Diacylglycerol Kinase η Activity in Cells Using Protein Myristoylation and Cellular Phosphatidic Acid Sensor

Lipids ◽  
2021 ◽  
Author(s):  
Ayuka Ishizaki ◽  
Chiaki Murakami ◽  
Haruka Yamada ◽  
Fumio Sakane
Keyword(s):  
Phosphatidic Acid ◽  
Diacylglycerol Kinase ◽  
Protein Myristoylation ◽  
In Cells

Phosphatidic acid production in chitosan-elicited tomato cells, via both phospholipase D and phospholipase C/diacylglycerol kinase, requires nitric oxide

2011 ◽  
Vol 168 (6) ◽  
pp. 534-539 ◽  
Author(s):  
Nicolás Raho ◽  
Leonor Ramirez ◽  
M. Luciana Lanteri ◽  
Gabriela Gonorazky ◽  
Lorenzo Lamattina ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Phosphatidic Acid ◽  
Phospholipase C ◽  
Phospholipase D ◽  
Acid Production ◽  
Diacylglycerol Kinase

scholarly journals Activation of rat liver plasma-membrane diacylglycerol kinase by vasopressin and phenylephrine

1988 ◽  
Vol 255 (3) ◽  
pp. 923-928 ◽  
Author(s):  
M H Rider ◽  
A Baquet
Keyword(s):  
Plasma Membrane ◽  
Rat Liver ◽  
Membrane Fraction ◽  
Kinase Activity ◽  
Diacylglycerol Kinase ◽  
Liver Plasma Membrane ◽  
Plasma Membrane Fraction ◽  
In Cells

Plasma-membrane fractions were prepared from the livers of rats injected with 0.15 M-NaCl (controls) or vasopressin (1 nmol/kg body wt.). When assayed in the presence of deoxycholate, vasopressin increased the Vmax. of plasma-membrane diacylglycerol kinase 2-4-fold, and the apparent Km of the enzyme for 1,2-dioleoyl-sn-glycerol was doubled. The effect of vasopressin on the Vmax. of plasma-membrane diacylglycerol kinase was twice as great between pH 7 and 8.5 than at pH 6 or 6.5. Vasopressin doubled the activity of diacylglycerol kinase in the plasma-membrane fraction when the enzyme was assayed with phosphatidylserine rather than deoxycholate as stimulator, and when either 1-stearoyl-2-arachidonoyl-sn-glycerol or 1,2-dioleoyl-sn-glycerol was the substrate. In perfused livers vasopressin (10 nM) increased the Vmax. of plasma-membrane diacylglycerol kinase 2-fold, and phenylephrine (3 microM) gave a similar effect. Vasopressin doubled diacylglycerol kinase activity in hepatocytes that had been preincubated for 55 min, but not in cells that had only been preincubated for 15 min.

scholarly journals Activation of phospholipase C and prostaglandin synthesis by [arginine]vasopressin in cultures

1984 ◽  
Vol 223 (3) ◽  
pp. 855-859 ◽  
Author(s):  
J Pfeilschifter ◽  
A Kurtz ◽  
C Bauer
Keyword(s):  
Arachidonic Acid ◽  
Phosphatidic Acid ◽  
Prostaglandin E2 ◽  
Phospholipase C ◽  
Arginine Vasopressin ◽  
Mesangial Cells ◽  
Significant Loss ◽  
Prostaglandin Synthesis ◽  
Phosphatidylinositol 4 ◽  
In Cells

[Arginine]vasopressin (AVP) stimulates maximal prostaglandin E2 production in cultured rat renal mesangial cells within 2 min. As early as 10s after addition of AVP (10(-6)M) a significant loss of radioactivity from phosphatidylinositol 4,5-bisphosphate but not from phosphatidylinositol 4-phosphate and phosphatidylinositol was observed in cells prelabelled with 32Pi. Cells labelled with [14C]arachidonic acid showed an increase of label in 1,2-diacylglycerol after 15 s and in phosphatidic acid after 30 s upon stimulation with AVP. Pretreatment of the cells with indomethacin (10(-5)M) did not abolish the effect of AVP on the increased labelling of phosphatidic acid.

scholarly journals Evidence from studies employing radioactively labelled fatty acids that the stimulation of flux through the diacylglycerol pool is an early action of vasopressin on hepatocytes

1987 ◽  
Vol 245 (1) ◽  
pp. 211-216 ◽  
Author(s):  
L B Pickford ◽  
A J Polverino ◽  
G J Barritt
Keyword(s):  
Fatty Acids ◽  
Arachidonic Acid ◽  
Phosphatidic Acid ◽  
Isolated Hepatocytes ◽  
Maximal Increase ◽  
Maximal Stimulation ◽  
Early Action ◽  
Palmitic Acids ◽  
Stimulation Of ◽  
In Cells

1. In isolated hepatocytes prelabelled with [14C]-arachidonic, -stearic, -linoleic, -oleic or -palmitic acids, vasopressin increased the amount of radioactivity present in diacylglycerols. The largest increase was observed in cells labelled with arachidonic or stearic acids. 2. In cells prelabelled with [14C]- or [3H]-arachidonic acid, the onset of the increase in radioactivity in diacylglycerols induced by vasopressin was slow, the increase was partly dependent on the presence of extracellular Ca2+, and was associated with an increase in radioactivity present in phosphatidic acid which was more rapid in onset. Vasopressin decreased the amount of [3H]arachidonyl-phosphatidylinositol 4,5-bisphosphate, but the magnitude of this decrease was less than 10% of the observed increase in radioactivity in [3H]arachidonyl-diacylglycerol. 3. The concentration of vasopressin which gave half-maximal increase in [14C]arachidonyl-diacylglycerol at low extracellular Ca2+ was 10-fold higher than that which gave half-maximal stimulation of 45Ca2+ efflux. Phenylephrine, but not glucagon, also increased the amount of [14C]arachidonyl-diacylglycerol. 4. It is concluded that an early action of vasopressin on the liver cell is to increase the flux of carbon from phospholipids, including the phosphoinositides, to diacylglycerols.

scholarly journals Modulation of the Mammalian Target of Rapamycin Pathway by Diacylglycerol Kinase-produced Phosphatidic Acid

2005 ◽  
Vol 280 (11) ◽  
pp. 10091-10099 ◽  
Author(s):  
Antonia Ávila-Flores ◽  
Teresa Santos ◽  
Esther Rincón ