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

Zhi Yong Tan, Birgit T. Priest, Jeffrey L. Krajewski, Kelly L. Knopp, Eric S. Nisenbaum, Theodore R. Cummins

Research output: Contribution to journalArticle

12 Scopus citations


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.

Original languageEnglish (US)
Pages (from-to)3964-3969
Number of pages6
JournalFEBS Letters
Issue number21
StatePublished - Nov 3 2014



  • Mutation
  • Protein kinase C
  • Resurgent current hNav1.7
  • Sodium channel
  • Voltage clamp

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Cell Biology
  • Genetics
  • Molecular Biology
  • Structural Biology

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