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Diacylglycerol kinase, delta 130kDa

diglyceride kinase, DGKdelta
This gene encodes a cytoplasmic enzyme that phosphorylates diacylglycerol to produce phosphatidic acid. Diacylglycerol and phosphatidic acid are two lipids that act as second messengers in signaling cascades. Their cellular concentrations are regulated by the encoded protein, and so it is thought to play an important role in cellular signal transduction. Alternative splicing results in two transcript variants encoding different isoforms. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: ACID, CAN, fibrillin-1, HAD, V1a
Papers on diglyceride kinase
DGKζ is involved in LPS-activated phagocytosis through IQGAP1/Rac1 pathway.
GeneRIF
Goto et al., Yamagata, Japan. In Biochem Biophys Res Commun, 2012
These results suggest that DGKzeta is involved in IQGAP1/Rac1-mediated phagocytosis upon LPS stimulation in macrophages.
Analysis of the genotype of diacylglycerol kinase delta single-nucleotide polymorphisms in Parkinson disease in the Han Chinese population.
GeneRIF
Shang et al., Chengdu, China. In Neurol India, 2012
This study demonistrated that the lack of association of DGKD SNPs with PD in the Han Chinese population.
Zinc binding drives sheet formation by the SAM domain of diacylglycerol kinase δ.
GeneRIF
Bowie et al., Los Angeles, United States. In Biochemistry, 2010
Zinc site mutations impair DGKdelta localization to cytoplasmic puncta and enhance localization the plasma membrane.
Diacylglycerol kinase delta and protein kinase C(alpha) modulate epidermal growth factor receptor abundance and degradation through ubiquitin-specific protease 8.
GeneRIF
Topham et al., Salt Lake City, United States. In J Biol Chem, 2010
Data indicate a novel mechanism where diacylglycerol kinase delta and protein kinase Calpha modulate the levels of ubiquitinated epidermal growth factor receptors through Akt and ubiquitin-specific protease 8.
Diacylglycerol kinase delta associates with receptor for activated C kinase 1, RACK1.
Sakane et al., Sapporo, Japan. In Biochim Biophys Acta, 2009
DGKdelta, which is distributed to clathrin-coated vesicles, interacts with DGKdelta itself, protein kinase C and AP2alpha.
Regulation of enzyme localization by polymerization: polymer formation by the SAM domain of diacylglycerol kinase delta1.
GeneRIF
Bowie et al., Los Angeles, United States. In Structure, 2008
Polymerization of DGK delta regulates the activity of the enzyme by sequestering DGK delta in an inactive cellular location.
Downregulation of diacylglycerol kinase delta contributes to hyperglycemia-induced insulin resistance.
Impact
GeneRIF
Zierath et al., Stockholm, Sweden. In Cell, 2008
Metabolic flexibility, evident by the transition between lipid and carbohydrate utilization during fasted and fed conditions, was impaired in DGKdelta haploinsufficient mice.
Regulation of clathrin-dependent endocytosis by diacylglycerol kinase delta: importance of kinase activity and binding to AP2alpha.
Saito et al., Kōbe, Japan. In Biochem J, 2008
DGKdelta (diacylglycerol kinase delta), which phosphorylates DAG (diacylglycerol) and converts it into PA (phosphatidic acid), has an important role in signal transduction.
Glucose regulates diacylglycerol intracellular levels and protein kinase C activity by modulating diacylglycerol kinase subcellular localization.
Formisano et al., Napoli, Italy. In J Biol Chem, 2007
However, antisense silencing of DGKdelta, but not of DGKalpha expression, was sufficient to prevent the effect of high glucose on PKCalpha activity, insulin receptor signaling, and glucose uptake.
Diacylglycerol kinase delta regulates protein kinase C and epidermal growth factor receptor signaling.
GeneRIF
Topham et al., Salt Lake City, United States. In Proc Natl Acad Sci U S A, 2006
Results suggest that diacylglycerol kinase delta regulates epidermal growth factor receptors by modulating protein kinase C signaling.
Identification and characterization of a novel human type II diacylglycerol kinase, DGK kappa.
Sakane et al., Sapporo, Japan. In J Biol Chem, 2006
The kappa-isozyme (1271 amino acids, calculated molecular mass, 142 kDa) contains a pleckstrin homology domain, two cysteine-rich zinc finger-like structures, and a separated catalytic region as have been found commonly for the type II isozymes previously cloned (DGKdelta and DGKeta).
Alternative splicing of the human diacylglycerol kinase delta gene generates two isoforms differing in their expression patterns and in regulatory functions.
GeneRIF
Kanoh et al., Sapporo, Japan. In J Biol Chem, 2002
Alternative splicing of the gene generates two isoforms differing in their expression patterns and in regulatory functions
Determination of ceramides and diglycerides by the diglyceride kinase assay.
Review
Hannun et al., Charleston, United States. In Anal Biochem, 2001
This review will discuss the utilization of the diglyceride (DG) kinase assay as an analytical method that allows the simultaneous quantitation of DG and ceramide from cell and tissue samples.
Progesterone induces meiotic division in the amphibian oocyte by releasing lipid second messengers from the plasma membrane.
Review
Kostellow et al., United States. In Steroids, 1999
Within minutes, diglyceride kinase converts newly formed DAG species to phosphatidic acid, turning off the successive DAG signals.
Diglyceride Kinase Activity in Cell Extracts of Rhizobium meliloti: Evidence for a Diglyceride Cycle during Cyclic beta-1,2-Glucan Biosynthesis.
Miller et al., United States. In Appl Environ Microbiol, 1991
In this article, we provide evidence for the presence of diglyceride kinase activity in cell extracts of Rhizobium meliloti 1021.
[Eicosanoids and phospholipases].
Review
Schettler et al., In Klin Wochenschr, 1985
Alternatively diglyceride is phosphorylated by diglyceride kinase yielding phosphatidic acid, which is believed to be reincorporated into phosphatidylinositol.
The structure of rat liver triglycerides.
Lands et al., Ann Arbor, United States. In Lipids, 1968
The fatty acid compositions at the 1-, 2-, and 3-positions(3) of rat liver triglycerides were determined by using pancreatic lipase and diglyceride kinase.
A micromethod for the stereospecific determination of triglyceride structure.
Zschocke et al., Ann Arbor, United States. In Lipids, 1966
Triglyceride lipase and diglyceride kinase can be used in a sensitive stereospecific analysis of the separate fatty acid compositions at the 1, 2 and 3 positions of a triglyceride.Diglyceride kinase fromEscherichia coli selectively catalyzes the phosphorylation of 1,2-diglycerides but not the 2,3-diglycerides.The composition of the 3-position in rat liver triglycerides is clearly different from that at the 1-position.
Studies on the carrier function of phosphatidic acid in sodium transport. I. The turnover of phosphatidic acid and phosphoinositide in the avian salt gland on stimulation of secretion.
HOKIN et al., In J Gen Physiol, 1960
The enzymes, diglyceride kinase and phosphatidic acid phosphatase, which catalyze the stimulated turnover of phosphatidic acid in brain cortex, were also found in highest concentration in the microsome fraction.
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