ArticleProceedings of the National Academy of Sciences of the United States of America2005
pH sensing in the two-pore domain K+ channel, TASK2.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers, 1 of them a synthesis that pooled it.
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Who cites it
24 citing papers in PubMed, 1 synthesis or guideline pooled it, 51 citations in OpenAlex.
- Meta-analysis of 375,000 individuals identifies 38 susceptibility loci for migraine.Nature genetics · 2016Pooled it
- Acid-Base homeostasis in the brain: regional heterogeneity and different Acid-Base transporters.Pflugers Archiv : European journal of physiology · 2026Review
- Cell Settling, Migration, and Stochastic Cancer Gene Expression Suggest Potassium Membrane Flux May Initiate pH Reversal.Biomolecules · 2025Article
- Kir5.1 regulates Kir4.2 expression and is a key component of the 50-pS inwardly rectifying potassium channel in basolateral membrane of mouse proximal tubules.American journal of physiology. Renal physiology · 2025Article
- Fine-tuning pH sensor H98 by remote essential residues in the hydrogen-bond network of mTASK-3.International journal of biological macromolecules · 2024Article
- Kv1.3 Channel Up-Regulation in Peripheral Blood T Lymphocytes of Patients With Multiple Sclerosis.Frontiers in pharmacology · 2021Article
- Dominant-Negative Effect of a Missense Variant in the TASK-2 (KCNK5) K+ Channel Associated with Balkan Endemic Nephropathy.PloS one · 2016Article
- Understanding the Cap Structure in K2P Channels.Frontiers in physiology · 2016Article
- Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Physiological reviews · 2015Review
- TASK-2: a K2P K(+) channel with complex regulation and diverse physiological functions.Frontiers in physiology · 2013Article
- The two-pore domain potassium channel KCNK5: induction by estrogen receptor alpha and role in proliferation of breast cancer cells.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Multiple modalities converge on a common gate to control K2P channel function.The EMBO journal · 2011Article
- Gating of a pH-sensitive K(2P) potassium channel by an electrostatic effect of basic sensor residues on the selectivity filter.PloS one · 2011Article
- Central respiratory chemoreception.The Journal of comparative neurology · 2010Review
- Endolymphatic sodium homeostasis by extramacular epithelium of the saccule.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009Article
- Gating the pore of potassium leak channels.European biophysics journal : EBJ · 2009Review
- Extracellular acidification exerts opposite actions on TREK1 and TREK2 potassium channels via a single conserved histidine residue.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Regulation of ENaC-mediated sodium transport by glucocorticoids in Reissner's membrane epithelium.American journal of physiology. Cell physiology · 2009Article
- Acid-sensitive ion channels and receptors.Handbook of experimental pharmacology · 2009Review
- Nephrin binds to the COOH terminus of a large-conductance Ca2+-activated K+ channel isoform and regulates its expression on the cell surface.American journal of physiology. Renal physiology · 2008Article
Corrections and comments
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Authors and funding
4 authors at 3 institutions in 2 countries.
Funding
Abstract
TASK2 is a member of the two-pore domain K(+) channel family that plays a role in acid-base homeostasis; TASK2 knockout animals have plasma electrolyte patterns typical of the human clinical condition of renal tubular acidosis. It is expressed preferentially in epithelia, including the proximal tubules of the kidney. In common with the other TASK channels, TASK2 is sensitive to changes in extracellular pH, although the molecular mechanism of such pH sensing is not understood. We have examined the role of charged residues in the extracellular domains in pH sensing using a mutational approach. Mutant channels were expressed in CHO cells and studied by whole-cell and single-channel patch clamp. Neutralization of no single amino acid in isolation gave complete loss of pH sensitivity. However, the combined removal of five charged amino acids in the large extracellular loop linking the first transmembrane and pore domains, the M1-P1 loop, resulted in an essentially pH-insensitive channel, stabilized in the open state. Wild-type channels contain two such loops, but a concatemeric construct, comprised of one wild-type subunit and one containing the five mutations, was fully pH-sensitive, indicating that only one M1-P1 loop is required to yield a fully pH-sensitive channel, demonstrating a regulatory role of this distinctive structure in two-pore domain K(+) channels. Thus, pH sensing in TASK2 channels is conferred by the combined action of several charged residues in the large extracellular M1-P1 loop.
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