Determinants of the Anesthetic Sensitivity of Two-pore Domain Acid-sensitive Potassium Channels
Open accessAbstract
Certain two-pore domain K(+) channels are plausible targets for volatile general anesthetics, yet little is known at the molecular level about how these simple agents cause channel activation. The first anesthetic-activated K(+) current I(K(An)) that was characterized was discovered in the mollusk Lymnaea stagnalis and is remarkable for both its sensitivity to general anesthetics and its stereoselective responses to anesthetic enantiomers (Franks, N. P., and Lieb, W. R. (1988) Nature 333, 662-664 and Franks, N. P., and Lieb, W. R. (1991) Science 254, 427-430). Here we report the molecular cloning of a two-pore domain K(+) channel LyTASK from L. stagnalis and show that, when expressed in HEK-293 cells, it displays the same biophysical characteristics as the anesthetic-activated K(+) current I(K(An)). Sequence analysis and functional properties show it to be a member of the TASK family of channels with approximately 47% identity at the amino acid level when compared with human TASK-1 and TASK-3. By using chimeric channel constructs and site-directed mutagenesis we have identified the specific amino acid 159 to be a critical determinant of anesthetic sensitivity, which, when mutated to alanine, essentially eliminates anesthetic activation in the human channels and greatly reduces activation in LyTASK. The L159A mutation in LyTASK disrupts the stereoselective response to isoflurane while having no effect on the pH sensitivity of the channel, suggesting this critical amino acid may form part of an anesthetic binding site.
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The K2P family includes mammalian homologues activated by anesthetics and others inhibited by anesthetics.
“Subsequent work led to the discovery of the tandem pore potassium channel (K2P) family, which contains mammalian homologues that are activated by anesthetics [48]) as well as those that are inhibited by anesthetics [49, 50].”
From The Biology of General Anesthesia from Paramecium to Primate (2019) · cites this paper as [48]
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- Authors
- Andres-Enguix, I., Caley, A., Yustos, R., Schumacher, M. A., Spanu, P. D., Dickinson, R., Maze, M., & Franks, N. P.
- Affiliations
- Imperial College London (GB)
- Chelsea and Westminster Hospital (GB)
- Corresponding author
- Franks, Nicholas P.
- ORCID
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 2007-07
- Volume
- 282
- Issue
- 29
- Pages
- 20977-20990
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2077052499
- Cited by
- 52
- References
- 40
- Citations by year
- 2026: 1 · 2025: 4 · 2024: 2 · 2023: 1 · 2022: 1 · 2021: 3 · 2020: 2 · 2019: 4 · 2018: 4 · 2017: 3 · 2015: 2 · 2014: 4 · 2013: 1 · 2012: 1
- FWCI
- 2.12
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Journal of Biological Chemistry (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Westminster Medical School Research Trust
- Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
- Health Sciences › Medicine › Anesthesiology and Pain Medicine › Anesthesia and Sedative Agents
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nicotinic Acetylcholine Receptors Study
- Keywords
- two-pore domain potassium channels, TASK channels, Lymnaea stagnalis, anesthetic sensitivity, volatile anesthetics, isoflurane, stereoselectivity, anesthetic binding sites, channel activation, pH sensitivity, chimeric channels, site-directed mutagenesis
- MeSH terms
- Amino Acid Sequence, Anesthetics, Animals, Base Sequence, Biophysics, Cell Line, Humans, Lymnaea, Molecular Sequence Data, Nerve Tissue Proteins, Recombinant Fusion Proteins, Stereoisomerism, Potassium Channels, Sequence Homology, Amino Acid, Potassium Channels, Tandem Pore Domain, Biophysical Phenomena
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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