ArticleBiophysical journal1999
Contribution of the selectivity filter to inactivation in potassium channels.
Article in Biophysical journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 102 papers.
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Who cites it
102 citing papers in PubMed.
- Constitutive sodium permeability in aProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Stability of N-type inactivation and the coupling between N-type and C-type inactivation in the Aplysia Kv1 channel.Pflugers Archiv : European journal of physiology · 2024Article
- Dilation of ion selectivity filters in cation channels.Trends in biochemical sciences · 2024Review
- Genetically-encoded BRET probes shed light on ligand bias-induced variable ion selectivity in TRPV1 and P2X5/7.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Probing the Structural Dynamics of the Activation Gate of KcsA Using Homo-FRET Measurements.International journal of molecular sciences · 2021Article
- Regulation of KMembranes · 2021Article
- The Selectivity Filter Is Involved in the U-Type Inactivation Process of Kv2.1 and Kv3.1 Channels.Biophysical journal · 2020Article
- Accessibility of Cations to the Selectivity Filter of KcsA in the Inactivated State: An Equilibrium Binding Study.International journal of molecular sciences · 2019Article
- Key role of segment IS4 in Cav1.2 inactivation: link between activation and inactivation.Pflugers Archiv : European journal of physiology · 2017Article
- Probing the Effects of Gating on the Ion Occupancy of the KJournal of the American Chemical Society · 2017Article
- Ion channels and ion selectivity.Essays in biochemistry · 2017Review
- Exploring the Dynamics of the TWIK-1 Channel.Biophysical journal · 2016Article
- Grafting voltage and pharmacological sensitivity in potassium channels.Cell research · 2016Article
- Multi-ion free energy landscapes underscore the microscopic mechanism of ion selectivity in the KcsA channel.Biochimica et biophysica acta · 2016Article
- Ion-binding properties of a K+ channel selectivity filter in different conformations.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- TASK-2 K₂p K⁺ channel: thoughts about gating and its fitness to physiological function.Pflugers Archiv : European journal of physiology · 2015Review
- Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Physiological reviews · 2015Review
- Altered and dynamic ion selectivity of K+ channels in cell development and excitability.Trends in pharmacological sciences · 2014Review
- Hydrogen bonds as molecular timers for slow inactivation in voltage-gated potassium channels.eLife · 2013Article
- ShakerIR and Kv1.5 mutant channels with enhanced slow inactivation also exhibit K⁺ o-dependent resting inactivation.Pflugers Archiv : European journal of physiology · 2013Article
42 more citing papers are in PubMed but not listed here.
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Voltage-gated K+ channels exhibit a slow inactivation process, which becomes an important influence on the rate of action potential repolarization during prolonged or repetitive depolarization. During slow inactivation, the outer mouth of the permeation pathway undergoes a conformational change. We report here that during the slow inactivation process, the channel progresses through at least three permeation states; from the initial open state that is highly selective for K+, the channel enters a state that is less permeable to K+ and more permeable to Na+, and then proceeds to a state that is non-conducting. Similar results were obtained in three different voltage-gated K+ channels: Kv2.1, a channel derived from Shaker (Shaker Delta A463C), and a chimeric channel derived from Kv2.1 and Kv1.3 that displays classical C-type inactivation. The change in selectivity displayed both voltage- and time-dependent properties of slow inactivation and was observed with K+ on either side of the channel. Elevation of internal [K+] inhibited Na+ conduction through the inactivating channel in a concentration-dependent manner. These results indicate that the change in selectivity filter function is an integral part of the slow inactivation mechanism, and argue against the hypothesis that the inactivation gate is independent from the selectivity filter. Thus, these data suggest that the selectivity filter is itself the inactivation gate.
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