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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
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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- Functional Consequences of a Decreased Potassium Affinity in a Potassium Channel Pore: Ion Interactions and C-Type Inactivation.
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J. Gen. Physiol.
113, 347-358
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- Structure and Function of the CFTR Chloride Channel.
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Physiol Rev
79, 23-45
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- Coexpression of the KCNA3B Gene Product with Kv1.5 Leads to a Novel A-type Potassium Channel.
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J. Biol. Chem.
273, 35095-35101
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- Two mutations linked to nocturnal frontal lobe epilepsy cause use-dependent potentiation of the nicotinic ACh response.
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J. Physiol.
513, 655-670
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- Voltage-dependent Gating of Single Wild-Type and S4 Mutant KAT1 Inward Rectifier Potassium Channels.
- P. C. Zei and R. W. Aldrich (1998)
J. Gen. Physiol.
112, 679-713
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- Regulation of Deactivation by an Amino Terminal Domain in Human Ether-a-go-go -related Gene Potassium Channels.
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J. Gen. Physiol.
112, 637-647
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- Subunit Folding and Assembly Steps Are Interspersed during Shaker Potassium Channel Biogenesis.
- C. T. Schulteis, N. Nagaya, and D. M. Papazian (1998)
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273, 26210-26217
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- Protein Rearrangements Underlying Slow Inactivation of the Shaker K+ Channel.
- E. Loots and E.Y. Isacoff (1998)
J. Gen. Physiol.
112, 377-389
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- Apoptotic proteins Reaper and Grim induce stable inactivation in voltage-gated K+ channels.
- V. Avdonin, J. Kasuya, M. A. Ciorba, B. Kaplan, T. Hoshi, and L. Iverson (1998)
PNAS
95, 11703-11708
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- Reduced K+ Channel Inactivation, Spike Broadening, and After-Hyperpolarization in Kvbeta 1.1-Deficient Mice with Impaired Learning.
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5, 257-273
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- The Diphtheria Toxin Channel-forming T Domain Translocates Its Own NH2-Terminal Region Across Planar Bilayers.
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J. Gen. Physiol.
112, 317-324
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