ArticleBiophysical journal2004
Ionic permeation and conduction properties of neuronal KCNQ2/KCNQ3 potassium channels.
Article in Biophysical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 45 citations in OpenAlex.
- Molecular dynamics of the pathogenic KCNQ2 variant G256W reveal mechanisms of channel dysfunction in epileptic encephalopathy.bioRxiv : the preprint server for biology · 2025Article
- Constitutive opening of the Kv7.2 pore activation gate causesProceedings of the National Academy of Sciences of the United States of America · 2024Article
- Electro-mechanical coupling of KCNQ channels is a target of epilepsy-associated mutations and retigabine.Science advances · 2022Article
- ML277 regulates KCNQ1 single-channel amplitudes and kinetics, modified by voltage sensor state.The Journal of general physiology · 2021Article
- Novel Analgesics with Peripheral Targets.Neurotherapeutics : the journal of the American Society for Experimental NeuroTherapeutics · 2020Review
- SMITten for KCNQ Channels.Biophysical journal · 2017Article
- SMIT1 Modifies KCNQ Channel Function and Pharmacology by Physical Interaction with the Pore.Biophysical journal · 2017Article
- Protective role of Kv7 channels in oxygen and glucose deprivation-induced damage in rat caudate brain slices.Journal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2015Article
- The Kv7.2/Kv7.3 heterotetramer assembles with a random subunit arrangement.The Journal of biological chemistry · 2012Article
- Surface expression and subunit specific control of steady protein levels by the Kv7.2 helix A-B linker.PloS one · 2012Article
- Activator-induced dynamic disorder and molecular memory in human two-pore domain hTREK1 K channel.Journal of chemical biology · 2011Article
- Phase response curve analysis of a full morphological globus pallidus neuron model reveals distinct perisomatic and dendritic modes of synaptic integration.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2010Article
- Contribution of KCNQ2 and KCNQ3 to the medium and slow afterhyperpolarization currents.Proceedings of the National Academy of Sciences of the United States of America · 2008Article
- Channel density distributions explain spiking variability in the globus pallidus: a combined physiology and computer simulation database approach.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2008Article
- Role of the S6 C-terminus in KCNQ1 channel gating.The Journal of physiology · 2007Article
- Dopaminergic regulation of neuronal excitability through modulation of Ih in layer V entorhinal cortex.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2006Article
- Three mechanisms underlie KCNQ2/3 heteromeric potassium M-channel potentiation.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2004Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heteromeric KCNQ2/3 potassium channels are thought to underlie the M-current, a subthreshold potassium current involved in the regulation of neuronal excitability. KCNQ channel subunits are structurally unique, but it is unknown whether these structural differences result in unique conduction properties. Heterologously expressed KCNQ2/3 channels showed a permeation sequence of while showing a conduction sequence of A differential contribution of component subunits to the properties of heteromeric KCNQ2/3 channels was demonstrated by studying homomeric KCNQ2 and KCNQ3 channels, which displayed contrasting ionic selectivities. KCNQ2/3 channels did not exhibit an anomalous mole-fraction effect in mixtures of K(+) and Rb(+). However, extreme voltage-dependence of block by external Cs(+) was indicative of multi-ion pore behavior. Block of KCNQ2/3 channels by external Ba(2+) ions was voltage-independent, demonstrating unusual ionic occupation of the outer pore. Selectivity properties and block of KCNQ2 were altered by mutation of outer pore residues in a manner consistent with the presence of multiple ion-binding sites. KCNQ2/3 channel deactivation kinetics were slowed exclusively by Rb(+), whereas activation of KCNQ2/3 channels was altered by a variety of external permeant ions. These data indicate that KCNQ2/3 channels are multi-ion pores which exhibit distinctive mechanisms of ion conduction and gating.
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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.