ArticleProceedings of the National Academy of Sciences of the United States of America2020
Dimer interaction in the Hv1 proton channel.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed.
- Fluctuating hydrogen-bond network of the Hv1 ion channel.Computational and structural biotechnology journal · 2025Article
- Dimerization is required for the glycosylation of S1-S2 linker of sea urchin voltage-gated proton channel Hv1.Biophysical journal · 2024Article
- The Emerging Role of Microglial Hv1 as a Target for Immunomodulation in Myelin Repair.Aging and disease · 2024Review
- Anionic omega currents from single countercharge mutants in the voltage-sensing domain of Ci-VSP.The Journal of general physiology · 2024Article
- Voltage sensors of a NaNature communications · 2023Article
- Review
- Voltage-Gated Proton Channels in the Tree of Life.Biomolecules · 2023Review
- The Role of Sperm Membrane Potential and Ion Channels in Regulating Sperm Function.International journal of molecular sciences · 2023Review
- Voltage-Gated Proton Channel Hv1 Regulates Neuroinflammation and Dopaminergic Neurodegeneration in Parkinson's Disease Models.Antioxidants (Basel, Switzerland) · 2023Article
- Role of voltage-gated proton channel (Hv1) in cancer biology.Frontiers in pharmacology · 2023Review
- Multiple mechanisms contribute to fluorometry signals from the voltage-gated proton channel.Communications biology · 2022Article
- A Review on the Role of Bicarbonate and Proton Transporters during Sperm Capacitation in Mammals.International journal of molecular sciences · 2022Review
- Microglial voltage-gated proton channel Hv1 in spinal cord injury.Neural regeneration research · 2022Review
- Discovery and characterization of HeLife · 2021Article
- Voltage-gated proton channels from fungi highlight role of peripheral regions in channel activation.Communications biology · 2021Article
Corrections and comments
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Authors and funding
3 authors.
Funding
Abstract
The voltage-gated proton channel Hv1 is a member of the voltage-gated ion channel superfamily, which stands out in design: It is a dimer of two voltage-sensing domains (VSDs), each containing a pore pathway, a voltage sensor (S4), and a gate (S1) and forming its own ion channel. Opening of the two channels in the dimer is cooperative. Part of the cooperativity is due to association between coiled-coil domains that extend intracellularly from the S4s. Interactions between the transmembrane portions of the subunits may also contribute, but the nature of transmembrane packing is unclear. Using functional analysis of a mutagenesis scan, biochemistry, and modeling, we find that the subunits form a dimer interface along the entire length of S1, and also have intersubunit contacts between S1 and S4. These interactions exert a strong effect on gating, in particular on the stability of the open state. Our results suggest that gating in Hv1 is tuned by extensive VSD-VSD interactions between the gates and voltage sensors of the dimeric channel.
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