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Published Online September 21, 2006
Science DOI: 10.1126/science.1131163

Reports

Submitted on June 12, 2006
Accepted on August 25, 2006

Rapid Chemically Induced Changes of PtdIns(4,5)P2 Gate KCNQ Ion Channels

Byung-Chang Suh 1, Takanari Inoue 2, Tobias Meyer 2, Bertil Hille 1*

1 Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195, USA.
2 Department of Molecular Pharmacology, Stanford University, Clark Center, 318 Campus Drive, Stanford, CA 94305, USA.

* To whom correspondence should be addressed.
Bertil Hille , E-mail: hille{at}u.washington.edu

To resolve controversy about messengers regulating KCNQ ion channels during phospholipase C-mediated suppression of current, we designed translocatable enzymes that quickly alter the phosphoinositide composition of the plasma membrane after application of a chemical cue. The KCNQ current falls rapidly to zero when PtdIns(4,5)P2 is depleted without changing Ca2+, diacylglycerol, or InsP3. Current rises by 30% when PtdIns(4,5)P2 is overproduced and does not change when PtdIns(3,4,5)P3 is raised. Hence depletion of PtdIns(4,5)P2 suffices to suppress current fully, and other second messengers are not needed. Our approach is ideally suited to study biological signaling networks involving membrane phosphoinositides.


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