ArticleThe Journal of general physiology2012
Characterization of KCNQ1 atrial fibrillation mutations reveals distinct dependence on KCNE1.
Article in The Journal of general physiology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed, 36 citations in OpenAlex.
- MultimodalCirculation · 2026Article
- A physiologically-relevant intermediate state structure of a voltage-gated potassium channel.Nature communications · 2025Article
- A general mechanism of KCNE1 modulation of KCNQ1 channels involving non-canonical VSD-PD coupling.Communications biology · 2021Article
- Insights into Cardiac IKs (KCNQ1/KCNE1) Channels Regulation.International journal of molecular sciences · 2020Review
- Article
- Genetics and Epigenetics of Atrial Fibrillation.International journal of molecular sciences · 2020Review
- Structures Illuminate Cardiac Ion Channel Functions in Health and in Long QT Syndrome.Frontiers in pharmacology · 2020Review
- ML277 specifically enhances the fully activated open state of KCNQ1 by modulating VSD-pore coupling.eLife · 2019Article
- Chronic in vivo angiotensin II administration differentially modulates the slow delayed rectifier channels in atrial and ventricular myocytes.Heart rhythm · 2019Article
- Article
- Photo-Cross-Linking of IBiophysical journal · 2017Article
- Gating mechanisms underlying deactivation slowing by two KCNQ1 atrial fibrillation mutations.Scientific reports · 2017Article
- Voltage-Dependent Gating: Novel Insights from KCNQ1 Channels.Biophysical journal · 2016Review
- Article
- Short QT and atrial fibrillation: AHeartRhythm case reports · 2015Article
- KCNQ1 channel modulation by KCNE proteins via the voltage-sensing domain.The Journal of physiology · 2015Review
- Article
- Purification and structural study of the voltage-sensor domain of the human KCNQ1 potassium ion channel.Biochemistry · 2014Article
- A KCNQ1 mutation causes age-dependant bradycardia and persistent atrial fibrillation.Pflugers Archiv : European journal of physiology · 2014Article
- Building KCNQ1/KCNE1 channel models and probing their interactions by molecular-dynamics simulations.Biophysical journal · 2013Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 3 countries.
Funding
Abstract
The I(Ks) potassium channel, critical to control of heart electrical activity, requires assembly of α (KCNQ1) and β (KCNE1) subunits. Inherited mutations in either I(Ks) channel subunit are associated with cardiac arrhythmia syndromes. Two mutations (S140G and V141M) that cause familial atrial fibrillation (AF) are located on adjacent residues in the first membrane-spanning domain of KCNQ1, S1. These mutations impair the deactivation process, causing channels to appear constitutively open. Previous studies suggest that both mutant phenotypes require the presence of KCNE1. Here we found that despite the proximity of these two mutations in the primary protein structure, they display different functional dependence in the presence of KCNE1. In the absence of KCNE1, the S140G mutation, but not V141M, confers a pronounced slowing of channel deactivation and a hyperpolarizing shift in voltage-dependent activation. When coexpressed with KCNE1, both mutants deactivate significantly slower than wild-type KCNQ1/KCNE1 channels. The differential dependence on KCNE1 can be correlated with the physical proximity between these positions and KCNE1 as shown by disulfide cross-linking studies: V141C forms disulfide bonds with cysteine-substituted KCNE1 residues, whereas S140C does not. These results further our understanding of the structural relationship between KCNE1 and KCNQ1 subunits in the I(Ks) channel, and provide mechanisms for understanding the effects on channel deactivation underlying these two atrial fibrillation mutations.
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