PUBLICATION

Mechanistic insights into volatile anesthetic modulation of K2P channels

Authors
Wague, A., Joseph, T.T., Woll, K.A., Bu, W., Vaidya, K.A., Bhanu, N.V., Garcia, B.A., Nimigean, C.M., Eckenhoff, R.G., Riegelhaupt, P.M.
ID
ZDB-PUB-201222-6
Date
2020
Source
eLIFE   9: (Journal)
Registered Authors
Keywords
biochemistry, chemical biology, molecular biophysics, mouse, structural biology, xenopus, zebrafish
MeSH Terms
  • Binding Sites
  • Molecular Docking Simulation
  • Animals
  • Potassium Channels, Tandem Pore Domain/drug effects*
  • Potassium Channels, Tandem Pore Domain/metabolism
  • Isoflurane/pharmacology
  • Potassium Channels/drug effects
  • Potassium Channels/metabolism
  • Anesthetics, Inhalation/metabolism
  • Anesthetics, Inhalation/pharmacology*
  • Humans
  • Zebrafish
  • Xenopus laevis
  • Mice
PubMed
33345771 Full text @ Elife
Abstract
K2P potassium channels are known to be modulated by volatile anesthetic (VA) drugs and play important roles in clinically relevant effects that accompany general anesthesia. Here, we utilize a photoaffinity analog of the VA isoflurane to identify a VA binding site in the TREK1 K2P channel. The functional importance of the identified site was validated by mutagenesis and biochemical modification. Molecular dynamics simulations of TREK1 in the presence of VA found multiple neighboring residues on TREK1 TM2, TM3 and TM4 that contribute to anesthetic binding. The identified VA binding region contains residues that play roles in the mechanisms by which heat, mechanical stretch, and pharmacological modulators alter TREK1 channel activity and overlaps with positions found to modulate TASK K2P channel VA sensitivity. Our findings define molecular contacts that mediate VA binding to TREK1 channels and suggest a mechanistic basis to explain how K2P channels are modulated by VAs.
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