ReviewEuropean biophysics journal : EBJ2009
Gating the pore of potassium leak channels.
Review in European biophysics journal : EBJ, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
27 citing papers in PubMed.
- Structure-Function Relationships of KAdvances in experimental medicine and biology · 2026Review
- Thalamocortical feedback selectively controls pyramidal neuron excitability.Nature communications · 2025Article
- Ion occupancy of the selectivity filter controls opening of a cytoplasmic gate in the KNature communications · 2024Article
- Cloxyquin activates hTRESK by allosteric modulation of the selectivity filter.Communications biology · 2023Article
- Contribution of membrane-associated oscillators to biological timing at different timescales.Frontiers in physiology · 2023Article
- Elucidating the Structural Basis of the Intracellular pH Sensing Mechanism of TASK-2 KInternational journal of molecular sciences · 2020Article
- Genetic variants of rs1275988 and rs2586886 in TWIK-related acid-sensitive K+ channel-1 gene may be potential risk factors for obese patients with obstructive sleep apnea.Chinese medical journal · 2019Article
- The Insensitivity of TASK-3 K₂P Channels to External Tetraethylammonium (TEA) Partially Depends on the Cap Structure.International journal of molecular sciences · 2018Article
- Two-pore domain potassium channels: potential therapeutic targets for the treatment of pain.Pflugers Archiv : European journal of physiology · 2015Review
- Golgi anti-apoptotic proteins are highly conserved ion channels that affect apoptosis and cell migration.The Journal of biological chemistry · 2015Article
- K2P channel gating mechanisms revealed by structures of TREK-2 and a complex with Prozac.Science (New York, N.Y.) · 2015Article
- Human trypanolytic factor APOL1 forms pH-gated cation-selective channels in planar lipid bilayers: relevance to trypanosome lysis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- Hydrophobic gating in ion channels.Journal of molecular biology · 2015Review
- Influence of lipids on the hydrophobic barrier within the pore of the TWIK-1 K2P channel.Channels (Austin, Tex.) · 2015Article
- Molecular aspects of structure, gating, and physiology of pH-sensitive background K2P and Kir K+-transport channels.Physiological reviews · 2015Review
- Enhancement of TWIK-related acid-sensitive potassium channel 3 (TASK3) two-pore domain potassium channel activity by tumor necrosis factor α.The Journal of biological chemistry · 2014Article
- An extracellular ion pathway plays a central role in the cooperative gating of a K(2P) K+ channel by extracellular pH.The Journal of biological chemistry · 2013Article
- TASK-2: a K2P K(+) channel with complex regulation and diverse physiological functions.Frontiers in physiology · 2013Article
- Acid-sensitive TWIK and TASK two-pore domain potassium channels change ion selectivity and become permeable to sodium in extracellular acidification.The Journal of biological chemistry · 2012Article
- Crystal structure of the human K2P TRAAK, a lipid- and mechano-sensitive K+ ion channel.Science (New York, N.Y.) · 2012Article
Corrections and comments
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A key feature of potassium channel function is the ability to switch between conducting and non-conducting states by undergoing conformational changes in response to cellular or extracellular signals. Such switching is facilitated by the mechanical coupling of gating domain movements to pore opening and closing. Two-pore domain potassium channels (K(2P)) conduct leak or background potassium-selective currents that are mostly time- and voltage-independent. These channels play a significant role in setting the cell resting membrane potential and, therefore modulate cell responsiveness and excitability. Thus, K(2P) channels are key players in numerous physiological processes and were recently shown to also be involved in human pathologies. It is well established that K(2P) channel conductance, open probability and cell surface expression are significantly modulated by various physical and chemical stimuli. However, in understanding how such signals are translated into conformational changes that open or close the channels gate, there remain more open questions than answers. A growing line of evidence suggests that the outer pore area assumes a critical role in gating K(2P) channels, in a manner reminiscent of C-type inactivation of voltage-gated potassium channels. In some K(2P) channels, this gating mechanism is facilitated in response to external pH levels. Recently, it was suggested that K(2P) channels also possess a lower activation gate that is positively coupled to the outer pore gate. The purpose of this review is to present an up-to-date summary of research describing the conformational changes and gating events that take place at the K(2P) channel ion-conducting pathway during the channel regulation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.