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Regulation of voltage dependence of the KAT1 channel by intracellular factors
The KAT1 channel is a hyperpolarization-activated K+ channel cloned from the higher plant Arabidopsis. The deduced amino acid sequence suggests that its structural organization is similar to that of the Shaker-like K+ channel activated by depolarization. Electrophysiological properties of the KAT1 c...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1995
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2216946/ https://www.ncbi.nlm.nih.gov/pubmed/7769379 |
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collection | PubMed |
description | The KAT1 channel is a hyperpolarization-activated K+ channel cloned from the higher plant Arabidopsis. The deduced amino acid sequence suggests that its structural organization is similar to that of the Shaker-like K+ channel activated by depolarization. Electrophysiological properties of the KAT1 channel expressed in Xenopus oocytes indicate that voltage-dependent activation of the KAT1 channel is not caused by the divalent ion block and that it is intrinsic to the channel. Activity of the KAT1 channel progressively decreases upon patch excision. This rundown of the channel is accompanied by a large shift in the voltage dependence of the channel to a more negative direction. The voltage dependence is also regulated by pH, ATP, and cGMP. |
format | Text |
id | pubmed-2216946 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1995 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-22169462008-04-23 Regulation of voltage dependence of the KAT1 channel by intracellular factors J Gen Physiol Articles The KAT1 channel is a hyperpolarization-activated K+ channel cloned from the higher plant Arabidopsis. The deduced amino acid sequence suggests that its structural organization is similar to that of the Shaker-like K+ channel activated by depolarization. Electrophysiological properties of the KAT1 channel expressed in Xenopus oocytes indicate that voltage-dependent activation of the KAT1 channel is not caused by the divalent ion block and that it is intrinsic to the channel. Activity of the KAT1 channel progressively decreases upon patch excision. This rundown of the channel is accompanied by a large shift in the voltage dependence of the channel to a more negative direction. The voltage dependence is also regulated by pH, ATP, and cGMP. The Rockefeller University Press 1995-03-01 /pmc/articles/PMC2216946/ /pubmed/7769379 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles Regulation of voltage dependence of the KAT1 channel by intracellular factors |
title | Regulation of voltage dependence of the KAT1 channel by intracellular factors |
title_full | Regulation of voltage dependence of the KAT1 channel by intracellular factors |
title_fullStr | Regulation of voltage dependence of the KAT1 channel by intracellular factors |
title_full_unstemmed | Regulation of voltage dependence of the KAT1 channel by intracellular factors |
title_short | Regulation of voltage dependence of the KAT1 channel by intracellular factors |
title_sort | regulation of voltage dependence of the kat1 channel by intracellular factors |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2216946/ https://www.ncbi.nlm.nih.gov/pubmed/7769379 |