Key result
Voltage- and patch-clamp fluorometry revealed that channel opening of the Hv1 proton channel involves a dynamic motion of the S1 helix relative to its surroundings, functioning as part of the gate.
The study reveals that the S1 helix of the Hv1 proton channel undergoes specialized motion to function as part of the channel's gate.
S1 motion in Hv1 gating shown in animals; extends channel models but leaves human relevance and therapies open.
Voltage- and patch-clamp fluorometry reveal structural rearrangements of the S1 helix and its surroundings that are important for gating of the Hv1 voltage-gated proton channel. The Hv1 proton channel is unique among voltage-gated channels for containing the pore and gate within its voltage-sensing domain. Pore opening has been proposed to include assembly of the selectivity filter between an arginine (R3) of segment S4 and an aspartate (D1) of segment S1. We determined whether gating involves motion of S1, using Ciona intestinalis Hv1. We found that channel opening is concomitant with solution access to the pore-lining face of S1, from the cytoplasm to deep inside the pore. Voltage- and patch-clamp fluorometry showed that this involves a motion of S1 relative to its surroundings. S1 motion and the S4 motion that precedes it are each influenced by residues on the other helix, thus suggesting a dynamic interaction between S1 and S4. Our findings suggest that the S1 of Hv1 has specialized to function as part of the channel's gate.
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Mony et al. (2015) studied this question. Voltage- and patch-clamp fluorometry was evaluated on Structural rearrangements of the S1 helix and its surroundings. Voltage- and patch-clamp fluorometry revealed that channel opening of the Hv1 proton channel involves a dynamic motion of the S1 helix relative to its surroundings, functioning as part of the gate.
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