ArticlePloS one2011
Gating of a pH-sensitive K(2P) potassium channel by an electrostatic effect of basic sensor residues on the selectivity filter.
Article in PloS one, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 38 citations in OpenAlex.
- The TASK-1 and TASK-3 activator JG-C3-98 attenuates cold and mechanical responses in primary somatosensory neurons.Frontiers in pharmacology · 2026Article
- Cell Settling, Migration, and Stochastic Cancer Gene Expression Suggest Potassium Membrane Flux May Initiate pH Reversal.Biomolecules · 2025Article
- Rational design, synthesis, and evaluation of novel polypharmacological compounds targeting NaThe Journal of biological chemistry · 2025Article
- Fine-tuning pH sensor H98 by remote essential residues in the hydrogen-bond network of mTASK-3.International journal of biological macromolecules · 2024Article
- A Direct Interaction between Cyclodextrins and TASK Channels Decreases the Leak Current in Cerebellar Granule Neurons.Biology · 2022Article
- The enigma of environmental pH sensing in plants.Nature plants · 2021Review
- Comparison of KHandbook of experimental pharmacology · 2021Article
- Elucidating the Structural Basis of the Intracellular pH Sensing Mechanism of TASK-2 KInternational journal of molecular sciences · 2020Article
- Structure/Activity Analysis of TASK-3 Channel Antagonists Based on a 5,6,7,8 tetrahydropyrido[4,3-d]pyrimidine.International journal of molecular sciences · 2019Article
- The Insensitivity of TASK-3 K₂P Channels to External Tetraethylammonium (TEA) Partially Depends on the Cap Structure.International journal of molecular sciences · 2018Article
- TASK-3 Downregulation Triggers Cellular Senescence and Growth Inhibition in Breast Cancer Cell Lines.International journal of molecular sciences · 2018Article
- 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
- Intersubunit Concerted Cooperative and cis-Type Mechanisms Modulate Allosteric Gating in Two-Pore-Domain Potassium Channel TREK-2.Frontiers in cellular neuroscience · 2016Article
- The isoforms generated by alternative translation initiation adopt similar conformation in the selectivity filter in TREK-2.Journal of physiology and biochemistry · 2015Article
- TASK-2 K₂p K⁺ channel: thoughts about gating and its fitness to physiological function.Pflugers Archiv : European journal of physiology · 2015Review
- Human trypanolytic factor APOL1 forms pH-gated cation-selective channels in planar lipid bilayers: relevance to trypanosome lysis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Physiological reviews · 2015Review
- G protein modulation of K2P potassium channel TASK-2 : a role of basic residues in the C terminus domain.Pflugers Archiv : European journal of physiology · 2013Article
- An extracellular ion pathway plays a central role in the cooperative gating of a K(2P) K+ channel by extracellular pH.The Journal of biological chemistry · 2013Article
- TASK-2: a K2P K(+) channel with complex regulation and diverse physiological functions.Frontiers in physiology · 2013Article
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Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
K(+) channels share common selectivity characteristics but exhibit a wide diversity in how they are gated open. Leak K(2P) K(+) channels TASK-2, TALK-1 and TALK-2 are gated open by extracellular alkalinization. The mechanism for this alkalinization-dependent gating has been proposed to be the neutralization of the side chain of a single arginine (lysine in TALK-2) residue near the pore of TASK-2, which occurs with the unusual pK(a) of 8.0. We now corroborate this hypothesis by transplanting the TASK-2 extracellular pH (pH(o)) sensor in the background of a pH(o)-insensitive TASK-3 channel, which leads to the restitution of pH(o)-gating. Using a concatenated channel approach, we also demonstrate that for TASK-2 to open, pH(o) sensors must be neutralized in each of the two subunits forming these dimeric channels with no apparent cross-talk between the sensors. These results are consistent with adaptive biasing force analysis of K(+) permeation using a model selectivity filter in wild-type and mutated channels. The underlying free-energy profiles confirm that either a doubly or a singly charged pH(o) sensor is sufficient to abolish ion flow. Atomic detail of the associated mechanism reveals that, rather than a collapse of the pore, as proposed for other K(2P) channels gated at the selectivity filter, an increased height of the energetic barriers for ion translocation accounts for channel blockade at acid pH(o). Our data, therefore, strongly suggest that a cycle of protonation/deprotonation of pH(o)-sensing arginine 224 side chain gates the TASK-2 channel by electrostatically tuning the conformational stability of its selectivity filter.
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