ArticleThe Journal of biological chemistry2010
The role and structure of the carboxyl-terminal domain of the human voltage-gated proton channel Hv1.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 41 papers.
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Who cites it
41 citing papers in PubMed, 61 citations in OpenAlex.
- 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
- Interaction with stomatin directs human proton channels into cholesterol-dependent membrane domains.Biophysical journal · 2024Article
- Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024Review
- Voltage-Gated Proton Channels in the Tree of Life.Biomolecules · 2023Review
- Biomimetic Artificial Proton Channels.Biomolecules · 2022Review
- Voltage-gated proton channels from fungi highlight role of peripheral regions in channel activation.Communications biology · 2021Article
- Zn2+ to probe voltage-gated proton (Hv1) channels.The Journal of general physiology · 2020Article
- HVCN1 Channels Are Relevant for the Maintenance of Sperm Motility During In Vitro Capacitation of Pig Spermatozoa.International journal of molecular sciences · 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
- Coupling between an electrostatic network and the ZnThe Journal of general physiology · 2018Article
- Exotic properties of a voltage-gated proton channel from the snailThe Journal of general physiology · 2018Article
- Proton pump inhibitors have pH-dependent effects on the thermostability of the carboxyl-terminal domain of voltage-gated proton channel Hv1.European biophysics journal : EBJ · 2018Article
- The Hv1 proton channel responds to mechanical stimuli.The Journal of general physiology · 2016Article
- Insights into the structure and function of HV1 from a meta-analysis of mutation studies.The Journal of general physiology · 2016Review
- Structural revelations of the human proton channel.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Resting state of the human proton channel dimer in a lipid bilayer.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Interrogation of the intersubunit interface of the open Hv1 proton channel with a probe of allosteric coupling.Scientific reports · 2015Article
- The Voltage-Gated Proton Channel: A Riddle, Wrapped in a Mystery, inside an Enigma.Biochemistry · 2015Review
- A specialized molecular motion opens the Hv1 voltage-gated proton channel.Nature structural & molecular biology · 2015Article
Corrections and comments
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Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The voltage-gated proton channel Hv1 has a voltage sensor domain but lacks a pore domain. Although the C-terminal domain of Hv1 is known to be responsible for dimeric architecture of the channel, its role and structure are not known. We report that the full-length Hv1 is mainly localized in intracellular compartment membranes rather than the plasma membrane. Truncation of either the N or C terminus alone or both together revealed that the N-terminal deletion did not alter localization, but deletion of the C terminus either alone or together with the N terminus resulted in expression throughout the cell. These results indicate that the C terminus is essential for Hv1 localization but not the N terminus. In the 2.0 A structure of the C-terminal domain, the two monomers form a dimer via a parallel alpha-helical coiled-coil, in which one chloride ion binds with the Neta atom of Arg(264). A pH-dependent structural change of the protein has been observed, but it remains a dimer irrespective of pH value.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.