ArticleThe Journal of biological chemistry2010
TRESK background K(+) channel is inhibited by phosphorylation via two distinct pathways.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 33 citations in OpenAlex.
- Calcium-dependent activation of TREK-1 and TREK-2 background potassium channels by calcineurin.Scientific reports · 2025Article
- The research progress into cellular mechanosensitive ion channels mediating cancer pain.Channels (Austin, Tex.) · 2025Review
- The Ubiquitin Ligase Adaptor NDFIP1 Interacts with TRESK and Negatively Regulates the Background KInternational journal of molecular sciences · 2024Article
- Cloxyquin activates hTRESK by allosteric modulation of the selectivity filter.Communications biology · 2023Article
- Article
- TRESK and TREK-2 two-pore-domain potassium channel subunits form functional heterodimers in primary somatosensory neurons.The Journal of biological chemistry · 2020Article
- The Background KInternational journal of molecular sciences · 2020Review
- Anionic Phospholipids Bind to and Modulate the Activity of Human TRESK Background KMolecular neurobiology · 2019Article
- Two-pore domain potassium channels: emerging targets for novel analgesic drugs: IUPHAR Review 26.British journal of pharmacology · 2019Review
- TRESK background potassium channel is not gated at the helix bundle crossing near the cytoplasmic end of the pore.PloS one · 2018Article
- Selective and state-dependent activation of TRESK (KBritish journal of pharmacology · 2017Article
- Locomotion Behavior Is Affected by the GαGenetics · 2017Article
- Aristolochic acid, a plant extract used in the treatment of pain and linked to Balkan endemic nephropathy, is a regulator of K2P channels.British journal of pharmacology · 2016Article
- Role of K₂p channels in stimulus-secretion coupling.Pflugers Archiv : European journal of physiology · 2015Review
- Properties, regulation, pharmacology, and functions of the K₂p channel, TRESK.Pflugers Archiv : European journal of physiology · 2015Review
- Forskolin suppresses delayed-rectifier K+ currents and enhances spike frequency-dependent adaptation of sympathetic neurons.PloS one · 2015Article
- The LQLP calcineurin docking site is a major determinant of the calcium-dependent activation of human TRESK background K+ channel.The Journal of biological chemistry · 2014Article
- Functional characterization of zebrafish K2P18.1 (TRESK) two-pore-domain K+ channels.Naunyn-Schmiedeberg's archives of pharmacology · 2014Article
- Article
- The complex actions of sumatriptan on rat dural afferents.Cephalalgia : an international journal of headache · 2012Article
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2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The two-pore domain K(+) channel, TRESK (TWIK-related spinal cord K(+) channel, KCNK18) is directly regulated by the calcium/calmodulin-dependent phosphatase calcineurin and 14-3-3 adaptor proteins. The calcium signal robustly activates the channel via calcineurin, whereas the anchoring of 14-3-3 interferes with the return of the current to the resting state after the activation in Xenopus oocytes. In the present study, we report that the phosphorylation of TRESK at two distinct regulatory regions, the 14-3-3 binding site (Ser-264) and the cluster of three adjacent serine residues (Ser-274, Ser-276, and Ser-279), are responsible for channel inhibition. The phosphorylation of Ser-264 by protein kinase A accelerated the return of the current of S276E mutant TRESK to the resting state after the calcineurin-dependent activation. In the presence of 14-3-3, the basal current of the S276E mutant was reduced, and its calcineurin-dependent activation was augmented, suggesting that the direct binding of the adaptor protein to TRESK contributed to the basal inhibition of the channel under resting conditions. Unexpectedly, we found that 14-3-3 impeded the recovery of the current of S264E mutant TRESK to the resting state after the calcineurin-dependent activation, despite of the mutated 14-3-3 binding site. This suggests that 14-3-3 inhibited the kinase phosphorylating the regulatory cluster of Ser-274, Ser-276, and Ser-279, independently of the direct interaction between TRESK and 14-3-3. In conclusion, two distinct inhibitory kinase pathways converge on TRESK, and their effect on the calcineurin-dependent regulation is differentially modulated by the functional availability of 14-3-3.
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