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Related Experiment Video

Updated: Apr 23, 2026

Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies
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Reconstitution of a Transmembrane Protein, the Voltage-gated Ion Channel, KvAP, into Giant Unilamellar Vesicles for Microscopy and Patch Clamp Studies

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Phosphatidic acid modulation of Kv channel voltage sensor function.

Richard K Hite1, Joel A Butterwick1, Roderick MacKinnon1

  • 1Laboratory of Molecular Neurobiology and Biophysics, Howard Hughes Medical Institute, Rockefeller University, New York, United States.

Elife
|October 7, 2014
PubMed
Summary
This summary is machine-generated.

Phosphatidic acid regulates Kv channel gating through electrostatic and specific interactions. Intracellular phosphatidic acid stabilizes the voltage sensor

Keywords:
biophysicselectrophysiologyion channelsratstructural biologyvoltage-gated potassium channels

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biophysics

Background:

  • Membrane phospholipids are crucial regulators of ion channel function.
  • Phosphatidic acid (PA) is a signaling lipid with known cellular roles.

Purpose of the Study:

  • To investigate the specific effects of phosphatidic acid on Kv channel gating.
  • To elucidate the molecular mechanisms underlying PA's regulation of Kv channels.

Main Methods:

  • Reconstitution of Kv channels and phosphatidic acid into planar lipid bilayers.
  • Electrophysiological recordings to measure Kv channel activation.
  • Analysis of electrostatic and specific lipid-protein interactions.

Main Results:

  • Phosphatidic acid exhibits dual effects on Kv channel gating: non-specific electrostatic and specific interactions.
  • The specific effect involves the intracellular leaflet, a primary phosphate group, and an arginine residue in the voltage sensor.
  • Intracellular phosphatidic acid shifts the activation midpoint by ~50 mV, favoring the closed state.

Conclusions:

  • Phosphatidic acid acts as a novel regulator of Kv channel voltage-sensor function.
  • These findings reveal a new mechanism for lipid-mediated control of ion channel activity.