ArticleBiochemistry2008
Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel.
Article in Biochemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.
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Who cites it
126 citing papers in PubMed, 199 citations in OpenAlex.
- Aberrant TMPRSS6-Protease Regulation of Disease Mutant HCN4-KCNE1 Channel Complex Depends on the KCNE1-G38S Polymorphism.Archiv der Pharmazie · 2026Article
- Functions of the KCNE Gene Family in Ion Channels.Biochemical genetics · 2026Review
- Voltage-dependent potassium channel regulatory subunits in the immune system.Biophysical reviews · 2026Review
- Vinyl ether maleic acid block copolymers: a versatile platform for tunable self-assembled lipid nanodiscs and membrane protein characterization.Polymer chemistry · 2026Article
- A physiologically-relevant intermediate state structure of a voltage-gated potassium channel.Nature communications · 2025Article
- Structural Dynamics and Topology of Human KCNE3 in Lipid Bilayers Studied by Site-Directed Spin Labeling and Electron Paramagnetic Resonance Spectroscopy.The journal of physical chemistry. B · 2025Article
- The Expression, Purification, Spectroscopic Characterization, and Membrane Topology Classification of KCNE4 from RecombinantThe journal of physical chemistry. B · 2025Article
- Vinyl Ether Maleic Acid Polymers: Tunable Polymers for Self-Assembled Lipid Nanodiscs and Environments for Membrane Proteins.Biomacromolecules · 2024Article
- Dynamic protein-protein interactions of KCNQ1 and KCNE1 measured by EPR line shape analysis.Biochimica et biophysica acta. Biomembranes · 2024Article
- Modulation of potassium channels by transmembrane auxiliary subunits via voltage-sensing domains.Physiological reports · 2024Review
- Perspective on the Effect of Membrane Mimetics on Dynamic Properties of Integral Membrane Proteins.The journal of physical chemistry. B · 2023Review
- Long-QT mutations in KCNE1 modulate the 17β-estradiol response of Kv7.1/KCNE1.Science advances · 2023Article
- Modulation of the IBBA advances · 2023Article
- Article
- The genetics of drug-induced QT prolongation: evaluating the evidence for pharmacodynamic variants.Pharmacogenomics · 2022Review
- Characterization of interactions within the Igα/Igβ transmembrane domains of the human B-cell receptor provides insights into receptor assembly.The Journal of biological chemistry · 2022Article
- Dengue virus NS4B protein as a target for developing antivirals.Frontiers in cellular and infection microbiology · 2022Review
- Crucial Genes in Aortic Dissection Identified by Weighted Gene Coexpression Network Analysis.Journal of immunology research · 2022Article
- Calmodulin-dependent KCNE4 dimerization controls membrane targeting.Scientific reports · 2021Article
- Fluorescence Fluctuation Spectroscopy enables quantification of potassium channel subunit dynamics and stoichiometry.Scientific reports · 2021Article
66 more citing papers are in PubMed but not listed here.
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
Abstract
KCNE1 is a single-span membrane protein that modulates the voltage-gated potassium channel KCNQ1 (K V7.1) by slowing activation and enhancing channel conductance to generate the slow delayed rectifier current ( I Ks) that is critical for the repolarization phase of the cardiac action potential. Perturbation of channel function by inherited mutations in KCNE1 or KCNQ1 results in increased susceptibility to cardiac arrhythmias and sudden death with or without accompanying deafness. Here, we present the three-dimensional structure of KCNE1. The transmembrane domain (TMD) of KCNE1 is a curved alpha-helix and is flanked by intra- and extracellular domains comprised of alpha-helices joined by flexible linkers. Experimentally restrained docking of the KCNE1 TMD to a closed state model of KCNQ1 suggests that KCNE1 slows channel activation by sitting on and restricting the movement of the S4-S5 linker that connects the voltage sensor to the pore domain. We postulate that this is an adhesive interaction that must be disrupted before the channel can be opened in response to membrane depolarization. Docking to open KCNQ1 indicates that the extracellular end of the KCNE1 TMD forms an interface with an intersubunit cleft in the channel that is associated with most known gain-of-function disease mutations. Binding of KCNE1 to this "gain-of-function cleft" may explain how it increases conductance and stabilizes the open state. These working models for the KCNE1-KCNQ1 complexes may be used to formulate testable hypotheses for the molecular bases of disease phenotypes associated with the dozens of known inherited mutations in KCNE1 and KCNQ1.
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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.