ArticleThe Journal of biological chemistry2013
An extracellular ion pathway plays a central role in the cooperative gating of a K(2P) K+ channel by extracellular pH.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.
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Who cites it
28 citing papers in PubMed, 40 citations in OpenAlex.
- Toward the rational design of oncogenic TASK-3 channel inhibitor peptides and nanoconjugate complexes.Frontiers in pharmacology · 2026Review
- C-type inactivation and proton modulation mechanisms of the TASK3 channel.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- Cooperativity in regulation of membrane protein function: phenomenological analysis of the effects of pH and phospholipids.Biophysical reviews · 2023Review
- Structure of human CALHM1 reveals key locations for channel regulation and blockade by ruthenium red.Nature communications · 2023Article
- Advances in the Understanding of Two-Pore Domain TASK Potassium Channels and Their Potential as Therapeutic Targets.Molecules (Basel, Switzerland) · 2022Review
- A Direct Interaction between Cyclodextrins and TASK Channels Decreases the Leak Current in Cerebellar Granule Neurons.Biology · 2022Article
- Structural Basis for pH-gating of the KNature communications · 2022Article
- Allosteric coupling between transmembrane segment 4 and the selectivity filter of TALK1 potassium channels regulates their gating by extracellular pH.The Journal of biological chemistry · 2022Article
- Negative Influence by the Force: Mechanically Induced Hyperpolarization via KInternational journal of molecular sciences · 2021Review
- Structural Insights into the Mechanisms and Pharmacology of KJournal of molecular biology · 2021Review
- The Polysite Pharmacology of TREK KAdvances in experimental medicine and biology · 2021Article
- Polynuclear Ruthenium Amines Inhibit KCell chemical biology · 2020Article
- Effects of the ventilatory stimulant, doxapram on human TASK-3 (KCNK9, K2P9.1) channels and TASK-1 (KCNK3, K2P3.1) channels.Acta physiologica (Oxford, England) · 2020Article
- 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
- An allosteric ligand-binding site in the extracellular cap of K2P channels.Nature communications · 2017Article
- Functional TASK-3-Like Channels in Mitochondria of Aldosterone-Producing Zona Glomerulosa Cells.Hypertension (Dallas, Tex. : 1979) · 2017Article
- Grafting voltage and pharmacological sensitivity in potassium channels.Cell research · 2016Article
- Functional mutagenesis screens reveal the 'cap structure' formation in disulfide-bridge free TASK channels.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proton-gated TASK-3 K(+) channel belongs to the K(2P) family of proteins that underlie the K(+) leak setting the membrane potential in all cells. TASK-3 is under cooperative gating control by extracellular [H(+)]. Use of recently solved K(2P) structures allows us to explore the molecular mechanism of TASK-3 cooperative pH gating. Tunnel-like side portals define an extracellular ion pathway to the selectivity filter. We use a combination of molecular modeling and functional assays to show that pH-sensing histidine residues and K(+) ions mutually interact electrostatically in the confines of the extracellular ion pathway. K(+) ions modulate the pK(a) of sensing histidine side chains whose charge states in turn determine the open/closed transition of the channel pore. Cooperativity, and therefore steep dependence of TASK-3 K(+) channel activity on extracellular pH, is dependent on an effect of the permeant ion on the channel pH(o) sensors.
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Registered trials
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.