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JXB Advance Access originally published online on November 1, 2005
Journal of Experimental Botany 2005 56(422):3103-3110; doi:10.1093/jxb/eri307
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© The Author [2005]. Published by Oxford University Press [on behalf of the Society for Experimental Biology]. All rights reserved. The online version of this article has been published under an Open Access model. Users are entitled to use, reproduce, disseminate, or display the Open Access version of this article for non-commercial purposes provided that: the original authorship is properly and fully attributed; the Journal and the Society for Experimental Biology are attributed as the original place of publication with the correct citation details given; if an article is subsequently reproduced or disseminated not in its entirety but only in part or as a derivative work this must be clearly indicated. For commercial re-use, please contact: journals.permissions@oxfordjournals.org

RESEARCH PAPER

KAT1 inactivates at sub-millimolar concentrations of external potassium

Brigitte Hertel1 *, Ferenc Horváth2 *, Barnabás Wodala2, Annette Hurst1, Anna Moroni3 and Gerhard Thiel1,{dagger}

1Institute of Botany, Department of Biology, Darmstadt University of Technology, Schnittspahnstraße 3, D-64287 Darmstadt, Germany
2Department Plant Physiology, University of Szeged, Szeged, Hungary
3Dipartimento di Biologia and IBF-CNR, Università degli Studi di Milano, Italy

{dagger} To whom correspondence should be addressed. E-mail: thiel{at}bio.tu-darmstadt.de

Structural analysis of K+ channel pores suggests that the selectivity filter of the pore is an inherent sensor for extracellular K+ channels seem to be inactivated at low because of a destabilization of the conducting state and a collapse of the pore. In the present study, the effect of depleting on the activity of a plant K+ channel, KAT1, from Arabidopsis thaliana was investigated. This channel is thought to be insensitive to The channel was therefore expressed in mammalian HEK293 cells and measured with patch clamp technology in the whole cell configuration. The effect of depletion on channel activity was monitored from the tail currents before, during, and after washing from the medium. The data show that a depletion of results in a decrease in channel conductance, irrespective of whether K+ is simply removed or replaced by either Na+ or Li+. Quantitative analysis suggests that the channel has two binding sites for K+ with the dissociation constant in the order of 20 µM. This high sensitivity of the channel to could serve as a safety mechanism, which inactivates the channel at low and, in this way, prevents leakage of K+ from the cells via this type of channel.

Key words: Cation sensitive gating, HEK293 cells, KAT1, potassium affinity


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 Plant Physiol.Home page
M. Mikosch, A. C. Hurst, B. Hertel, and U. Homann
Diacidic Motif Is Required for Efficient Transport of the K+ Channel KAT1 to the Plasma Membrane
Plant Physiology, November 1, 2006; 142(3): 923 - 930.
[Abstract] [Full Text] [PDF]


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