Biophysical and Molecular Mechanisms of <i>Shaker</i> Potassium Channel Inactivation

  • Toshinori Hoshi
    Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305.
  • William N. Zagotta
    Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305.
  • Richard W. Aldrich
    Department of Molecular and Cellular Physiology, Stanford University School of Medicine, Stanford, CA 94305.

書誌事項

公開日
1990-10-26
DOI
  • 10.1126/science.2122519
公開者
American Association for the Advancement of Science (AAAS)

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説明

<jats:p> The potassium channels encoded by the <jats:italic>Drosophila</jats:italic> <jats:italic>Shaker</jats:italic> gene activate and inactivate rapidly when the membrane potential becomes more positive. Site-directed mutagenesis and single-channel patch-clamp recording were used to explore the molecular transitions that underlie inactivation in <jats:italic>Shaker</jats:italic> potassium channels expressed in <jats:italic>Xenopus</jats:italic> oocytes. A region near the amino terminus with an important role in inactivation has now been identified. The results suggest a model where this region forms a cytoplasmic domain that interacts with the open channel to cause inactivation. </jats:p>

収録刊行物

  • Science

    Science 250 (4980), 533-538, 1990-10-26

    American Association for the Advancement of Science (AAAS)

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