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Science 6 November 1998:
Vol. 282. no. 5391, pp. 1141 - 1144
DOI: 10.1126/science.282.5391.1141
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Reports

PIP2 and PIP as Determinants for ATP Inhibition of KATP Channels

Thomas Baukrowitz, * Uwe Schulte, * Dominik Oliver, Stefan Herlitze, Tobias Krauter, Stephen J. Tucker, J. Peter Ruppersberg, Bernd Fakler dagger

Adenosine triphosphate (ATP)-sensitive potassium (KATP) channels couple electrical activity to cellular metabolism through their inhibition by intracellular ATP. ATP inhibition of KATP channels varies among tissues and is affected by the metabolic and regulatory state of individual cells, suggesting involvement of endogenous factors. It is reported here that phosphatidylinositol-4,5-bisphosphate (PIP2) and phosphatidylinositol-4-phosphate (PIP) controlled ATP inhibition of cloned KATP channels (Kir6.2 and SUR1). These phospholipids acted on the Kir6.2 subunit and shifted ATP sensitivity by several orders of magnitude. Receptor-mediated activation of phospholipase C resulted in inhibition of KATP-mediated currents. These results represent a mechanism for control of excitability through phospholipids.

T. Baukrowitz, U. Schulte, D. Oliver, S. Herlitze, T. Krauter, J. P. Ruppersberg, B. Fakler, Department of Physiology II, University of Tübingen, Gmelinstrasse 5, 72076 Tübingen, Germany. S. J. Tucker, University Laboratory of Physiology, Parks Road, Oxford OX1 3PT, UK.
*   These authors contributed equally to this work.

dagger    To whom correspondence should be addressed. E-mail: bernd.fakler{at}uni-tuebingen.de

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