ArticleThe Journal of biological chemistry2010
G protein {beta}{gamma} gating confers volatile anesthetic inhibition to Kir3 channels.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Satellite glial GPR37L1 and its ligand maresin 1 regulate potassium channel signaling and pain homeostasis.The Journal of clinical investigation · 2024Article
- A novel small-molecule selective activator of homomeric GIRK4 channels.The Journal of biological chemistry · 2022Article
- Isoflurane inhibits a Kir4.1/5.1-like conductance in neonatal rat brainstem astrocytes and recombinant Kir4.1/5.1 channels in a heterologous expression system.Journal of neurophysiology · 2020Article
- Chloroform is a potent activator of cardiac and neuronal Kir3 channels.Naunyn-Schmiedeberg's archives of pharmacology · 2020Article
- Alcohol modulation of G-protein-gated inwardly rectifying potassium channels: from binding to therapeutics.Frontiers in physiology · 2014Review
- Molecular mechanism underlying ethanol activation of G-protein-gated inwardly rectifying potassium channels.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- PKC independent inhibition of voltage gated calcium channels by volatile anesthetics in freshly isolated vascular myocytes from the aorta.Cell calcium · 2013Article
- Synergistic roles for G-protein γ3 and γ7 subtypes in seizure susceptibility as revealed in double knock-out mice.The Journal of biological chemistry · 2012Article
- Genetic defects in the hotspot of inwardly rectifying K(+) (Kir) channels and their metabolic consequences: a review.Molecular genetics and metabolism · 2012Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
G protein-activated inwardly rectifying potassium (GIRK or Kir3) channels are directly gated by the βγ subunits of G proteins and contribute to inhibitory neurotransmitter signaling pathways. Paradoxically, volatile anesthetics such as halothane inhibit these channels. We find that neuronal Kir3 currents are highly sensitive to inhibition by halothane. Given that Kir3 currents result from increased Gβγ available to the channels, we asked whether reducing available Gβγ to the channel would adversely affect halothane inhibition. Remarkably, scavenging Gβγ using the C-terminal domain of β-adrenergic receptor kinase (cβARK) resulted in channel activation by halothane. Consistent with this effect, channel mutants that impair Gβγ activation were also activated by halothane. A single residue, phenylalanine 192, occupies the putative Gβγ gate of neuronal Kir3.2 channels. Mutation of Phe-192 at the gate to other residues rendered the channel non-responsive, either activated or inhibited by halothane. These data indicated that halothane predominantly interferes with Gβγ-mediated Kir3 currents, such as those functioning during inhibitory synaptic activity. Our report identifies the molecular correlate for anesthetic inhibition of Kir3 channels and highlights the significance of these effects in modulating neurotransmitter-mediated inhibitory signaling.
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