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Evolutionarily conserved intracellular gate of voltage-dependent sodium channels

Author

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  • Kevin Oelstrom

    (University of Wisconsin
    Molecular Pharmacology Graduate Program, University of Wisconsin)

  • Marcel P. Goldschen-Ohm

    (University of Wisconsin)

  • Miguel Holmgren

    (Molecular Neurophysiology Section, National Institute of Neurological Disorders and Stroke, National Institutes of Health)

  • Baron Chanda

    (University of Wisconsin)

Abstract

Members of the voltage-gated ion channel superfamily (VGIC) regulate ion flux and generate electrical signals in excitable cells by opening and closing pore gates. The location of the gate in voltage-gated sodium channels, a founding member of this superfamily, remains unresolved. Here we explore the chemical modification rates of introduced cysteines along the S6 helix of domain IV in an inactivation-removed background. We find that state-dependent accessibility is demarcated by an S6 hydrophobic residue; substituted cysteines above this site are not modified by charged thiol reagents when the channel is closed. These accessibilities are consistent with those inferred from open- and closed-state structures of prokaryotic sodium channels. Our findings suggest that an intracellular gate composed of a ring of hydrophobic residues is not only responsible for regulating access to the pore of sodium channels, but is also a conserved feature within canonical members of the VGIC superfamily.

Suggested Citation

  • Kevin Oelstrom & Marcel P. Goldschen-Ohm & Miguel Holmgren & Baron Chanda, 2014. "Evolutionarily conserved intracellular gate of voltage-dependent sodium channels," Nature Communications, Nature, vol. 5(1), pages 1-9, May.
    • Handle: RePEc:nat:natcom:v:5:y:2014:i:1:d:10.1038_ncomms4420
    DOI: 10.1038/ncomms4420
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