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(S)-2-amino-2-((S)-6-octyl-1,2,3,4-tetrahydronaphthalen-2-yl)propan-1-ol
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analogue of FTY720, 0.01 mM increase phosphorylation of 1-O-hexadecyl-sn-2-acetyl glycerol by isoform diacylglycerol kinase alpha about 3.5fold.
1,3-dioleoylglycerol
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activates
1-monooleoylglycerol
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activates
1-O-alkylphosphatidylcholine
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half-maximal activation at 21.9 mol%
1-palmitoyl-2-oleoylglycerophosphocholine
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activates
4-(2,4-dimethylphenoxy)-N-hydroxybutanamide
0.1 mM KU-10 activates isoform DGKalpha by about 10%
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4beta-phorbol-12-myristate-13-acetate
enhances voltage-dependent opening of wild-type and cAMP/H+-uncoupled hyperpolarization activated, cyclic nucleotide-regulated channels. 4beta-Phorbol-12-myristate-13-acetate exerts its effects on channel gating via sequential activation ofprotein kinase C and diacylglycerol kinase coupled with upregulation of mitogen-activated protein kinase and phospholipase A2
acidic phospholipids
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activation in vitro
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benzothiadiazole
activation of the expression of diacylglycerol kinase OsDAGK1
bis-phosphatidic acid
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half-maximal activation at 3.9 mol%
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cAMP
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stimulates nuclear diacylglycerol kinase catalytic activity
cholesterol 3-sulfate
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activates
D-glucose
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exposure of L6 cell myotubes overexpressing human insulin receptors to 25 mM glucose for 5 min decreases the intracellular levels of diacylglycerol, paralleled by transient activation of diacylglycerol kinase and of insulin receptor signaling. Following 30-min exposure, both diacylglycerol levels and diacylglycerol kinase activity return close to basal levels. Glucose exposure redistributes diacylglycerol kinase isoforms alpha and delta, from the prevalent cytosolic localization to the plasma membrane fraction
detergent
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no activity in absence of detergent
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di-O-hexadecylphosphatidylcholine
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half-maximal activation at 13.5 mol%
diacylglycerol 3-phosphate
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the enzyme apoprotein is attributed to a novel feedback activation involving diacylglycerol 3-phosphate
dilauroyl-N,N-dimethylglycerophosphoethanolamine
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activates
dilauroyl-N-methylglycerophosphoethanolamine
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activates
dilauroylglycerophosphocholine
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activates
dilauroylglycerophosphoethanolamine
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activates
dilauroylphosphatidylcholine
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half-maximal activation at 11.9 mol%
dimethylmyristamide
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activates
dioleoyl ethylene glycol
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activates
dioleoyl-phosphatidylglycerol
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dioleoylphosphatidylcholine
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half-maximal activation at 10.4 mol%
dioleoylphosphatidylglycerol
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half-maximal activation at 6.3 mol%
dipalmitoylphosphatidic acid
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activates only in presence of Triton X-100
endothelin-1
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activates diacylglycerol kinase in caveolae/rafts and noncaveolae/rafts of mesenteric arteries. Activation does not depend on phosphatidylinositol 3-kinase. In response to norepinephrin, but not to epithelin-1, protein kinase PKB translocates to caveolae/rafts
epigallocatechin gallate
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FTY720
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in presence of 0.01 mM FTY720, phosphorylation of 1-O-hexadecyl-sn-2-acetyl glycerol by isoforms diacylglycerol kinase alpha, beta or gamma is 3fold increased
H2O2
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endogenous nuclear diacylglycerol kinase zeta rapidly translocates to the cytoplasm following H2O2 treatment
hepatocyte growth factor
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induces diaclyglycerol kinase activity, which is required for cell invasiveness
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hexadecyl phosphorylcholine
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half-maximal activation at 17.3 mol%
hexadecylphosphorylcholine
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activates
lauryl maltoside
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activates in presence of 11 mM Triton X-100
Lipid
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purified enzyme is completely inactive unless a lipid is added to the assay buffer containing Triton X-100
lysophosphatidylcholine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
lysophosphatidylethanolamine
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activates
methyl myristate
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activates
