Ion currents through Kir potassium channels are gated by anionic lipids

• Published in: Nature communications Vol. 13; no. 1; p. 490
• Main Authors: Jin, Ruitao, He, Sitong, Black, Katrina A., Clarke, Oliver B., Wu, Di, Bolla, Jani R., Johnson, Paul, Periasamy, Agalya, Wardak, Ahmad, Czabotar, Peter, Colman, Peter M., Robinson, Carol V., Laver, Derek, Smith, Brian J., Gulbis, Jacqueline M.
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 25.01.2022; Nature Publishing Group; Nature Portfolio
• Subjects: 101/58; 631/45/269/1151; 631/535/1266; 631/535/1267; 82/83; 9/97; Anions - chemistry; Anions - metabolism; Binding Sites; Channels; Conduction; Crystallography, X-Ray; Grooves; Humanities and Social Sciences; Humans; Ion Channel Gating; Ion currents; Ion Transport; Lipids; Liposomes - chemistry; Liposomes - metabolism; Membrane Lipids - chemistry; Membrane Lipids - metabolism; Molecular Dynamics Simulation; multidisciplinary; Mutation; Penetration; Phosphatidylcholines - chemistry; Phosphatidylcholines - metabolism; Phosphatidylserines - chemistry; Phosphatidylserines - metabolism; Phospholipids; Plugs; Potassium; Potassium - metabolism; Potassium channels (inwardly-rectifying); Potassium Channels, Inwardly Rectifying - chemistry; Potassium Channels, Inwardly Rectifying - genetics; Potassium Channels, Inwardly Rectifying - metabolism; Regulatory sequences; Science; Science (multidisciplinary); Walls

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...