Site-directed mutagenesis identified a region near the amino terminus of the Shaker potassium channel that forms a cytoplasmic domain interacting with the open channel to cause inactivation.
Shaker potassium channel inactivation
Site-directed mutagenesis
Molecular transitions underlying inactivation
The potassium channels encoded by the Drosophila Shaker 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 Shaker potassium channels expressed in Xenopus 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.
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Hoshi et al. (Fri,) conducted a other in Shaker potassium channel inactivation. Site-directed mutagenesis was evaluated on Molecular transitions underlying inactivation. Site-directed mutagenesis identified a region near the amino terminus of the Shaker potassium channel that forms a cytoplasmic domain interacting with the open channel to cause inactivation.
synapsesocial.com/papers/6a0b1e91e1320844825d1f1e — DOI: https://doi.org/10.1126/science.2122519
Toshinori Hoshi
Leibniz University Hannover
William N. Zagotta
Electrophysiology
Richard W. Aldrich
Electrophysiology
Science
Stanford University
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