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Dimer interaction in the Hv1 proton channel.

Laetitia Mony1,2, David Stroebel2, Ehud Y Isacoff3,4,5

  • 1Department of Molecular and Cell Biology, University of California, Berkeley, CA 94720.

Proceedings of the National Academy of Sciences of the United States of America
|August 14, 2020
PubMed
Summary

The voltage-gated proton channel Hv1, a unique ion channel dimer, features extensive interactions between its voltage-sensing domains (VSDs). These VSD-VSD contacts significantly influence channel gating and stability.

Keywords:
Hv1ion channelproton channelvoltage-gated channel

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Area of Science:

  • Molecular biology
  • Biophysics
  • Ion channel research

Background:

  • The voltage-gated proton channel Hv1 (Hv1) is a dimeric ion channel.
  • Each subunit comprises a voltage-sensing domain (VSD) with pore and gating elements.
  • Cooperative opening of the two channels is a key functional characteristic.

Purpose of the Study:

  • To elucidate the structural basis of transmembrane subunit interactions in Hv1.
  • To understand how these interactions contribute to the channel's cooperative gating mechanism.

Main Methods:

  • Functional analysis via mutagenesis scanning.
  • Biochemical assays to probe subunit interactions.
  • Computational modeling to visualize VSD-VSD interfaces.

Main Results:

  • Hv1 subunits form a continuous dimer interface along the S1 segments.
  • Intersubunit contacts also occur between S1 and S4 segments.
  • These extensive VSD-VSD interactions critically affect channel gating, particularly the stability of the open state.

Conclusions:

  • Gating of the Hv1 channel is finely tuned by substantial interactions between the VSDs of dimeric subunits.
  • These interactions involve both the gates (S1) and voltage sensors (S4).
  • The findings provide a detailed structural and functional model for Hv1 gating.