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First published online August 19, 2005; 10.1104/pp.105.065599

Plant Physiology 139:417-424 (2005)
© 2005 American Society of Plant Biologists

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CELL BIOLOGY AND SIGNAL TRANSDUCTION

TPK1 Is a Vacuolar Ion Channel Different from the Slow-Vacuolar Cation Channel1

Hermann Bihler2,3, Christian Eing2, Simon Hebeisen4, Anja Roller, Katrin Czempinski and Adam Bertl*

Botanisches Institut I, Universität Karlsruhe, D–76128 Karlsruhe, Germany (H.B., C.E., S.H., A.R., A.B.); and Universität Potsdam, Institut für Biochemie und Biologie, D–14476 Golm, Germany (K.C.)

TPK1 (formerly KCO1) is the founding member of the family of two-pore domain K+ channels in Arabidopsis (Arabidopsis thaliana), which originally was described following expression in Sf9 insect cells as a Ca2+- and voltage-dependent outwardly rectifying plasma membrane K+ channel. In plants, this channel has been shown by green fluorescent protein fusion to localize to the vacuolar membrane, which led to speculations that the TPK1 gene product would be a component of the nonselective, Ca2+ and voltage-dependent slow-vacuolar (SV) cation channel found in many plants species. Using yeast (Saccharomyces cerevisiae) as an expression system for TPK1, we show functional expression of the channel in the vacuolar membrane. In isolated vacuoles of yeast yvc1 disruption mutants, the TPK1 gene product shows ion channel activity with some characteristics very similar to the SV-type channel. The open channel conductance of TPK1 in symmetrically 100 mM KCl is slightly asymmetric with roughly 40 pS at positive membrane voltages and 75 pS at negative voltages. Similar to the SV-type channel, TPK1 is activated by cytosolic Ca2+, requiring micromolar concentration for activation. However, in contrast to the SV-type channel, TPK1 exhibits strong selectivity for K+ over Na+, and its activity turned out to be independent of the membrane voltage over the range of ±80 mV. Our data clearly demonstrate that TPK1 is a voltage-independent, Ca2+-activated, K+-selective ion channel in the vacuolar membrane that does not mediate SV-type ionic currents.

1 This work was supported by the Deutsche Forschungsgemeinschaft (grant nos. Be1181/6–1 to A.B. and Cz87/1–1 to K.C.).

2 These authors contributed equally to the paper.

3 Present address: Molecular Biophysics and Biochemistry, Yale University, 266 Whitney Avenue, P.O. Box 208114, New Haven, CT 06520–8114.

4 Present address: Naturwissenschaftliches und Medizinisches Institut an der Universität Tübingen, Markwiesenstrasse 55, D–72770 Reutlingen, Germany.

Article, publication date, and citation information can be found at www.plantphysiol.org/cgi/doi/10.1104/pp.105.065599.

* Corresponding author; e-mail adam.bertl{at}botanik1.uni-karlsruhe.de; fax 49–721–608–4193.

Received May 16, 2005; returned for revision May 27, 2005; accepted May 27, 2005.




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