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Phospholipids and the origin of cationic gating charges in voltage sensors

Author

Listed:
  • Daniel Schmidt

    (Rockefeller University)

  • Qiu-Xing Jiang

    (Rockefeller University)

  • Roderick MacKinnon

    (Rockefeller University)

Abstract

Cells communicate with their external environment through physical and chemical processes that take place in the cell-surrounding membrane. The membrane serves as a barrier as well as a special environment in which membrane proteins are able to carry out important processes. Certain membrane proteins have the ability to detect the membrane voltage and regulate ion conduction or enzyme activity1,2. Such voltage-dependent processes rely on the action of protein domains known as voltage sensors, which are embedded inside the cell membrane and contain an excess of positively charged amino acids, which react to an electric field. How does the membrane create an environment suitable for voltage sensors? Here we show under a variety of conditions that the function of a voltage-dependent K+ channel is dependent on the negatively charged phosphodiester of phospholipid molecules. A non-voltage-dependent K+ channel does not exhibit the same dependence. The data lead us to propose that the phospholipid membrane, by providing stabilizing interactions between positively charged voltage-sensor arginine residues and negatively charged lipid phosphodiester groups, provides an appropriate environment for the energetic stability and operation of the voltage-sensing machinery. We suggest that the usage of arginine residues in voltage sensors is an adaptation to the phospholipid composition of cell membranes.

Suggested Citation

  • Daniel Schmidt & Qiu-Xing Jiang & Roderick MacKinnon, 2006. "Phospholipids and the origin of cationic gating charges in voltage sensors," Nature, Nature, vol. 444(7120), pages 775-779, December.
  • Handle: RePEc:nat:nature:v:444:y:2006:i:7120:d:10.1038_nature05416
    DOI: 10.1038/nature05416
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    Cited by:

    1. Georg Kuenze & Amanda M Duran & Hope Woods & Kathryn R Brewer & Eli Fritz McDonald & Carlos G Vanoye & Alfred L George Jr. & Charles R Sanders & Jens Meiler, 2019. "Upgraded molecular models of the human KCNQ1 potassium channel," PLOS ONE, Public Library of Science, vol. 14(9), pages 1-33, September.
    2. Spencer C. Guo & Rong Shen & BenoƮt Roux & Aaron R. Dinner, 2024. "Dynamics of activation in the voltage-sensing domain of Ciona intestinalis phosphatase Ci-VSP," Nature Communications, Nature, vol. 15(1), pages 1-13, December.

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