ArticleThe Journal of biological chemistry2011
Protein kinase A is central for forward transport of two-pore domain potassium channels K2P3.1 and K2P9.1.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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Who cites it
17 citing papers in PubMed, 27 citations in OpenAlex.
- Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026Review
- Biochemical Analysis of AKAP-Anchored PKA Signaling Complexes.Methods in molecular biology (Clifton, N.J.) · 2022Article
- TASK channels: channelopathies, trafficking, and receptor-mediated inhibition.Pflugers Archiv : European journal of physiology · 2020Review
- A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1.Journal of cell science · 2016Article
- The role of protein-protein interactions in the intracellular traffic of the potassium channels TASK-1 and TASK-3.Pflugers Archiv : European journal of physiology · 2015Review
- Much more than a leak: structure and function of K₂p-channels.Pflugers Archiv : European journal of physiology · 2015Review
- 14-3-3τ promotes surface expression of Cav2.2 (α1B) Ca2+ channels.The Journal of biological chemistry · 2015Article
- Tuning the electrical properties of the heart by differential trafficking of KATP ion channel complexes.Journal of cell science · 2014Article
- Silencing of the tandem pore domain halothane-inhibited K+ channel 2 (THIK2) relies on combined intracellular retention and low intrinsic activity at the plasma membrane.The Journal of biological chemistry · 2013Article
- N-glycosylation-dependent control of functional expression of background potassium channels K2P3.1 and K2P9.1.The Journal of biological chemistry · 2013Article
- Article
- The acid-sensitive, anesthetic-activated potassium leak channel, KCNK3, is regulated by 14-3-3β-dependent, protein kinase C (PKC)-mediated endocytic trafficking.The Journal of biological chemistry · 2012Article
- PKC-dependent activation of human K(2P) 18.1 K(+) channels.British journal of pharmacology · 2012Article
- Using bacteria to determine protein kinase specificity and predict target substrates.PloS one · 2012Article
- The anti-atherosclerotic di-peptide, Trp-His, inhibits the phosphorylation of voltage-dependent L-type Ca(2+) channels in rat vascular smooth muscle cells.FEBS open bio · 2012Article
- Molecular and electrophysiological characterization of a novel cation channel of Trypanosoma cruzi.PLoS pathogens · 2012Article
- Acid sensitive background potassium channels K2P3.1 and K2P9.1 undergo rapid dynamin-dependent endocytosis.Channels (Austin, Tex.)Article
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Authors and funding
4 authors at 3 institutions in 1 country.
Funding
Abstract
Acid-sensitive two-pore domain potassium channels (K2P3.1 and K2P9.1) play key roles in both physiological and pathophysiological mechanisms, the most fundamental of which is control of resting membrane potential of cells in which they are expressed. These background "leak" channels are constitutively active once expressed at the plasma membrane, and hence tight control of their targeting and surface expression is fundamental to the regulation of K(+) flux and cell excitability. The chaperone protein, 14-3-3, binds to a critical phosphorylated serine in the channel C termini of K2P3.1 and K2P9.1 (Ser(393) and Ser(373), respectively) and overcomes retention in the endoplasmic reticulum by βCOP. We sought to identify the kinase responsible for phosphorylation of the terminal serine in human and rat variants of K2P3.1 and K2P9.1. Adopting a bioinformatic approach, three candidate protein kinases were identified: cAMP-dependent protein kinase, ribosomal S6 kinase, and protein kinase C. In vitro phosphorylation assays were utilized to determine the ability of the candidate kinases to phosphorylate the channel C termini. Electrophysiological measurements of human K2P3.1 transiently expressed in HEK293 cells and cell surface assays of GFP-tagged K2P3.1 and K2P9.1 enabled the determination of the functional implications of phosphorylation by specific kinases. All of our findings support the conclusion that cAMP-dependent protein kinase is responsible for the phosphorylation of the terminal serine in both K2P3.1 and K2P9.1.
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Registered trials
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