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J. Biol. Chem., Vol. 280, Issue 11, 9870-9878, March 18, 2005

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Translocation of Diacylglycerol Kinase from Cytosol to Plasma Membrane in Response to Activation of G Protein-coupled Receptors and Protein Kinase C^*

Jürgen van Baal, John de Widt, Nullin Divecha, and Wim J. van Blitterswijk

From the Division of Cellular Biochemistry, The Netherlands Cancer Institute, Amsterdam 1066 CX, The Netherlands

Diacylglycerol kinase (DGK) phosphorylates the second messenger diacylglycerol (DAG) to phosphatidic acid. We previously identified DGK as one of nine mammalian DGK isoforms and reported on its regulation by interaction with RhoA and by translocation to the plasma membrane in response to noradrenaline. Here, we have investigated how the localization of DGK, fused to green fluorescent protein, is controlled upon activation of G protein-coupled receptors in A431 cells. Extracellular ATP, bradykinin, or thrombin induced DGK translocation from the cytoplasm to the plasma membrane within 2–6 min. This translocation, independent of DGK activity, was preceded by protein kinase C (PKC) translocation and was blocked by PKC inhibitors. Conversely, activation of PKC by 12-O-tetradecanoylphorbol-13-acetate induced DGK translocation. Membrane-permeable DAG (dioctanoylglycerol) also induced DGK translocation but in a PKC (staurosporin)-independent fashion. Mutations in the cysteine-rich domains of DGK abrogated its hormone- and DAG-induced translocation, suggesting that these domains are essential for DAG binding and DGK recruitment to the membrane. We show that DGK interacts selectively with and is phosphorylated by PKC and - and that peptide agonist-induced selective activation of PKC directly leads to DGK translocation. Our data are consistent with the concept that hormone-induced PKC activation regulates the intracellular localization of DGK, which may be important in the negative regulation of PKC and/or PKC activity.

Received for publication, August 13, 2004 , and in revised form, November 19, 2004.

^* This work was supported by the Dutch Cancer Society, Grant NKI 2000-2209. 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 four additional figures and four videos.

To whom correspondence may be addressed. Fax: 31-205121989; E-mail: n.divecha{at}nki.nl. To whom correspondence may be addressed. Fax: 31-205121989; E-mail: w.v.blitterswijk{at}nki.nl.

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