ArticleThe Journal of biological chemistry2011
External Ba2+ block of the two-pore domain potassium channel TREK-1 defines conformational transition in its selectivity filter.
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 34 papers.
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Who cites it
34 citing papers in PubMed.
- Role for TREK-1 as a polymodal sensor and regulator of cell activity.Channels (Austin, Tex.) · 2026Review
- Temperature and pH-dependent potassium currents of muscles of the stomatogastric nervous system of the crab,iScience · 2026Article
- G Proteins-Associated Dose-Dependent Effects of Oxytocin on Oxytocin Neuronal Activity and Astrocytic Plasticity of the Supraoptic Nucleus.Molecular neurobiology · 2025Article
- Article
- The two-pore KAmerican journal of physiology. Heart and circulatory physiology · 2025Article
- Effect of two activators on the gating of a KBiophysical journal · 2024Article
- FOXP1 negatively regulates intrinsic excitability in D2 striatal projection neurons by promoting inwardly rectifying and leak potassium currents.Molecular psychiatry · 2021Article
- Next-generation inward rectifier potassium channel modulators: discovery and molecular pharmacology.American journal of physiology. Cell physiology · 2021Review
- TOK channels use the two gates in classical KFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2020Article
- Ion currents, action potentials, and noradrenergic responses in rat pulmonary vein and left atrial cardiomyocytes.Physiological reports · 2020Article
- Spadin Selectively Antagonizes Arachidonic Acid Activation of TREK-1 Channels.Frontiers in pharmacology · 2020Article
- Mutation of a single residue promotes gating of vertebrate and invertebrate two-pore domain potassium channels.Nature communications · 2019Article
- TREK-1 Channel Expression in Smooth Muscle as a Target for Regulating Murine Intestinal Contractility: Therapeutic Implications for Motility Disorders.Frontiers in physiology · 2018Article
- Modulation of Hyperpolarization-Activated Inward Current and Thalamic Activity Modes by Different Cyclic Nucleotides.Frontiers in cellular neuroscience · 2018Article
- TRESK background potassium channel is not gated at the helix bundle crossing near the cytoplasmic end of the pore.PloS one · 2018Article
- Article
- Potassium channel dysfunction underlies Purkinje neuron spiking abnormalities in spinocerebellar ataxia type 2.Human molecular genetics · 2017Article
- Contribution of two-pore KAmerican journal of physiology. Heart and circulatory physiology · 2017Article
- Unambiguous observation of blocked states reveals altered, blocker-induced, cardiac ryanodine receptor gating.Scientific reports · 2016Article
- Myometrial relaxation of mice via expression of two pore domain acid sensitive K(+) (TASK-2) channels.The Korean journal of physiology & pharmacology : official journal of the Korean Physiological Society and the Korean Society of Pharmacology · 2016Article
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10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
TREK-1 is a member of the two-pore domain potassium channel family that is known as a leak channel and plays a key role in many physiological and pathological processes. The conformational transition of the selectivity filter is considered as an effective strategy for potassium channels to control the course of potassium efflux. It is well known that TREK-1 is regulated by a large volume of extracellular and intracellular signals. However, until now, little was known about the selectivity filter gating mechanism of the channel. In this research, it was found that Ba(2+) blocked the TREK-1 channel in a concentration- and time-dependent manner. A mutagenesis analysis showed that overlapped binding of Ba(2+) at the assumed K(+) binding site 4 (S4) within the selectivity filter was responsible for the inhibitory effects on TREK-1. Then, Ba(2+) was used as a probe to explore the conformational transition in the selectivity filter of the channel. It was confirmed that collapsed conformations were induced by extracellular K(+)-free and acidification at the selectivity filters, leading to nonconductive to permeable ions. Further detailed characterization demonstrated that the two conformations presented different properties. Additionally, the N-terminal truncated isoform (ΔN41), a product derived from alternative translation initiation, was identified as a constitutively nonconductive variant. Together, these results illustrate the important role of selectivity filter gating in the regulation of TREK-1 by the extracellular K(+) and proton.
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