ArticleThe Journal of general physiology2006
Na+ permeation and block of hERG potassium channels.
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 16 papers.
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Who cites it
16 citing papers in PubMed, 41 citations in OpenAlex.
- Amiodarone irrecoverably impairs the function of human ether-a-go-go-related gene potassium channels.Molecular pharmacology · 2026Article
- Potassium dependent structural changes in the selectivity filter of HERG potassium channels.Nature communications · 2024Article
- An LQT2-related mutation in the voltage-sensing domain is involved in switching the gating polarity of hERG.BMC biology · 2024Article
- Early Steps in C-Type Inactivation of the hERG Potassium Channel.Journal of chemical information and modeling · 2023Article
- A General Model of Ion Passive Transmembrane Transport Based on Ionic Concentration.Frontiers in computational neuroscience · 2018Article
- Dynamics of the EAG1 KBiochemical and biophysical research communications · 2017Article
- Exploring the Dynamics of the TWIK-1 Channel.Biophysical journal · 2016Article
- Molecular determinants of pentamidine-induced hERG trafficking inhibition.Molecular pharmacology · 2012Article
- Blockade of permeation by potassium but normal gating of the G628S nonconducting hERG channel mutant.Biophysical journal · 2011Article
- The role of monoubiquitination in endocytic degradation of human ether-a-go-go-related gene (hERG) channels under low K+ conditions.The Journal of biological chemistry · 2011Article
- Mapping the sequence of conformational changes underlying selectivity filter gating in the K(v)11.1 potassium channel.Nature structural & molecular biology · 2011Article
- The calmodulin inhibitor N-(6-aminohexyl)-5-chloro-1-naphthalene sulphonamide directly blocks human ether à-go-go-related gene potassium channels stably expressed in human embryonic kidney 293 cells.British journal of pharmacology · 2010Article
- Intracellular potassium stabilizes human ether-à-go-go-related gene channels for export from endoplasmic reticulum.Molecular pharmacology · 2009Article
- The 5-HT2 antagonist ketanserin is an open channel blocker of human cardiac ether-à-go-go-related gene (hERG) potassium channels.British journal of pharmacology · 2008Article
- Probing the outer mouth structure of the HERG channel with peptide toxin footprinting and molecular modeling.Biophysical journal · 2007Article
- Linkage between 'disruption of inactivation' and 'reduction of K+ selectivity' among hERG mutants in the S5-P linker region.The Journal of physiology · 2006Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inactivation gating of hERG channels is important for the channel function and drug-channel interaction. Whereas hERG channels are highly selective for K+, we have found that inactivated hERG channels allow Na+ to permeate in the absence of K+. This provides a new way to directly monitor and investigate hERG inactivation. By using whole cell patch clamp method with an internal solution containing 135 mM Na+ and an external solution containing 135 mM NMG+, we recorded a robust Na+ current through hERG channels expressed in HEK 293 cells. Kinetic analyses of the hERG Na+ and K+ currents indicate that the channel experiences at least two states during the inactivation process, an initial fast, less stable state followed by a slow, more stable state. The Na+ current reflects Na+ ions permeating through the fast inactivated state but not through the slow inactivated state or open state. Thus the hERG Na+ current displayed a slow inactivation as the channels travel from the less stable, fast inactivated state into the more stable, slow inactivated state. Removal of fast inactivation by the S631A mutation abolished the Na+ current. Moreover, acceleration of fast inactivation by mutations T623A, F627Y, and S641A did not affect the hERG Na+ current, but greatly diminished the hERG K+ current. We also found that external Na+ potently blocked the hERG outward Na+ current with an IC50 of 3.5 mM. Mutations in the channel pore and S6 regions, such as S624A, F627Y, and S641A, abolished the inhibitory effects of external Na+ on the hERG Na+ current. Na+ permeation and blockade of hERG channels provide novel ways to extend our understanding of the hERG gating mechanisms.
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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.