ArticleProceedings of the National Academy of Sciences of the United States of America2012
Allosteric gating mechanism underlies the flexible gating of KCNQ1 potassium channels.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 63 papers.
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Who cites it
63 citing papers in PubMed, 83 citations in OpenAlex.
- Article
- Barium senses subtle pore changes in a voltage-gated KScience advances · 2026Article
- Electro-Mechanical Uncoupling of KArchiv der Pharmazie · 2026Article
- The conductance of KCNQ2 and its pathogenic variants is determined by individual subunit gating.Science advances · 2025Article
- Identification of KCNE6, a new member of the KCNE family of potassium channel auxiliary subunits.Communications biology · 2024Article
- Dynamic protein-protein interactions of KCNQ1 and KCNE1 measured by EPR line shape analysis.Biochimica et biophysica acta. Biomembranes · 2024Article
- Lipophilic compounds restore function to neurodevelopmental-associated KCNQ3 mutations.Communications biology · 2024Article
- Evaluating sequential and allosteric activation models in IKs channels with mutated voltage sensors.The Journal of general physiology · 2024Article
- The role of native cysteine residues in the oligomerization of KCNQ1 channels.Biochemical and biophysical research communications · 2023Article
- Emerging methods to model cardiac ion channel and myocyte electrophysiology.Biophysics reviews · 2023Review
- Article
- Purification and membrane interactions of human KCNQ1Biochimica et biophysica acta. Biomembranes · 2022Article
- Kv Channel Ancillary Subunits: Where Do We Go from Here?Physiology (Bethesda, Md.) · 2022Review
- Distinctive mechanisms of epilepsy-causing mutants discovered by measuring S4 movement in KCNQ2 channels.eLife · 2022Article
- Two small-molecule activators share similar effector sites in the KCNQ1 channel pore but have distinct effects on voltage sensor movements.Frontiers in physiology · 2022Article
- ML277 regulates KCNQ1 single-channel amplitudes and kinetics, modified by voltage sensor state.The Journal of general physiology · 2021Article
- A general mechanism of KCNE1 modulation of KCNQ1 channels involving non-canonical VSD-PD coupling.Communications biology · 2021Article
- Identification of PUFA interaction sites on the cardiac potassium channel KCNQ1.The Journal of general physiology · 2021Article
- Control of Biophysical and Pharmacological Properties of Potassium Channels by Ancillary Subunits.Handbook of experimental pharmacology · 2021Article
- Kv7 Channels and Excitability Disorders.Handbook of experimental pharmacology · 2021Article
3 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
KCNQ1 (Kv7.1) is a unique member of the superfamily of voltage-gated K(+) channels in that it displays a remarkable range of gating behaviors tuned by coassembly with different β subunits of the KCNE family of proteins. To better understand the basis for the biophysical diversity of KCNQ1 channels, we here investigate the basis of KCNQ1 gating in the absence of β subunits using voltage-clamp fluorometry (VCF). In our previous study, we found the kinetics and voltage dependence of voltage-sensor movements are very similar to those of the channel gate, as if multiple voltage-sensor movements are not required to precede gate opening. Here, we have tested two different hypotheses to explain KCNQ1 gating: (i) KCNQ1 voltage sensors undergo a single concerted movement that leads to channel opening, or (ii) individual voltage-sensor movements lead to channel opening before all voltage sensors have moved. Here, we find that KCNQ1 voltage sensors move relatively independently, but that the channel can conduct before all voltage sensors have activated. We explore a KCNQ1 point mutation that causes some channels to transition to the open state even in the absence of voltage-sensor movement. To interpret these results, we adopt an allosteric gating scheme wherein KCNQ1 is able to transition to the open state after zero to four voltage-sensor movements. This model allows for widely varying gating behavior, depending on the relative strength of the opening transition, and suggests how KCNQ1 could be controlled by coassembly with different KCNE family members.
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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.