ArticleProceedings of the National Academy of Sciences of the United States of America2020
Determining the correct stoichiometry of Kv2.1/Kv6.4 heterotetramers, functional in multiple stoichiometrical configurations.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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14 citing papers in PubMed, 42 citations in OpenAlex.
- 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 Historical Outline of Fluorescence Spectroscopy in Ion Channel Research.Advances in experimental medicine and biology · 2026Review
- 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
- Functional control of heteromeric Kv2.1/6.4 channels by the voltage sensor domain of the silent Kv6.4 subunit.The Journal of physiology · 2025Article
- Regulation of Kv2.1 Channels by Kv9.1 Variants.Biomedicines · 2025Article
- The Electrically Silent Kv5.1 Subunit Forms Heteromeric Kv2 Channels in Cortical Neurons and Confers Distinct Functional Properties.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2025Article
- KCNG4 Genetic Variant Linked to Migraine Prevents Expression of KCNB1.International journal of molecular sciences · 2024Article
- A versatile functional interaction between electrically silent KCellular and molecular life sciences : CMLS · 2024Article
- Identifiability of equilibrium constants for receptors with two to five binding sites.The Journal of general physiology · 2023Article
- Retinoschisin and novel Na/K-ATPase interaction partners Kv2.1 and Kv8.2 define a growing protein complex at the inner segments of mammalian photoreceptors.Cellular and molecular life sciences : CMLS · 2022Article
- A strategy for determining the equilibrium constants for heteromeric ion channels in a complex model.The Journal of general physiology · 2022Article
- Pentameric assembly of the Kv2.1 tetramerization domain.Acta crystallographica. Section D, Structural biology · 2022Article
- Reply to Pisupati et al.: Evaluating single subunit counting data to find the correct stoichiometry.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- 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
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5 authors at 2 institutions in 2 countries.
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Abstract
The electrically silent (KvS) members of the voltage-gated potassium (Kv) subfamilies Kv5, Kv6, Kv8, and Kv9 selectively modulate Kv2 subunits by forming heterotetrameric Kv2/KvS channels. Based on the reported 3:1 stoichiometry of Kv2.1/Kv9.3 channels, we tested the hypothesis that Kv2.1/Kv6.4 channels express, in contrast to the assumed 3:1, in a 2:2 stoichiometry. We investigate the Kv2.1/Kv6.4 stoichiometry using single subunit counting and functional characterization of tetrameric concatemers. For selecting the most probable stoichiometry, we introduce a model-selection method that is applicable for any multimeric complex by investigating the stoichiometry of Kv2.1/Kv6.4 channels. Weighted likelihood calculations bring rigor to a powerful technique. Using the weighted-likelihood model-selection method and analysis of electrophysiological data, we show that Kv2.1/Kv6.4 channels express, in contrast to the assumed 3:1, in a 2:2 stoichiometry. Within this stoichiometry, the Kv6.4 subunits have to be positioned alternating with Kv2.1 to express functional channels. The variability in Kv2/KvS assembly increases the diversity of heterotetrameric configurations and extends the regulatory possibilities of KvS by allowing the presence of more than one silent subunit.
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