ArticleThe Journal of general physiology2010
Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1.
Article in The Journal of general physiology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 47 citations in OpenAlex.
- Functional Profiling ofCirculation. Genomic and precision medicine · 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
- Long-QT mutations in KCNE1 modulate the 17β-estradiol response of Kv7.1/KCNE1.Science advances · 2023Article
- Article
- Physical and functional interaction sites in cytoplasmic domains of KCNQ1 and KCNE1 channel subunits.American journal of physiology. Heart and circulatory physiology · 2020Article
- Mutational and phenotypic spectra of KCNE1 deficiency in Jervell and Lange-Nielsen Syndrome and Romano-Ward Syndrome.Human mutation · 2019Article
- The IBiophysical journal · 2018Article
- Effects of β-subunit on gating of a potassium ion channel: Molecular simulations of cardiac IKs activation.Journal of molecular and cellular cardiology · 2018Article
- Engineered Cross-Linking to Study the Pore Architecture of the CRAC Channel.Methods in molecular biology (Clifton, N.J.) · 2018Article
- KCNE1 and KCNE3 modulate KCNQ1 channels by affecting different gating transitions.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Structural basis for KCNE3 modulation of potassium recycling in epithelia.Science advances · 2016Article
- Review
- Voltage-Dependent Gating: Novel Insights from KCNQ1 Channels.Biophysical journal · 2016Review
- Probing binding sites and mechanisms of action of an I(Ks) activator by computations and experiments.Biophysical journal · 2015Article
- Article
- KCNE1 divides the voltage sensor movement in KCNQ1/KCNE1 channels into two steps.Nature communications · 2014Article
- Building KCNQ1/KCNE1 channel models and probing their interactions by molecular-dynamics simulations.Biophysical journal · 2013Article
- Probing the structural basis for differential KCNQ1 modulation by KCNE1 and KCNE2.The Journal of general physiology · 2012Article
- The KCNE Tango - How KCNE1 Interacts with Kv7.1.Frontiers in pharmacology · 2012Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
KCNQ1 channels assemble with KCNE1 transmembrane (TM) peptides to form voltage-gated K(+) channel complexes with slow activation gate opening. The cytoplasmic C-terminal domain that abuts the KCNE1 TM segment has been implicated in regulating KCNQ1 gating, yet its interaction with KCNQ1 has not been described. Here, we identified a protein-protein interaction between the KCNE1 C-terminal domain and the KCNQ1 S6 activation gate and S4-S5 linker. Using cysteine cross-linking, we biochemically screened over 300 cysteine pairs in the KCNQ1-KCNE1 complex and identified three residues in KCNQ1 (H363C, P369C, and I257C) that formed disulfide bonds with cysteine residues in the KCNE1 C-terminal domain. Statistical analysis of cross-link efficiency showed that H363C preferentially reacted with KCNE1 residues H73C, S74C, and D76C, whereas P369C showed preference for only D76C. Electrophysiological investigation of the mutant K(+) channel complexes revealed that the KCNQ1 residue, H363C, formed cross-links not only with KCNE1 subunits, but also with neighboring KCNQ1 subunits in the complex. Cross-link formation involving the H363C residue was state dependent, primarily occurring when the KCNQ1-KCNE1 complex was closed. Based on these biochemical and electrophysiological data, we generated a closed-state model of the KCNQ1-KCNE1 cytoplasmic region where these protein-protein interactions are poised to slow activation gate opening.
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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.