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Science 26 October 1990:
Vol. 250. no. 4980, pp. 568 - 571
DOI: 10.1126/science.2122520
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Articles

Science, Vol 250, Issue 4980, 568-571
Copyright © 1990 by American Association for the Advancement of Science

articles

Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB

WN Zagotta, T Hoshi, and RW Aldrich

Department of Molecular and Cellular Physiology, Stanford University School of Medicine, CA 94305.

Site-directed mutagenesis experiments have suggested a model for the inactivation mechanism of Shaker potassium channels from Drosophila melanogaster. In this model, the first 20 amino acids form a cytoplasmic domain that interacts with the open channel to cause inactivation. The model was tested by the internal application of a synthetic peptide, with the sequence of the first 20 residues of the ShB alternatively spliced variant, to noninactivating mutant channels expressed in Xenopus oocytes. The peptide restored inactivation in a concentration-dependent manner. Like normal inactivation, peptide-induced inactivation was not noticeably voltage-dependent. Trypsin-treated peptide and peptides with sequences derived from the first 20 residues of noninactivating mutants did not restore inactivation. These results support the proposal that inactivation occurs by a cytoplasmic domain that occludes the ion-conducting pore of the channel.


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Apoptotic proteins Reaper and Grim induce stable inactivation in voltage-gated K+ channels.
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