ArticleScientific reports2016
Functional mutagenesis screens reveal the 'cap structure' formation in disulfide-bridge free TASK channels.
Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 20 citations in OpenAlex.
- Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026Review
- Decoding the mechanism of proanthocyanidins in central analgesia: redox regulation and KCNK3 blockade.Experimental & molecular medicine · 2025Article
- Structures of TASK-1 and TASK-3 K2P channels provide insight into their gating and dysfunction in disease.Structure (London, England : 1993) · 2025Article
- Potassium channel TASK-5 forms functional heterodimers with TASK-1 and TASK-3 to break its silence.Nature communications · 2024Article
- Advances in the Understanding of Two-Pore Domain TASK Potassium Channels and Their Potential as Therapeutic Targets.Molecules (Basel, Switzerland) · 2022Review
- A Deafness Associated Protein TMEM43 Interacts with KCNK3 (TASK-1) Two-pore Domain KExperimental neurobiology · 2021Article
- Structural Insights into the Mechanisms and Pharmacology of KJournal of molecular biology · 2021Review
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- N-glycosylation-dependent regulation of hKMolecular biology of the cell · 2019Article
- Heterodimerization of two pore domain K+ channel TASK1 and TALK2 in living heterologous expression systems.PloS one · 2017Article
- Understanding the Cap Structure in K2P Channels.Frontiers in physiology · 2016Article
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Authors and funding
9 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Two-pore-domain potassium (K2P) channels have a large extracellular cap structure formed by two M1-P1 linkers, containing a cysteine for dimerization. However, this cysteine is not present in the TASK-1/3/5 subfamily. The functional role of the cap is poorly understood and it remained unclear whether K2P channels assemble in the domain-swapped orientation or not. Functional alanine-mutagenesis screens of TASK-1 and TRAAK were used to build an in silico model of the TASK-1 cap. According to our data the cap structure of disulfide-bridge free TASK channels is similar to that of other K2P channels and is most likely assembled in the domain-swapped orientation. As the conserved cysteine is not essential for functional expression of all K2P channels tested, we propose that hydrophobic residues at the inner leaflets of the cap domains can interact with each other and that this way of stabilizing the cap is most likely conserved among K2P channels.
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