ArticleScientific reports2015
Interrogation of the intersubunit interface of the open Hv1 proton channel with a probe of allosteric coupling.
Article in Scientific reports, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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Who cites it
19 citing papers in PubMed.
- Hydrophobic residues in S1 modulate enzymatic function and voltage sensing in voltage-sensing phosphatase.The Journal of general physiology · 2024Article
- Article
- Trapping Charge Mechanism in Hv1 Channels (International journal of molecular sciences · 2023Article
- Voltage-Gated Proton Channels in the Tree of Life.Biomolecules · 2023Review
- Microglial reprogramming by Hv1 antagonism protects neurons from inflammatory and glutamate toxicity.Journal of neurochemistry · 2023Article
- Proton transfer reactions: From photochemistry to biochemistry and bioenergetics.BBA advances · 2023Article
- HIFs: New arginine mimic inhibitors of the Hv1 channel with improved VSD-ligand interactions.The Journal of general physiology · 2021Article
- A novel Hv1 inhibitor reveals a new mechanism of inhibition of a voltage-sensing domain.The Journal of general physiology · 2021Article
- Voltage-gated proton channels from fungi highlight role of peripheral regions in channel activation.Communications biology · 2021Article
- Zinc modulation of proton currents in a new voltage-gated proton channel suggests a mechanism of inhibition.The FEBS journal · 2020Article
- Dimer interaction in the Hv1 proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Voltage-dependent structural models of the human Hv1 proton channel from long-timescale molecular dynamics simulations.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- Role of human Hv1 channels in sperm capacitation and white blood cell respiratory burst established by a designed peptide inhibitor.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Gating charge displacement in a monomeric voltage-gated proton (HProceedings of the National Academy of Sciences of the United States of America · 2018Article
- On the role of water density fluctuations in the inhibition of a proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- The Hv1 proton channel responds to mechanical stimuli.The Journal of general physiology · 2016Article
- Molecular mechanism of Zn2+ inhibition of a voltage-gated proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Insights into the structure and function of HV1 from a meta-analysis of mutation studies.The Journal of general physiology · 2016Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
The Hv1 voltage-gated proton channel is a dimeric complex consisting of two voltage-sensing domains (VSDs), each containing a gated proton permeation pathway. Dimerization is controlled by a cytoplasmic coiled-coil domain. The transitions from the closed to the open state in the two VSDs are known to occur cooperatively; however, the underlying mechanism is poorly understood. Intersubunit interfaces play a critical role in allosteric processes; but, such interfaces have not been determined in the open Hv1 channel. Here we show that 2-guanidinothiazole derivatives block the two Hv1 VSDs in a cooperative way, and use one of the compounds as a probe of allosteric coupling between open subunits. We find that the extracellular ends of the first transmembrane segments of the VSDs form the intersubunit interface that mediates coupling between binding sites, while the coiled-coil domain does not directly participate in the process. We also find strong evidence that the channel's proton selectivity filter controls blocker binding cooperativity.
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