myristoylcholine chloride
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activates
myristyl acetate
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activates
n-hexyl beta-D-glucoside
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activates in presence of 11 mM Triton X-100
N-[7-[cyclopropyl(hydroxy)methyl]-2,3-dihydro-1,4-benzodioxin-6-yl]cyclopropanecarboxamide
0.1 mM KU-8 activates isoform DGKalpha by 19%
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nitrododecane
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activates
norepinephrine
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stimulates an increase in diacylglycerol kinase activity in caveolae/rafts of mesenteric arteries. Activation depends on phosphatidylinositol 3-kinase. In response to norepinephrin, but not to epithelin-1, protein kinase PKB translocates to caveolae/rafts
octyl acetate
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activates
octyl beta-glucoside
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activates in presence of 11 mM Triton X-100
oleic acid
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activates only in presence of Triton X-100
oleoylcholine chloride
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activates
palmitic acid
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activates only in presence of Triton X-100
phorbol-12-myristate-13-acetate
diacylglycerol kinase zeta activity at the T cell receptor is enhanced by phorbol-12-myristate-13-acetate cotreatment
phosphatidyl glycerol
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good activator
phosphatidylcholine plasmalogen
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half-maximal activation at 7.3 mol%
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phosphatidylglycerol
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effective stimulation
phosphatidylinositol 4,5-bisphosphate
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highly stimulating
platelet-activating factor
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half-maximal activation at 22.4 mol%
rac-1,2-dioleoylglycero-3-sulfate
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half-maximal activation at 2.7 mol%
sn-1,2-dioleoylglycerol
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activates
sn-1,3-dioleoylglycerol
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activates
sodium cholate
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enhances activity of DGK I and DGK IV
sodium deoxycholate
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enhances activity of DGK I and DGK IV
Sodium dodecyl sulfate
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activates
sodium hexadecyl sulfate
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half-maximal activation at 9.8 mol%
sphingomyelin
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
stearic acid
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activates only in presence of Triton X-100
stearoyllysophosphatidylcholine
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half-maximal activation at 15.8 mol%
cardiolipin
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activates
cardiolipin
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good activator
cardiolipin
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mitochondrial, half-maximal activation at 2.3 mol%
cardiolipin
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half-maximal activation by 1 mol%
cholesterol
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such cholesterol
cholesterol
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such cholesterol
deoxycholate
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stimulation
deoxycholate
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purified enzyme is completely devoid of activity without addition of phospholipid or deoxycholate
deoxycholate
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enhances activity of enzyme form DGK-II and DGK-III, enzyme form DGK-I is not much affected
deoxycholate
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the enzyme shows optimal activity in presence of phosphatidylserine or deoxycholate. Lower activity in presence of phosphatidylcholine. Diacylglycerol analogs containing an unsaturated fatty acid at the sn-2 position give optimal enzyme activity irrespective of the presence of deoxycholate
deoxycholate
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enhances activity
P53
p53 activates DGKalpha in response to DNA damage
P53
p53 activates DGKalpha in response to DNA damage
phosphatidic acid
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highly stimulating
phosphatidic acid
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activates only in presence of Triton X-100
phosphatidic acid
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more effective activator than phosphatidylserine. Phosphatidic acid decreases the apparent surface KM of DGKtheta for dioleoylglycerol and promotes binding to vesicles in a dose-dependent manner
phosphatidic acid
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phosphatidic acid is more effective than phosphatidiylserine. Both decreases the apparent surface KM value for dioleoylglycerol and promote binding to vesicles, but through different mechanisms
phosphatidic acid
production of oxidative burst and hypersensitive cell death. Activation of the epxression of diacylglycerol kinase and transcritional factor gene OsBIERF3. Neomycin partially inhibits the poduction of oxidatve burst, hypersensitive cell death, and expression of both genes
phosphatidic acid
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good activator of DGK IV, no effect on DGK I activity
