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PMID: 2122519 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Biophysical and molecular mechanisms of Shaker potassium channel inactivation.

Science (New York, N.Y.) ·Vol. 250 ·No. 4980 ·1990-10-26 ·Pages 533-8

Hoshi T, Zagotta WN, Aldrich RW

Abstract

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.

Related Genes
MeSH Terms
Amino Acid Sequence Animals DNA/genetics Drosophila melanogaster/genetics Electric Conductivity Ion Channel Gating/drug effects,physiology Kinetics Membrane Potentials/physiology Molecular Sequence Data Mutagenesis Mutagenesis, Site-Directed Oocytes/metabolism Potassium Channels/genetics,physiology RNA Splicing Structure-Activity Relationship Trypsin/pharmacology Xenopus
Chemicals
Potassium Channels DNA Trypsin
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Hoshi T
Department of Molecular and Cellular Physiology, Stanford University, School of Medicine, CA 94305.
Zagotta W N
Aldrich R W
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1990-10-26
Pages
533-8
Language
English
Region
United States
NLM ID
0404511
Subset
IM
Grants
NINDS NIH HHS · NS07158 · United States
NINDS NIH HHS · NS23294 · United States
Corrections
CommentIn
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