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Three distinct and sequential steps in the release of sodium ions by the Na+/K+-ATPase

Author

Listed:
  • Miguel Holmgren

    (The Marine Biological Laboratory
    Harvard Medical School)

  • Jonathan Wagg

    (The Marine Biological Laboratory
    rSafe Inc)

  • Francisco Bezanilla

    (The Marine Biological Laboratory
    UCLA School of Medicine)

  • Robert F. Rakowski

    (The Marine Biological Laboratory
    FUHS/Chicago Medical School)

  • Paul De Weer

    (The Marine Biological Laboratory
    University of Pennsylvania School of Medicine)

  • David C. Gadsby

    (The Marine Biological Laboratory
    The Rockefeller University)

Abstract

The Na+/K+ pump, a P-type ion-motive ATPase, exports three sodium ions and then imports two potassium ions in each transport cycle. Ions on one side of the membrane bind to sites within the protein and become temporarily occluded (trapped within the protein) before being released to the other side1,2, but details of these occlusion and de-occlusion transitions remain obscure for all P-type ATPases. If it is deprived of potassium ions, the Na+/K+ pump is restricted to sodium translocation steps3, at least one involving charge movement through the membrane's electric field4,5. Changes in membrane potential alter the rate of such electrogenic reactions and so shift the distribution of enzyme conformations. Here we use high-speed voltage jumps to initiate this redistribution and show that the resulting pre-steady-state charge movements relax in three identifiable phases, apparently reflecting de-occlusion and release of the three sodium ions. Reciprocal relationships among the sizes of these three charge components show that the three sodium ions are de-occluded and released to the extracellular solution one at a time, in a strict order.

Suggested Citation

  • Miguel Holmgren & Jonathan Wagg & Francisco Bezanilla & Robert F. Rakowski & Paul De Weer & David C. Gadsby, 2000. "Three distinct and sequential steps in the release of sodium ions by the Na+/K+-ATPase," Nature, Nature, vol. 403(6772), pages 898-901, February.
    • Handle: RePEc:nat:nature:v:403:y:2000:i:6772:d:10.1038_35002599
    DOI: 10.1038/35002599
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    Cited by:

    1. Peng Zhao & Chaoran Zhao & Dandan Chen & Caihong Yun & Huilin Li & Lin Bai, 2021. "Structure and activation mechanism of the hexameric plasma membrane H+-ATPase," Nature Communications, Nature, vol. 12(1), pages 1-11, December.

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