ArticleThe Journal of general physiology2006
Secondary structure of a KCNE cytoplasmic domain.
Article in The Journal of general physiology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 37 citations in OpenAlex.
- Functional Profiling ofCirculation. Genomic and precision medicine · 2025Article
- The Expression, Purification, Spectroscopic Characterization, and Membrane Topology Classification of KCNE4 from RecombinantThe journal of physical chemistry. B · 2025Article
- High-throughput functional mapping of variants in an arrhythmia gene, KCNE1, reveals novel biology.Genome medicine · 2024Article
- Long-QT mutations in KCNE1 modulate the 17β-estradiol response of Kv7.1/KCNE1.Science advances · 2023Article
- Physical and functional interaction sites in cytoplasmic domains of KCNQ1 and KCNE1 channel subunits.American journal of physiology. Heart and circulatory physiology · 2020Article
- KCNQs: Ligand- and Voltage-Gated Potassium Channels.Frontiers in physiology · 2020Review
- Structural basis for KCNE3 modulation of potassium recycling in epithelia.Science advances · 2016Article
- Reconstitution of KCNE1 into lipid bilayers: comparing the structural, dynamic, and activity differences in micelle and vesicle environments.Biochemistry · 2011Article
- KCNQ1 subdomains involved in KCNE modulation revealed by an invertebrate KCNQ1 orthologue.The Journal of general physiology · 2011Article
- Xenopus laevis oocytes infected with multi-drug-resistant bacteria: implications for electrical recordings.The Journal of general physiology · 2011Article
- KCNE1 enhances phosphatidylinositol 4,5-bisphosphate (PIP2) sensitivity of IKs to modulate channel activity.Proceedings of the National Academy of Sciences of the United States of America · 2011Article
- Identification of a protein-protein interaction between KCNE1 and the activation gate machinery of KCNQ1.The Journal of general physiology · 2010Article
- Analysis of the interactions between the C-terminal cytoplasmic domains of KCNQ1 and KCNE1 channel subunits.The Biochemical journal · 2010Article
- Article
- Intracellular domains interactions and gated motions of I(KS) potassium channel subunits.The EMBO journal · 2009Article
- Dynamic partnership between KCNQ1 and KCNE1 and influence on cardiac IKs current amplitude by KCNE2.The Journal of biological chemistry · 2009Article
- KCNE4 domains required for inhibition of KCNQ1.The Journal of physiology · 2009Article
- Structure of KCNE1 and implications for how it modulates the KCNQ1 potassium channel.Biochemistry · 2008Article
- Structural models for the KCNQ1 voltage-gated potassium channel.Biochemistry · 2007Article
- Role of the S6 C-terminus in KCNQ1 channel gating.The Journal of physiology · 2007Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Type I transmembrane KCNE peptides contain a conserved C-terminal cytoplasmic domain that abuts the transmembrane segment. In KCNE1, this region is required for modulation of KCNQ1 K(+) channels to afford the slowly activating cardiac I(Ks) current. We utilized alanine/leucine scanning to determine whether this region possesses any secondary structure and to identify the KCNE1 residues that face the KCNQ1 channel complex. Helical periodicity analysis of the mutation-induced perturbations in voltage activation and deactivation kinetics of KCNQ1-KCNE1 complexes defined that the KCNE1 C terminus is alpha-helical when split in half at a conserved proline residue. This helical rendering assigns all known long QT mutations in the KCNE1 C-terminal domain as protein facing. The identification of a secondary structure within the KCNE1 C-terminal domain provides a structural scaffold to map protein-protein interactions with the pore-forming KCNQ1 subunit as well as the cytoplasmic regulatory proteins anchored to KCNQ1-KCNE complexes.
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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.