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J Biol Chem, Vol. 274, Issue 51, 36065-36072, December 17, 1999

Distinct Specificities of Inwardly Rectifying K+ Channels for Phosphoinositides*

Tibor Rohács, Jian ChenDagger , Glenn D. PrestwichDagger , and Diomedes E. Logothetis§

From the Department of Physiology and Biophysics, Mount Sinai School of Medicine of the New York University, New York, New York 10029 and the Dagger  Department of Medicinal Chemistry, University of Utah, Salt Lake City, Utah 84112

Activation of several inwardly rectifying K+ channels (Kir) requires the presence of phosphatidylinositol 4,5-bisphosphate (PtdIns(4,5)P2). The constitutively active Kir2.1 (IRK1) channels interact with PtdIns(4,5)P2 strongly, whereas the G-protein activated Kir3.1/3.4 channels (GIRK1/GIRK4), show only weak interactions with PtdIns(4,5)P2. We investigated whether these inwardly rectifying K+ channels displayed distinct specificities for different phosphoinositides. IRK1, but not GIRK1/GIRK4 channels, showed a marked specificity toward phosphates in the 4,5 head group positions. GIRK1/GIRK4 channels were activated with a similar efficacy by PtdIns(3,4)P2, PtdIns(3,5)P2, PtdIns(4,5)P2, and PtdIns(3,4,5)P3. In contrast, IRK1 channels were not activated by PtdIns(3,4)P2 and only marginally by high concentrations of PtdIns(3,5)P2. Similarly, high concentrations of PtdIns(3,4,5)P3 were required to activate IRK1 channels. For either channel, PtdIns(4)P was much less effective than PtdIns(4,5)P2, whereas PtdIns was inactive. In contrast to the dependence on the position of phosphates of the phospholipid head group, GIRK1/GIRK4, but not IRK1 channel activation, showed a remarkable dependence on the phospholipid acyl chains. GIRK1/GIRK4 channels were activated most effectively by the natural arachidonyl stearyl PtdIns(4,5)P2 and much less by the synthetic dipalmitoyl analog, whereas IRK1 channels were activated equally by dipalmitoyl and arachidonyl stearyl PtdIns(4,5)P2. Incorporation of PtdInsP2 into the membrane is necessary for activation, as the short chain water soluble diC4 PtdIns(4,5)P2 did not activate either channel, whereas activation by diC8 PtdIns(4, 5)P2 required high concentrations.

* This work was supported by Grant HL-59949 from the National Institutes of Health (to D. E. L.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

§ To whom correspondence should be addressed: Dept. of Physiology and Biophysics, Mount Sinai School of Medicine, One Gustave L. Levy Pl., Box 1218, New York, NY 10029. Tel.: 212-241-6284; Fax: 212-860-3369; E-mail: logothetis@msvax.mssm.edu.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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