Ion currents through Kir potassium channels are gated by anionic lipids

Ruitao Jin, Sitong He, Katrina A. Black, Oliver B. Clarke, Di Wu, Jani R. Bolla, Paul Johnson, Agalya Periasamy, Ahmad Wardak, Peter Czabotar, Peter M. Colman, Carol V. Robinson, Derek Laver, Brian J. Smith () and Jacqueline M. Gulbis ()
Additional contact information
Ruitao Jin: La Trobe University
Sitong He: La Trobe University
Katrina A. Black: The Walter and Eliza Hall Institute of Medical Research
Oliver B. Clarke: Columbia University
Di Wu: University of Oxford
Jani R. Bolla: The Kavli Institute for Nanoscience Discovery
Paul Johnson: University of Newcastle and Hunter Medical Research Institute
Agalya Periasamy: The Walter and Eliza Hall Institute of Medical Research
Ahmad Wardak: The Walter and Eliza Hall Institute of Medical Research
Peter Czabotar: The Walter and Eliza Hall Institute of Medical Research
Peter M. Colman: The Walter and Eliza Hall Institute of Medical Research
Carol V. Robinson: University of Oxford
Derek Laver: University of Newcastle and Hunter Medical Research Institute
Brian J. Smith: La Trobe University
Jacqueline M. Gulbis: The Walter and Eliza Hall Institute of Medical Research

Nature Communications, 2022, vol. 13, issue 1, 1-11

Abstract: Abstract Ion currents through potassium channels are gated. Constriction of the ion conduction pathway at the inner helix bundle, the textbook gate of Kir potassium channels, has been shown to be an ineffective permeation control, creating a rift in our understanding of how these channels are gated. Here we present evidence that anionic lipids act as interactive response elements sufficient to gate potassium conduction. We demonstrate the limiting barrier to K+ permeation lies within the ion conduction pathway and show that this gate is operated by the fatty acyl tails of lipids that infiltrate the conduction pathway via fenestrations in the walls of the pore. Acyl tails occupying a surface groove extending from the cytosolic interface to the conduction pathway provide a potential means of relaying cellular signals, mediated by anionic lipid head groups bound at the canonical lipid binding site, to the internal gate.

Date: 2022
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Persistent link: https://EconPapers.repec.org/RePEc:nat:natcom:v:13:y:2022:i:1:d:10.1038_s41467-022-28148-4

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DOI: 10.1038/s41467-022-28148-4

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