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Originally published In Press as doi:10.1074/jbc.M203943200 on July 11, 2002

J. Biol. Chem., Vol. 277, Issue 38, 34909-34917, September 20, 2002
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Modulation of a Brain Voltage-gated K+ Channel by Syntaxin 1A Requires the Physical Interaction of Gbeta gamma with the Channel*

Izhak MichaelevskiDagger , Dodo ChikvashviliDagger , Sharon Tsuk, Oded Fili, Martin J. Lohse§, Dafna Singer-Lahat, and Ilana Lotan

From the Department of Physiology and Pharmacology, Sackler Faculty of Medicine, Tel-Aviv University, 69978 Ramat-Aviv, Israel and the § Department of Pharmacology, Institute of Pharmacology and Toxicology, University of Wurzburg, Wurzburg D-97078 Germany

Recently we suggested that direct interactions between voltage-gated K+ channels and proteins of the exocytotic machinery, such as those observed between the Kv1.1/Kvbeta channel, syntaxin 1A, and SNAP-25 may be involved in neurotransmitter release. Furthermore, we demonstrated that the direct interaction with syntaxin 1A enhances the fast inactivation of Kv1.1/Kvbeta 1.1 in oocytes. Here we show that G-protein beta gamma subunits play a crucial role in the enhancement of inactivation by syntaxin 1A. The effect caused by overexpression of syntaxin 1A is eliminated in the presence of chelators of endogenous beta gamma subunits in the whole cell and at the plasma membrane. Conversely, enhancement of inactivation caused by overexpression of beta 1gamma 2 subunits is eliminated upon knock-down of endogenous syntaxin or its scavenging at the plasma membrane. We further show that the N terminus of Kv1.1 binds brain synaptosomal and recombinant syntaxin 1A and concomitantly binds beta 1gamma 2; the binding of beta 1gamma 2 enhances that of syntaxin 1A. Taken together, we suggest a mechanism whereby syntaxin and G protein beta gamma subunits interact concomitantly with a Kv channel to regulate its inactivation.

* This work was supported by Israel Science Foundation Grant 437/98 (to I. L.), United States-Israel Binational Science Foundation Grant 1999396 (to I. L.), and a grant from the Deutsche Forschungsgemeinschaft (to M. 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.

Dagger Both authors contributed equally to this work.

To whom correspondence should be addressed: Dept. of Physiology and Pharmacology, Sackler School of Medicine, Tel Aviv University, 69978 Ramat-Aviv, Israel. Tel.: 972-3-6409863; Fax: 972-3-6409113; E-mail: ilotan@post.tau.ac.il.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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