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.
Restoration of inactivation in mutants of Shaker potassium channels by a peptide derived from ShB
W. N. Zagotta,T. Hoshi,R. Aldrich
Published 1990 in Science
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- Publication year
1990
- Venue
Science
- Publication date
1990-10-26
- Fields of study
Biology, Medicine
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Semantic Scholar, PubMed
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