ArticlePloS one2012
The electrically silent Kv6.4 subunit confers hyperpolarized gating charge movement in Kv2.1/Kv6.4 heterotetrameric channels.
Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- A silent Kv channel subunit shapes PV neuron action potential waveform and short-term synaptic plasticity during high-frequency firing.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- A silent Kv channel subunit shapes PV neuron action potential waveform and short-term synaptic plasticity during high-frequency firing.bioRxiv : the preprint server for biology · 2025Article
- Kv2/Kv6.4 Heteromeric Potassium Channels Are Expressed in Spinal Motoneurons and Localized at C-Bouton Synapses.The European journal of neuroscience · 2025Article
- Gene expression correlates and mechanistic insights into electric organ discharge duration changes in mormyrid electric fish.The Journal of experimental biology · 2025Article
- A Kv2 inhibitor combination reveals native neuronal conductances consistent with Kv2/KvS heteromers.eLife · 2025Article
- Regulation of Kv2.1 Channels by Kv9.1 Variants.Biomedicines · 2025Article
- KCNG4 Genetic Variant Linked to Migraine Prevents Expression of KCNB1.International journal of molecular sciences · 2024Article
- A broad survey of choanoflagellates revises the evolutionary history of the Shaker family of voltage-gated KProceedings of the National Academy of Sciences of the United States of America · 2024Article
- What is the correct stoichiometry of Kv2.1:Kv6.4 heteromers?Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Western influenced lifestyle and Kv2.1 association as predicted biomarkers for Tunisian colorectal cancer.BMC cancer · 2020Article
- Human Labor Pain Is Influenced by the Voltage-Gated Potassium Channel KCell reports · 2020Article
- Determining the correct stoichiometry of Kv2.1/Kv6.4 heterotetramers, functional in multiple stoichiometrical configurations.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Kv2.1 channels play opposing roles in regulating membrane potential, CaProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Article
- Transcriptomics Analysis of Porcine Caudal Dorsal Root Ganglia in Tail Amputated Pigs Shows Long-Term Effects on Many Pain-Associated Genes.Frontiers in veterinary science · 2019Article
- Independent movement of the voltage sensors in KScientific reports · 2017Article
- Kv5, Kv6, Kv8, and Kv9 subunits: No simple silent bystanders.The Journal of general physiology · 2016Review
- Modulation of Closed-State Inactivation in Kv2.1/Kv6.4 Heterotetramers as Mechanism for 4-AP Induced Potentiation.PloS one · 2015Article
- Oxidation of KCNB1 K(+) channels in central nervous system and beyond.World journal of biological chemistry · 2014Review
- Kv2 dysfunction after peripheral axotomy enhances sensory neuron responsiveness to sustained input.Experimental neurology · 2014Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The voltage-gated K(+) (Kv) channel subunit Kv6.4 does not form functional homotetrameric channels but co-assembles with Kv2.1 to form functional Kv2.1/Kv6.4 heterotetrameric channels. Compared to Kv2.1 homotetramers, Kv6.4 exerts a ~40 mV hyperpolarizing shift in the voltage-dependence of Kv2.1/Kv6.4 channel inactivation, without a significant effect on activation gating. However, the underlying mechanism of this Kv6.4-induced modulation of Kv2.1 channel inactivation, and whether the Kv6.4 subunit participates in the voltage-dependent gating of heterotetrameric channels is not well understood. Here we report distinct gating charge movement of Kv2.1/Kv6.4 heterotetrameric channels, compared to Kv2.1 homotetramers, as revealed by gating current recordings from mammalian cells expressing these channels. The gating charge movement of Kv2.1/Kv6.4 heterotetrameric channels displayed an extra component around the physiological K(+) equilibrium potential, characterized by a second sigmoidal relationship of the voltage-dependence of gating charge movement. This distinct gating charge displacement reflects movement of the Kv6.4 voltage-sensing domain and has a voltage-dependency that matches the hyperpolarizing shift in Kv2.1/Kv6.4 channel inactivation. These results provide a mechanistic basis for the modulation of Kv2.1 channel inactivation gating kinetics by silent Kv6.4 subunits.
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