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J. Biol. Chem., Vol. 278, Issue 20, 18448-18454, May 16, 2003
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From the Diacylglycerol kinase (DGK) and protein
kinase C (PKC) are two distinct enzyme families associated with
diacylglycerol. Both enzymes have cysteine-rich C1 domains (C1A, C1B,
and C1C) in the regulatory region. Although most PKC C1 domains
strongly bind phorbol esters, there has been no direct evidence that
DGK C1 domains bind phorbol esters. We synthesized 11 cysteine-rich
sequences of DGK C1 domains with good sequence homology to those of the PKC C1 domains. Among them, only DGK
Synthesis and Phorbol Ester Binding of the
Cysteine-rich Domains of Diacylglycerol Kinase (DGK) Isozymes
DGK
AND DGK
ARE NEW TARGETS OF TUMOR-PROMOTING PHORBOL
ESTERS*
,
,, and
Applied Biosystems Japan Ltd., 4-5-4 Hacchobori, Chuo-ku, Tokyo 104-0032, § Division of Food
Science and Biotechnology, Graduate School of Agriculture, Kyoto
University, Kitashirakawa Oiwake-cho, Sakyo-ku, Kyoto 606-8502, and
Biosignal Research Center, Kobe University, 1-1 Rokkodai-cho,
Nada-ku, Kobe 657-8501, Japan
-C1A and DGK-C1A exhibited significant binding to phorbol 12,13-dibutyrate (PDBu). Scatchard analysis of rat-DGK-C1A, human-DGK-C1A, and human-DGK-C1A gave Kd values of 3.6, 2.8, and 14.6 nM,
respectively, suggesting that DGK and DGK are new targets of
phorbol esters. An A12T mutation of human-DGK-C1A enhanced the
affinity to bind PDBu, indicating that the -hydroxyl group of
Thr-12 significantly contributes to the binding. The
Kd value for PDBu of FLAG-tagged whole rat-DGK
(4.4 nM) was nearly equal to that of rat-DGK-C1A (3.6 nM). Moreover, 12-O-tetradecanoylphorbol
13-acetate induced the irreversible translocation of whole rat-DGK
and its C1B deletion mutant, not the C1A deletion mutant, from
the cytoplasm to the plasma membrane of CHO-K1 cells. These results
indicate that 12-O-tetradecanoylphorbol 13-acetate binds to
C1A of DGK to cause its translocation.
*
This work was supported in part by a Grant-in-aid
for Scientific Research on Priority Areas (A) (2) 12045241 and 13024245 from the Ministry of Education, Science, Culture, and Sports of Japan
(to K. I.) and a grant from Takeda Science Foundation (to K. I.).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.
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