Tan, Zhi-YongPriest, Birgit T.Krajewski, Jeffrey L.Knopp, Kelly L.Nisenbaum, Eric S.Cummins, Theodore R.2016-10-122016-10-122014-11-03Tan, Z.-Y., Priest, B. T., Krajewski, J. L., Knopp, K. L., Nisenbaum, E. S., & Cummins, T. R. (2014). Protein Kinase C enhances human sodium channel hNav1.7 resurgent currents via a serine residue in the domain III–IV linker. FEBS Letters, 588(21), 3964–3969. http://doi.org/10.1016/j.febslet.2014.09.0111873-3468https://hdl.handle.net/1805/11163Resurgent 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.en-USPublisher PolicyElectrophysiological ProcessesNAV1.7 Voltage-Gated Sodium ChannelchemistrygeneticsmetabolismProtein Kinase CSerineArticle