ArticleThe Journal of general physiology2014
Long α helices projecting from the membrane as the dimer interface in the voltage-gated H(+) channel.
Article in The Journal of general physiology, 2014. 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.
- Temperature Dependent Activity of the Voltage-Gated Proton Channel.Advances in experimental medicine and biology · 2024Review
- Voltage and pH difference across the membrane control the S4 voltage-sensor motion of the Hv1 proton channel.Scientific reports · 2020Article
- Engineered high-affinity zinc binding site reveals gating configurations of a human proton channel.The Journal of general physiology · 2020Article
- Dimer interaction in the Hv1 proton channel.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
- Identification of a vacuolar proton channel that triggers the bioluminescent flash in dinoflagellates.PloS one · 2017Article
- 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
- Direct Interaction between the Voltage Sensors Produces Cooperative Sustained Deactivation in Voltage-gated H+ Channel Dimers.The Journal of biological chemistry · 2016Article
- Effects of unsaturated fatty acids on the kinetics of voltage-gated proton channels heterologously expressed in cultured cells.The Journal of physiology · 2016Article
- 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
- Bacterial voltage-gated sodium channels (BacNa(V)s) from the soil, sea, and salt lakes enlighten molecular mechanisms of electrical signaling and pharmacology in the brain and heart.Journal of molecular biology · 2015Review
- Enhanced activation of an amino-terminally truncated isoform of the voltage-gated proton channel HVCN1 enriched in malignant B cells.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- X-ray crystal structure of voltage-gated proton channel.Nature structural & molecular biology · 2014Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The voltage-gated H(+) channel (Hv) is a H(+)-permeable voltage-sensor domain (VSD) protein that consists of four transmembrane segments (S1-S4). Hv assembles as a dimeric channel and two transmembrane channel domains function cooperatively, which is mediated by the coiled-coil assembly domain in the cytoplasmic C terminus. However, the structural basis of the interdomain interactions remains unknown. Here, we provide a picture of the dimer configuration based on the analyses of interactions among two VSDs and a coiled-coil domain. Systematic mutations of the linker region between S4 of VSD and the coiled-coil showed that the channel gating was altered in the helical periodicity with the linker length, suggesting that two domains are linked by helices. Cross-linking analyses revealed that the two S4 helices were situated closely in the dimeric channel. The interaction interface between the two S4 and the assembly interface of the coiled-coil domain were aligned in the same direction based on the phase angle calculation along α helices. Collectively, we propose that continuous helices stretching from the transmembrane to the cytoplasmic region in the dimeric interface regulate the channel activation in the Hv dimer.
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