ArticleThe Journal of physiology2009
The response of the tandem pore potassium channel TASK-3 (K(2P)9.1) to voltage: gating at the cytoplasmic mouth.
Article in The Journal of physiology, 2009. 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, 36 citations in OpenAlex.
- Structures of TASK-1 and TASK-3 K2P channels provide insight into their gating and dysfunction in disease.Structure (London, England : 1993) · 2025Article
- Gain-of-function mutations in KCNK3 cause a developmental disorder with sleep apnea.Nature genetics · 2022Article
- Gain and loss of TASK3 channel function and its regulation by novel variation cause KCNK9 imprinting syndrome.Genome medicine · 2022Article
- Structural Insights into the Mechanisms and Pharmacology of KJournal of molecular biology · 2021Review
- Routes for Potassium Ions across Mitochondrial Membranes: A Biophysical Point of View with Special Focus on the ATP-Sensitive KBiomolecules · 2021Review
- TRESK background potassium channel is not gated at the helix bundle crossing near the cytoplasmic end of the pore.PloS one · 2018Article
- Grafting voltage and pharmacological sensitivity in potassium channels.Cell research · 2016Article
- Allosteric coupling between proximal C-terminus and selectivity filter is facilitated by the movement of transmembrane segment 4 in TREK-2 channel.Scientific reports · 2016Article
- Much more than a leak: structure and function of K₂p-channels.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
- Potassium channel in the mitochondria of human keratinocytes.The Journal of investigative dermatology · 2014Article
- A new TASK for Dipeptidyl Peptidase-like Protein 6.PloS one · 2013Article
- The pore structure and gating mechanism of K2P channels.The EMBO journal · 2011Article
- Multiple modalities converge on a common gate to control K2P channel function.The EMBO journal · 2011Article
- Gating of two pore domain potassium channels.The Journal of physiology · 2010Review
- The response of the tandem pore potassium channel TASK-3 (K(2P)9.1) to voltage: gating at the cytoplasmic mouth.The Journal of physiology · 2009Article
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Authors and funding
7 authors at 3 institutions in 1 country.
Funding
Abstract
Although the tandem pore potassium channel TASK-3 is thought to open and shut at its selectivity filter in response to changes of extracellular pH, it is currently unknown whether the channel also shows gating at its inner, cytoplasmic mouth through movements of membrane helices M2 and M4. We used two electrode voltage clamp and single channel recording to show that TASK-3 responds to voltage in a way that reveals such gating. In wild-type channels, P(open) was very low at negative voltages, but increased with depolarisation. The effect of voltage was relatively weak and the gating charge small, 0.17. Mutants A237T (in M4) and N133A (in M2) increased P(open) at a given voltage, increasing mean open time and the number of openings per burst. In addition, the relationship between P(open) and voltage was shifted to less positive voltages. Mutation of putative hinge glycines (G117A, G231A), residues that are conserved throughout the tandem pore channel family, reduced P(open) at a given voltage, shifting the relationship with voltage to a more positive potential range. None of these mutants substantially affected the response of the channel to extracellular acidification. We have used the results from single channel recording to develop a simple kinetic model to show how gating occurs through two classes of conformation change, with two routes out of the open state, as expected if gating occurs both at the selectivity filter and at its cytoplasmic mouth.
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