ArticleThe Journal of physiology2011
Probing the regulation of TASK potassium channels by PI4,5P₂ with switchable phosphoinositide phosphatases.
Article in The Journal of physiology, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed, 45 citations in OpenAlex.
- Aberrant PCM1 accumulation in Trisomy 21 mislocalizes E3 ligases, delaying primary ciliogenesis.bioRxiv : the preprint server for biology · 2026Article
- A versatile functional interaction between electrically silent KCellular and molecular life sciences : CMLS · 2024Article
- Two-Pore Domain Potassium Channel in Neurological Disorders.The Journal of membrane biology · 2021Review
- TASK channels: channelopathies, trafficking, and receptor-mediated inhibition.Pflugers Archiv : European journal of physiology · 2020Review
- Depletion of plasma membrane-associated phosphoinositides mimics inhibition of TRPM7 channels by cytosolic MgThe Journal of biological chemistry · 2018Article
- KChannels (Austin, Tex.) · 2018Article
- Endocytosis: another pathway in receptor-Gq-TASK signalling.The Journal of physiology · 2017Article
- Phosphatidylinositol (4,5)-bisphosphate dynamically regulates the KScientific reports · 2017Article
- Dynamic NHERF interaction with TRPC4/5 proteins is required for channel gating by diacylglycerol.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Direct modulation of TRPM4 and TRPM3 channels by the phospholipase C inhibitor U73122.British journal of pharmacology · 2016Article
- A Polybasic Plasma Membrane Binding Motif in the I-II Linker Stabilizes Voltage-gated CaV1.2 Calcium Channel Function.The Journal of biological chemistry · 2015Article
- The role of acid-sensitive two-pore domain potassium channels in cardiac electrophysiology: focus on arrhythmias.Pflugers Archiv : European journal of physiology · 2015Review
- Two-pore domain potassium channels in the adrenal cortex.Pflugers Archiv : European journal of physiology · 2015Review
- The role of two-pore-domain background K⁺ (K₂p) channels in the thalamus.Pflugers Archiv : European journal of physiology · 2015Review
- TASK channels in arterial chemoreceptors and their role in oxygen and acid sensing.Pflugers Archiv : European journal of physiology · 2015Review
- Differential phospholipase C-dependent modulation of TASK and TREK two-pore domain K+ channels in rat thalamocortical relay neurons.The Journal of physiology · 2015Article
- A method to control phosphoinositides and to analyze PTEN function in living cells using voltage sensitive phosphatases.Frontiers in pharmacology · 2015Article
- Ion channel regulation by phosphoinositides analyzed with VSPs-PI(4,5)P2 affinity, phosphoinositide selectivity, and PI(4,5)P2 pool accessibility.Frontiers in pharmacology · 2015Article
- Phosphatidylinositol 4,5-bisphosphate depletion fails to affect neurosteroid modulation of GABAA receptor function.Psychopharmacology · 2014Article
- Golgi and plasma membrane pools of PI(4)P contribute to plasma membrane PI(4,5)P2 and maintenance of KCNQ2/3 ion channel current.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TASK channels are background K+ channels that contribute to the resting conductance in many neurons. A key feature of TASK channels is the reversible inhibition by Gq-coupled receptors, thereby mediating the dynamic regulation of neuronal activity by modulatory transmitters. The mechanism that mediates channel inhibition is not fully understood. While it is clear that activation of Gαq is required, the immediate signal for channel closure remains controversial. Experimental evidence pointed to either phospholipase C (PLC)-mediated depletion of phosphatidylinositol-4,5-bisphosphate (PI(4,5)P2) as the cause for channel closure or to a direct inhibitory interaction of active Gαq with the channel. Here, we address the role of PI(4,5)P2 for G-protein-coupled receptor (GPCR)-mediated TASK inhibition by using recently developed genetically encoded tools to alter phosphoinositide (PI) concentrations in the living cell.When expressed in CHO cells, TASK-1- and TASK-3-mediated currents were not affected by depletion of plasma membrane PI(4,5)P2 either via the voltage-activated phosphatase Ci-VSP or via chemically triggered recruitment of a PI(4,5)P2-5'-phosphatase. Depletion of both PI(4,5)P2 and PI(4)P via membrane recruitment of a novel engineered dual-specificity phosphatase also did not inhibit TASK currents. In contrast, each of these methods produced robust inhibition of the bona fide PI(4,5)P2-dependent channel KCNQ4. Efficient depletion of PI(4,5)P2 and PI(4)P was further confirmed with a fluorescent phosphoinositide sensor. Moreover, TASK channels recovered normally from inhibition by co-expressed muscarinic M1 receptors when resynthesis of PI(4,5)P2 was prevented by depletion of cellular ATP. These results demonstrate that TASK channel activity is independent of phosphoinositide concentrations within the physiological range. Consequently, Gq-mediated inhibition of TASK channels is not mediated by depletion of PI(4,5)P2.
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