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Originally published In Press as doi:10.1074/jbc.M602215200 on August 10, 2006
J. Biol. Chem., Vol. 281, Issue 40, 29693-29702, October 6, 2006
Receptor-induced Activation of Drosophila TRP by Polyunsaturated Fatty Acids*
Simone Jörs ,
Victor Kazanski ,
Anna Foik ,
Dietmar Krautwurst¶, and
Christian Harteneck 1
From the
Institut für Pharmakologie, Charité Campus Benjamin Franklin, Thielallee 69-73, 14195 Berlin, Fachbereich Biologie, Chemie, Pharmazie, Freie Universität Berlin, Takustrasse 3, 14195 Berlin, and ¶Abteilung für Molekulare Genetik, Deutsches Institut für Ernährungsforschung Potsdam-Rehbrücke, Arthur-Scheunert-Allee 114-116, 14558 Nuthetal, Germany
Cellular calcium homeostasis is regulated by hormones and neurotransmitters, resulting in the activation of a variety of proteins, in particular, channel proteins of the plasma membrane and of intracellular compartments. Such channels are, for example, TRP channels of the TRPC protein family that are activated by various mediators from receptor-stimulated signaling cascades. In Drosophila, two TRPC channels, TRP and TRPL, are involved in phototransduction. In addition, a third Drosophila TRPC channel, TRP , has been identified and described as an auxiliary subunit of TRPL. Beyond it, our data show that heterologously expressed TRP formed a receptor-activated, outwardly rectifying cation channel independent from TRPL co-expression. Analysis of the activation mechanism revealed that TRP is activated by various polyunsaturated fatty acids generated in a phospholipase C- and phospholipase A2-dependent manner. The most potent activator of TRP , the stable analogue of arachidonic acid, 5,8,11,14-eicosatetraynoic acid, induced currents in single channel recordings. Here we show that upon heterologous expression TRP forms a homomeric channel complex that is activated by polyunsaturated fatty acids as mediators of receptor-dependent signaling pathways. Reverse transcription PCR analysis showed that TRP is expressed in Drosophila heads and bodies. Its body-wide expression pattern and its activation mechanism suggest that TRP forms a fly cation channel responsible for the regulation of intracellular calcium in a variety of hormonal signaling cascades.
Received for publication, March 9, 2006
, and in revised form, July 28, 2006.
* This work was supported by the Deutsche Forschungsgemeinschaft, Fonds der Chemischen Industrie, and Sonnenfeld-Stiftung. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.
The on-line version of this article (available at http://www.jbc.org) contains supplemental Figs. S1S3.
1 To whom correspondence should be addressed. Tel.: 49-30-84451825; Fax: 49-30-84451818; E-mail: Christian.Harteneck{at}charite.de.

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Copyright © 2006 by the American Society for Biochemistry and Molecular Biology.
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