ArticleNature communications2017
Inactivation of KCNQ1 potassium channels reveals dynamic coupling between voltage sensing and pore opening.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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Who cites it
52 citing papers in PubMed.
- Structural and kinetic mechanisms of state-dependent potassium channel inhibition.Science advances · 2026Article
- Article
- Barium senses subtle pore changes in a voltage-gated KScience advances · 2026Article
- PIPNature communications · 2026Article
- Two-step voltage-sensor activation of the human KNature communications · 2026Article
- Chemical tuning reveals a cation-π gating bridge between the voltage-sensor and pore domains in the KProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Electrophysiological characterization of the state-dependent inhibition of Kv7.1 and IMolecular pharmacology · 2025Article
- Secondary structure transitions and dual PIP2 binding define cardiac KCNQ1-KCNE1 channel gating.Cell research · 2025Article
- PIPResearch square · 2025Article
- A physiologically-relevant intermediate state structure of a voltage-gated potassium channel.Nature communications · 2025Article
- The fully activated open state of KCNQ1 controls the cardiac "fight-or-flight" response.PNAS nexus · 2024Article
- Targeting the ICirculation research · 2024Article
- Evaluating sequential and allosteric activation models in IKs channels with mutated voltage sensors.The Journal of general physiology · 2024Article
- Modulation of potassium channels by transmembrane auxiliary subunits via voltage-sensing domains.Physiological reports · 2024Review
- Arrhythmia-associated calmodulin variants interact with KCNQ1 to confer aberrant membrane trafficking and function.PNAS nexus · 2023Article
- Mechanistic understanding of KCNQ1 activating polyunsaturated fatty acid analogs.The Journal of general physiology · 2023Article
- The membrane electric field regulates the PIPProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Mechanism of external K+ sensitivity of KCNQ1 channels.The Journal of general physiology · 2023Article
- Long-QT mutations in KCNE1 modulate the 17β-estradiol response of Kv7.1/KCNE1.Science advances · 2023Article
- Modulation of the IBBA advances · 2023Article
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8 authors.
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Abstract
In voltage-activated ion channels, voltage sensor (VSD) activation induces pore opening via VSD-pore coupling. Previous studies show that the pore in KCNQ1 channels opens when the VSD activates to both intermediate and fully activated states, resulting in the intermediate open (IO) and activated open (AO) states, respectively. It is also well known that accompanying KCNQ1 channel opening, the ionic current is suppressed by a rapid process called inactivation. Here we show that inactivation of KCNQ1 channels derives from the different mechanisms of the VSD-pore coupling that lead to the IO and AO states, respectively. When the VSD activates from the intermediate state to the activated state, the VSD-pore coupling has less efficacy in opening the pore, producing inactivation. These results indicate that different mechanisms, other than the canonical VSD-pore coupling, are at work in voltage-dependent ion channel activation.
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