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

作者：Tan Zhi Yong^*; Priest Birgit T; Krajewski Jeffrey L; Knopp Kelly L; Nisenbaum Eric S; Cummins Theodore R

来源：FEBS LETTERS, 2014, 588(21): 3964-3969.

DOI：10.1016/j.febslet.2014.09.011

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

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.

• 出版日期2014-11-3