Hydrophobic gasket mutation produces gating pore currents in closed human voltage-gated proton channels.

ABSTRACT: The hydrophobic gasket (HG), a ring of hydrophobic amino acids in the voltage-sensing domain of most voltage-gated ion channels, forms a constriction between internal and external aqueous vestibules. Cationic Arg or Lys side chains lining the S4 helix move through this "gating pore" when the channel opens. S4 movement may occur during gating of the human voltage-gated proton channel, hH_V1, but proton current flows through the same pore in open channels. Here, we replaced putative HG residues with less hydrophobic residues or acidic Asp. Substitution of individuals, pairs, or all 3 HG positions did not impair proton selectivity. Evidently, the HG does not act as a secondary selectivity filter. However, 2 unexpected functions of the HG in H_V1 were discovered. Mutating H

SUBMITTER: Banh R 

PROVIDER: S-EPMC6754559 | biostudies-literature | 2019 Sep

REPOSITORIES: biostudies-literature