phosphatidylcholine
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phosphatidylcholine
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activates
phosphatidylcholine
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the enzyme shows optimal activity in presence of phosphatidylserine or deoxycholate. Lower activity in presence of phosphatidylcholine
phosphatidylcholine
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moderate enhancement of DGK IV, no effect on DGK I activity
phosphatidylcholine
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enzyme type II has a preference for phosphatidylcholine as cofactor, enzyme type I can utilize both phosphatidylserine and phosphatidylinositol, but has a lower preference for phosphatidylcholine
phosphatidylcholine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylethanolamine
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activates only in presence of Triton X-100
phosphatidylethanolamine
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plus cardiolipin, activates
phosphatidylethanolamine
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such as phosphatidylethanolamine
phosphatidylethanolamine
DGKalpha can be activated in vitro in a Ca2+-independent manner by lipids such as phosphatidylethanolamine
phosphatidylethanolamine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylinositol
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effective stimulation
phosphatidylinositol
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enzyme type II has a preference for phosphatidylcholine as cofactor, enzyme type I can utilize both phosphatidylserine and phosphatidylinositol, but has a lower preference for phosphatidylcholine
phosphatidylinositol
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enhances activity of DGK I and DGK IV
phosphatidylserine
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strong activation
phosphatidylserine
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activates
phosphatidylserine
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good activator
phosphatidylserine
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the enzyme shows optimal activity in presence of phosphatidylserine or deoxycholate. Lower activity in presence of phosphatidylcholine
phosphatidylserine
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less effective activator than phosphatidic acid. Phosphatidylserine decreases the apparent surface KM of DGKtheta for dioleoylglycerol
phosphatidylserine
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phosphatidic acid is more effective than phosphatidiylserine. Both decreases the apparent surface KM value for dioleoylglycerol and promote binding to vesicles, but through different mechanisms
phosphatidylserine
broadens the pH-dependent activity when the enzyme is assayed in cytosolic extracts. Phosphatidylserineconcentrates Mg2+ ions at the interface
phosphatidylserine
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enzyme type II has a preference for phosphatidylcholine as cofactor, enzyme type I can utilize both phosphatidylserine and phosphatidylinositol, but has a lower preference for phosphatidylcholine
phosphatidylserine
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enhances activity of DGK I and DGK IV
phosphatidylserine
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activates
phosphatidylserine
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activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
phosphatidylserine
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10-20 mol% result in 7.5-7.8fold activation of the recombinant wild-type enzyme, 3.8fold of the recombinant mutant DELTA196, and 6.5fold of the recombinant mutant DELTA332
Phospholipid
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purified enzyme is completely devoid of activity without addition of phospholipid or deoxycholate
Phospholipid
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a combination of diacylglycerol and phospholipid exclusively leads to full activation
Phospholipid
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activation by phospholipid is not stereospecific and is mimicked partially by fatty acids
Phospholipid
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enhances activity. Activation of phospholipids in the order of decreasing efficiency: phosphatidylcholine, lysophosphatidylcholine, phosphatidylethanolamine, phosphatidylserine, sphingomyelin
sphingosine
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in presence of 0.01 mM sphingosine, phosphorylation of 1-O-hexadecyl-sn-2-acetyl glycerol by isoforms diacylglycerol kinase alpha, beta or gamma is 7-9fold increased
sphingosine
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potently activates the 80000 Da enzyme
additional information
the isozyme DGK2 is induced by exposure to low temperatures, e.g. 4°C
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additional information
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the isozyme DGK2 is induced by exposure to low temperatures, e.g. 4°C
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additional information
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serotonin signalling activates the enzyme
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additional information
DGKzeta interacts with and is regulated by the retinoblastoma protein
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additional information
isozyme DGK-teta is dependent on an activating accessory protein containing a poly-basic region, the broadening of the pH profile of DGK-theta is also dependent on a PBR-containing activator
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