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Diacylglycerol kinase, gamma 90kDa

DGKgamma, DAGK3, DAG kinase gamma, 88-kDa diacylglycerol kinase
This gene encodes an enzyme that is a member of the type I subfamily of diacylglycerol kinases, which are involved in lipid metabolism. These enzymes generate phosphatidic acid by catalyzing the phosphorylation of diacylglycerol, a fundamental lipid second messenger that activates numerous proteins, including protein kinase C isoforms, Ras guanyl nucleotide-releasing proteins and some transient receptor potential channels. Diacylglycerol kinase gamma has been implicated in cell cycle regulation and in the negative regulation of macrophage differentiation in leukemia cells. Multiple transcript variants encoding different isoforms have been found for this gene. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, GAP, Akt, beta2, Inactive
Papers on DGKgamma
Phorbol ester and hydrogen peroxide synergistically induce the interaction of diacylglycerol kinase gamma with the Src homology 2 and C1 domains of beta2-chimaerin.
Sakane et al., Sapporo, Japan. In Biochem J, 2008
the interaction of diacylglycerol kinase gamma with the Src homology 2 and C1 domains of beta2-chimaerin is induced synergistically by Phorbol ester and hydrogen peroxide
Nuclear diacylglycerol kinases: regulation and roles.
Tu-Sekine et al., Baltimore, United States. In Front Biosci, 2007
In this review we focus primarily on the nuclear localization, modulation of intrinsic enzymatic activity, and the potential physiological roles of the six diacylglycerol kinases that have been found in the nucleus: DGK-alpha, DGK-gamma, DGK-delta, DGK-zeta, DGK-iota, and DGK-theta.
Diacylglycerol kinase alpha suppresses tumor necrosis factor-alpha-induced apoptosis of human melanoma cells through NF-kappaB activation.
Sakane et al., Sapporo, Japan. In Biochim Biophys Acta, 2007
The overexpression of other type I isoforms (DGKbeta and DGKgamma) had, on the other hand, no detectable effects on the apoptosis.
Diacylglycerol kinase gamma interacts with and activates beta2-chimaerin, a Rac-specific GAP, in response to epidermal growth factor.
Sakane et al., Sapporo, Japan. In Febs Lett, 2007
Here we report that, in COS7 cells stimulated with epidermal growth factor (EGF), DGKgamma specifically interacts and co-localizes at the plasma membrane with beta2-chimaerin, a GTPase-activating protein (GAP) for Rac.
Phosphorylation and up-regulation of diacylglycerol kinase gamma via its interaction with protein kinase C gamma.
Saito et al., Kōbe, Japan. In J Biol Chem, 2006
localization and activation of the functionally correlated kinases, gammaPKC and DGKgamma, are spatio-temporally orchestrated by their direct association and phosphorylation, contributing to subtype-specific regulation of DGKgamma and DAG signaling
Nuclear transportation of diacylglycerol kinase gamma and its possible function in the nucleus.
Saito et al., Kōbe, Japan. In J Biol Chem, 2006
In an effort to investigate one of nine subtypes, we found that DGKgamma came to be localized in the nucleus with time in all cell lines tested while seen only in the cytoplasm at the early stage of culture, indicating that DGKgamma is transported from the cytoplasm to the nucleus.
Immunocytochemical localization of a neuron-specific diacylglycerol kinase beta and gamma in the developing rat brain.
Saito et al., Kōbe, Japan. In Brain Res Mol Brain Res, 2005
In brain, DGKgamma showed sustained expression throughout the postnatal developmental periods. And In the hippocampal pyramidal cell, Dgkg localized in the cytosol.
Diacylglycerol kinase gamma serves as an upstream suppressor of Rac1 and lamellipodium formation.
Sakane et al., Sapporo, Japan. In J Biol Chem, 2004
DGKgamma functions through its catalytic action as an upstream suppressor of Rac1 and has a role in lamellipodium/ruffle formation
Regulatory role of diacylglycerol kinase gamma in macrophage differentiation of leukemia cells.
Kanoh et al., Sapporo, Japan. In Biochem Biophys Res Commun, 2003
diacylglycerol kinase gamma regulates macrophage differentiation.
Synthesis and phorbol ester binding of the cysteine-rich domains of diacylglycerol kinase (DGK) isozymes. DGKgamma and DGKbeta are new targets of tumor-promoting phorbol esters.
Saito et al., Tokyo, Japan. In J Biol Chem, 2003
Among them, only DGKgamma-C1A and DGKbeta-C1A exhibited significant binding to phorbol 12,13-dibutyrate (PDBu).
Move over protein kinase C, you've got company: alternative cellular effectors of diacylglycerol and phorbol esters.
Rosenmund et al., Göttingen, Germany. In J Cell Sci, 2003
However, at least five alternative types of high-affinity diacylglycerol/phorbol-ester receptor are known: chimaerins, protein kinase D, RasGRPs, Munc13s and DAG kinase gamma.
Diacylglycerol kinase gamma is one of the specific receptors of tumor-promoting phorbol esters.
Saito et al., Tokyo, Japan. In Biochem Biophys Res Commun, 2001
We focused on DGK gamma because its C1A domain has a high degree of sequence homology to those of PKCs, and because DGK gamma translocates from the cytoplasm to the plasma membrane following 12-O-tetradecanoylphorbol-13-acetate treatment similar to PKCs.
Genetic mapping and functional studies of a natural inhibitor of the insulin receptor tyrosine kinase: the mouse ortholog of human alpha2-HS glycoprotein.
Grunberger et al., Detroit, United States. In Int J Exp Diabetes Res, 2000
We have mapped mouse Ahsg at 16 cM adjacent to the Diacylglycerol kinase 3 (Dagk3) gene on chromosome 16 by genotyping interspecific backcross panels between C57BL/6J and Mus spretus.
Subtype-specific translocation of diacylglycerol kinase alpha and gamma and its correlation with protein kinase C.
Saito et al., Kōbe, Japan. In J Biol Chem, 2000
Tetradecanoylphorbol 13-acetate (TPA) induced irreversible translocation of DGKgamma, but not DGKalpha, from the cytoplasm to the plasma membrane.
Diacylglycerol kinase in the central nervous system--molecular heterogeneity and gene expression.
Kondo et al., Yamagata, Japan. In Chem Phys Lipids, 1999
Interestingly, it is revealed that the mRNA for each isozyme is expressed in a distinct pattern in the brain; DGK alpha is expressed in oligodendrocytes, glial cells that form myelin; DGK beta in neurons of the caudate-putamen; DGK gamma predominantly in the cerebellar Purkinje cells; and DGK zeta in the cerebellar and cerebral cortices.
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