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Originally published In Press as doi:10.1074/jbc.M202035200 on June 25, 2002

J. Biol. Chem., Vol. 277, Issue 38, 35323-35332, September 20, 2002
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Phorbol Ester-regulated Oligomerization of Diacylglycerol Kinase delta  Linked to Its Phosphorylation and Translocation*

Shin-ichi Imai, Fumio SakaneDagger , and Hideo Kanoh

From the Department of Biochemistry, Sapporo Medical University School of Medicine, South-1, West-17, Chuo-ku, Sapporo 060-8556, Japan

Diacylglycerol kinase (DGK) plays an important role in signal transduction through modulating the balance between two signaling lipids, diacylglycerol and phosphatidic acid. In yeast two-hybrid screening, we unexpectedly found a self-association of the C-terminal part of DGKdelta containing a sterile alpha -motif (SAM) domain. We then bacterially expressed the SAM domain fused with maltose-binding protein and confirmed the formation of dimeric and tetrameric structures. Moreover, gel filtration and co-immunoprecipitation analyses demonstrated that DGKdelta formed homo-oligomeric structures in intact cells and that the SAM domain was critically involved in the oligomerization. Interestingly, phorbol ester stimulation induced dissociation of the oligomeric structures with concomitant phosphorylation of DGKdelta . Furthermore, we found that DGKdelta was translocated from cytoplasmic vesicles to the plasma membrane upon phorbol ester stimulation. In this case, DGKdelta mutants lacking the ability of self-association were localized at the plasma membranes even in the absence of phorbol ester. A protein kinase C inhibitor, staurosporine, blocked all of the effects of phorbol ester, i.e. oligomer dissociation, phosphorylation, and translocation. We confirmed that tumor-promoting phorbol esters did not directly bind to DGKdelta . The present studies demonstrated that the formation and dissociation of oligomers serve as the regulatory mechanisms of DGKdelta and that DGKdelta is a novel downstream effector of phorbol ester/protein kinase C signaling pathway.

* This work was supported by Special Coordination Funds (to H. K.) and grants from the Ministry of Education, Culture, Sports, Science and Technology, the Japanese Government (to S. I., F. S., and H. K.), the Hokkaido Foundation for the Promotion of Scientific and Industrial Technology (to F. S.), and the Naito Foundation (to F. S.).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 To whom correspondence should be addressed: Dept. of Biochemistry, Sapporo Medical University School of Medicine, South-1, West-17, Chuo-ku, Sapporo 060-8556, Japan. Tel.: 81-11-611-2111; Fax: 81-11-622-1918; E-mail: sakane@sapmed.ac.jp.

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