry , threonine , residue (chemistry) , protein kinase domain , microbiology and biotechnology , sodium , biochemistry , biophysics , biology , mutant , organic chemistry , computer science , gene , operating system

Resurgent sodium currents likely play a role in modulating neuronal excitability. Here we studied whether protein kinase C (PKC) activation can increase resurgent currents produced by the human sodium channel hNav1.7. We found that a PKC agonist significantly enhanced hNav1.7‐mediated resurgent currents and this was prevented by PKC antagonists. The enhancing effects were replicated by two phosphorylation‐mimicking mutations and were prevented by a phosphorylation‐deficient mutation at a conserved PKC phosphorylation site (Serine 1479). Our results suggest that PKC can increase sodium resurgent currents through phosphorylation of a conserved Serine residue located in the domain III–IV linker of sodium channels.

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