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Updated: Jun 18, 2026

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Structural evidence that a lipid plug controls K2P6.1(TWIK-2) function.

Abhisek Mondal1, Sangeeta Niranjan1, Daniel L Minor2,3,4,5,6,7

  • 1Cardiovascular Research Institute, University of California, San Francisco, CA, USA.

Nature Communications
|June 16, 2026
PubMed
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This summary is machine-generated.

Lipids regulate K2P6.1 (TWIK2) potassium channels by forming a

Area of Science:

  • Structural Biology
  • Biophysics
  • Molecular Biology

Background:

  • Lipids are crucial for ion channel function, but their regulatory mechanisms remain unclear.
  • The K2P family of potassium channels has shown lipid densities, suggesting bilayer access regulates function.
  • Investigating lipid-protein interactions is key to understanding ion channel regulation.

Purpose of the Study:

  • To elucidate the structural basis of lipid regulation in the K2P6.1 (TWIK2) channel.
  • To characterize the 'lipid plug' conformation and its interaction sites.
  • To determine the role of specific residues, like Arg257, in lipid binding and channel function.

Main Methods:

  • Cryo-electron microscopy (cryo-EM) of K2P6.1 (TWIK2) in nanodisc and detergent.

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  • Analysis of K2P6.1 (TWIK2) mutants affecting membrane localization and function.
  • Molecular dynamics (MD) simulations to assess lipid plug stability and binding interactions.

    • Main Results:

    • Cryo-EM revealed a novel lipid plug within the K2P6.1 (TWIK2) channel cavity.
    • The lipid plug features two lipid tails binding to distinct sites, including a fenestration.
    • Mutant R257A revealed Arg257's critical role in lipid binding and plug coordination, influencing channel gating.
    • MD simulations confirmed lipid plug stability and the importance of Arg257.

    Conclusions:

    • A lipid plug mechanism inactivates TWIK channels by occupying the central cavity.
    • Lipid plug removal is necessary for ion permeation, regulating K2P channel leak function.
    • This provides a novel regulatory mechanism for K2P channels based on lipid interactions and cellular context.