ArticleJournal of cell science2016
A dual phosphorylation switch controls 14-3-3-dependent cell surface expression of TASK-1.
Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 45 citations in OpenAlex.
- 14-3-3 proteins: Regulators of cardiac excitation-contraction coupling and stress responses.The Journal of physiology · 2026Review
- Potassium channels in vascular smooth muscle cells.Physiological reviews · 2026Review
- 14-3-3 promotes sarcolemmal expression of cardiac CaProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Competitive protein recruitment in artificial cells.Communications chemistry · 2024Article
- Fragment-based exploration of the 14-3-3/Amot-p130 interface.Current research in structural biology · 2022Article
- Article
- Hierarchized phosphotarget binding by the seven human 14-3-3 isoforms.Nature communications · 2021Article
- Binding of the Human 14-3-3 Isoforms to Distinct Sites in the Leucine-Rich Repeat Kinase 2.Frontiers in neuroscience · 2020Article
- Emerging modes-of-action in drug discovery.MedChemComm · 2019Review
- Activation of the CaMolecular biology of the cell · 2019Article
- 14-3-3 signal adaptor and scaffold proteins mediate GPCR trafficking.Scientific reports · 2019Article
- Directing Traffic: Regulation of COPI Transport by Post-translational Modifications.Frontiers in cell and developmental biology · 2019Review
- Temperature-induced changes in the wheat phosphoproteome reveal temperature-regulated interconversion of phosphoforms.Journal of experimental botany · 2018Article
- The kinase activity of the channel-kinase protein TRPM7 regulates stability and localization of the TRPM7 channel in polarized epithelial cells.The Journal of biological chemistry · 2018Article
- Analysis of 14-3-3 isoforms expressed in photoreceptors.Experimental eye research · 2018Article
- Direct interaction with 14-3-3γ promotes surface expression of Best1 channel in astrocyte.Molecular brain · 2017Article
- Acetylcholine-dependent upregulation of TASK-1 channels in thalamic interneurons by a smooth muscle-like signalling pathway.The Journal of physiology · 2017Article
- Kinase Inhibition Leads to Hormesis in a Dual Phosphorylation-Dephosphorylation Cycle.PLoS computational biology · 2016Article
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The transport of the K(+) channels TASK-1 and TASK-3 (also known as KCNK3 and KCNK9, respectively) to the cell surface is controlled by the binding of 14-3-3 proteins to a trafficking control region at the extreme C-terminus of the channels. The current model proposes that phosphorylation-dependent binding of 14-3-3 sterically masks a COPI-binding motif. However, the direct effects of phosphorylation on COPI binding and on the binding parameters of 14-3-3 isoforms are still unknown. We find that phosphorylation of the trafficking control region prevents COPI binding even in the absence of 14-3-3, and we present a quantitative analysis of the binding of all human 14-3-3 isoforms to the trafficking control regions of TASK-1 and TASK-3. Surprisingly, the affinities of 14-3-3 proteins for TASK-1 are two orders of magnitude lower than for TASK-3. Furthermore, we find that phosphorylation of a second serine residue in the C-terminus of TASK-1 inhibits 14-3-3 binding. Thus, phosphorylation of the trafficking control region can stimulate or inhibit transport of TASK-1 to the cell surface depending on the target serine residue. Our findings indicate that control of TASK-1 trafficking by COPI, kinases, phosphatases and 14-3-3 proteins is highly dynamic.
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