ArticleThe Journal of general physiology2013
Sensing charges of the Ciona intestinalis voltage-sensing phosphatase.
Article in The Journal of general physiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
33 citing papers in PubMed, 43 citations in OpenAlex.
- Voltage sensors.Molecular pharmacology · 2025Review
- Coupling sensor to enzyme in the voltage sensing phosphatase.Nature communications · 2024Article
- An Ultrasensitive Genetically Encoded Voltage Indicator Uncovers the Electrical Activity of Non-Excitable Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Effect of a sensing charge mutation on the deactivation of KV7.2 channels.The Journal of general physiology · 2024Article
- Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP.Nature communications · 2024Article
- Anionic omega currents from single countercharge mutants in the voltage-sensing domain of Ci-VSP.The Journal of general physiology · 2024Article
- Ion currents through the voltage sensor domain of distinct families of proteins.Journal of biological physics · 2023Review
- Modulation of cardiac voltage-activated KLife sciences · 2022Article
- Mechanism of voltage gating in the voltage-sensing phosphatase Ci-VSP.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Monitoring of compound resting membrane potentials of cell cultures with ratiometric genetically encoded voltage indicators.Communications biology · 2021Article
- The voltage sensor is responsible for ΔpH dependence in HProceedings of the National Academy of Sciences of the United States of America · 2021Article
- Reinterpretation of the substrate specificity of the voltage-sensing phosphatase during dimerization.The Journal of general physiology · 2019Article
- Molecular mechanisms of coupling to voltage sensors in voltage-evoked cellular signals.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2019Review
- The Role of Proton Transport in Gating Current in a Voltage Gated Ion Channel, as Shown by Quantum Calculations.Sensors (Basel, Switzerland) · 2018Article
- Gating-induced large aqueous volumetric remodeling and aspartate tolerance in the voltage sensor domain of Shaker KProceedings of the National Academy of Sciences of the United States of America · 2018Article
- The solute carrier SLC9C1 is a NaNature communications · 2018Article
- Dimerization of the voltage-sensing phosphatase controls its voltage-sensing and catalytic activity.The Journal of general physiology · 2018Article
- Nonsensing residues in S3-S4 linker's C terminus affect the voltage sensor set point in KThe Journal of general physiology · 2018Article
- Gating Charge Calculations by Computational Electrophysiology Simulations.Biophysical journal · 2017Article
- Hysteresis in voltage-gated channels.Channels (Austin, Tex.) · 2017Review
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
Voltage control over enzymatic activity in voltage-sensitive phosphatases (VSPs) is conferred by a voltage-sensing domain (VSD) located in the N terminus. These VSDs are constituted by four putative transmembrane segments (S1 to S4) resembling those found in voltage-gated ion channels. The putative fourth segment (S4) of the VSD contains positive residues that likely function as voltage-sensing elements. To study in detail how these residues sense the plasma membrane potential, we have focused on five arginines in the S4 segment of the Ciona intestinalis VSP (Ci-VSP). After implementing a histidine scan, here we show that four arginine-to-histidine mutants, namely R223H to R232H, mediate voltage-dependent proton translocation across the membrane, indicating that these residues transit through the hydrophobic core of Ci-VSP as a function of the membrane potential. These observations indicate that the charges carried by these residues are sensing charges. Furthermore, our results also show that the electrical field in VSPs is focused in a narrow hydrophobic region that separates the extracellular and intracellular space and constitutes the energy barrier for charge crossing.
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What OpenQuestion holds
Registered trials
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.