The DOI matches its Crossref record.
A Voltage Sensor-Domain Protein Is a Voltage-Gated Proton Channel
Abstract
Voltage-gated proton channels have been widely observed but have not been identified at a molecular level. Here we report that a four-transmembrane protein similar to the voltage-sensor domain of voltage-gated ion channels is a voltage-gated proton channel. Cells overexpressing this protein showed depolarization-induced outward currents accompanied by tail currents. Current reversal occured at equilibrium potentials for protons. The currents exhibited pH-dependent gating and zinc ion sensitivity, two features which are characteristic of voltage-gated proton channels. Responses of voltage dependence to sequence changes suggest that mouse voltage-sensor domain–only protein is itself a channel, rather than a regulator of another channel protein.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cited by
The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology
Bedard, K., & Krause, K.-H. (2007) · Physiological Reviews · doi:10.1152/physrev.00044.2005 · Cited by 6,989
NADPH Oxidases (NOX): An Overview from Discovery, Molecular Mechanisms to Physiology and Pathology
Vermot, A., Petit-Härtlein, I., Smith, S. M. E., & Fieschi, F. (2021) · Antioxidants · doi:10.3390/antiox10060890 · Cited by 766
Redox signaling across cell membranes
Fisher, A. B. (2009) · Antioxidants & Redox Signaling · doi:10.1089/ars.2008.2378 · Cited by 269
Parkinson’s disease-risk protein TMEM175 is a proton-activated proton channel in lysosomes
Hu, M., Li, P., Wang, C., Feng, X., Geng, Q., Chen, W., Marthi, M., Zhang, W., Gao, C., Reid, W., et al. (2022) · Cell · doi:10.1016/j.cell.2022.05.021 · Cited by 254
The voltage-gated proton channel Hv1 enhances brain damage from ischemic stroke
Wu, L.-J., Wu, G., Sharif, M. R. A., Baker, A., Jia, Y., Fahey, F. H., Luo, H. R., Feener, E. P., & Clapham, D. E. (2012) · Nature Neuroscience · doi:10.1038/nn.3059 · Cited by 252
Metadata
- Authors
- Sasaki, M., Takagi, M., & Okamura, Y.
- Venue
- Science
- Published
- 2006-04-28
- Volume
- 312
- Issue
- 5773
- Pages
- 589-592
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W1965191256
- Cited by
- 542
- References
- 0
- FWCI
- 11.79
- Type
- journal article
- Language
- en
- Open access
- closed
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: A Voltage Sensor-Domain Protein Is a Voltage-Gated Proton Channel. https://app.cochat.ai/papers/10.1126/science.1122352
- The paper
- Sasaki, M., Takagi, M., & Okamura, Y. (2006). A Voltage Sensor-Domain Protein Is a Voltage-Gated Proton Channel. Science. https://doi.org/10.1126/science.1122352
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.