ArticleBiophysical journal2007
An inactivation gate in the selectivity filter of KCNQ1 potassium channels.
Article in Biophysical journal, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed.
- Barium senses subtle pore changes in a voltage-gated KScience advances · 2026Article
- Do selectivity filter carbonyls in KJournal of structural biology: X · 2024Article
- A benzodiazepine activator locks KCommunications biology · 2022Article
- P-Loop Channels: Experimental Structures, and Physics-Based and Neural Networks-Based Models.Membranes · 2022Review
- ML277 regulates KCNQ1 single-channel amplitudes and kinetics, modified by voltage sensor state.The Journal of general physiology · 2021Article
- A unique mechanism of inactivation gating of the Kv channel family member Kv7.1 and its modulation by PIP2 and calmodulin.Science advances · 2020Article
- Gating and Regulation of KCNQ1 and KCNQ1 + KCNE1 Channel Complexes.Frontiers in physiology · 2020Review
- ML277 specifically enhances the fully activated open state of KCNQ1 by modulating VSD-pore coupling.eLife · 2019Article
- Mechanisms Underlying the Dual Effect of Polyunsaturated Fatty Acid Analogs on Kv7.1.Cell reports · 2018Article
- Inactivation gating of Kv7.1 channels does not involve concerted cooperative subunit interactions.Channels (Austin, Tex.) · 2018Article
- Inactivation of KCNQ1 potassium channels reveals dynamic coupling between voltage sensing and pore opening.Nature communications · 2017Article
- Voltage-Dependent Gating: Novel Insights from KCNQ1 Channels.Biophysical journal · 2016Review
- Tuning of EAG K(+) channel inactivation: molecular determinants of amplification by mutations and a small molecule.The Journal of general physiology · 2012Article
- Pore helix-S6 interactions are critical in governing current amplitudes of KCNQ3 K+ channels.Biophysical journal · 2012Article
- External Ba2+ block of the two-pore domain potassium channel TREK-1 defines conformational transition in its selectivity filter.The Journal of biological chemistry · 2011Article
- Extracellular potassium inhibits Kv7.1 potassium channels by stabilizing an inactivated state.Biophysical journal · 2011Article
- The S4-S5 linker of KCNQ1 channels forms a structural scaffold with the S6 segment controlling gate closure.The Journal of biological chemistry · 2011Article
- Molecular basis of decreased Kir4.1 function in SeSAME/EAST syndrome.Journal of the American Society of Nephrology : JASN · 2010Article
- Determinants within the turret and pore-loop domains of KCNQ3 K+ channels governing functional activity.Biophysical journal · 2008Article
- External Ba2+ block of human Kv1.5 at neutral and acidic pH: evidence for Ho+-induced constriction of the outer pore mouth at rest.Biophysical journal · 2008Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Inactivation is an inherent property of most voltage-gated K(+) channels. While fast N-type inactivation has been analyzed in biophysical and structural details, the mechanisms underlying slow inactivation are yet poorly understood. Here, we characterized a slow inactivation mechanism in various KCNQ1 pore mutants, including L273F, which hinders entry of external Ba(2+) to its deep site in the pore and traps it by slowing its egress. Kinetic studies, molecular modeling, and dynamics simulations suggest that this slow inactivation involves conformational changes that converge to the outer carbonyl ring of the selectivity filter, where the backbone becomes less flexible. This mechanism involves acceleration of inactivation kinetics and enhancement of Ba(2+) trapping at elevated external K(+) concentrations. Hence, KCNQ1 slow inactivation considerably differs from C-type inactivation where vacation of K(+) from the filter was invoked. We suggest that trapping of K(+) at s(1) due to filter rigidity and hindrance of the dehydration-resolvation transition underlie the slow inactivation of KCNQ1 pore mutants.
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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.