Evolutionarily conserved intracellular gate of voltage-dependent sodium channels

Kevin Oelstrom, Marcel P. Goldschen-Ohm, Miguel Holmgren and Baron Chanda ()
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Kevin Oelstrom: 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

Nature Communications, 2014, vol. 5, issue 1, 1-9

Abstract: 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.

Date: 2014
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DOI: 10.1038/ncomms4420

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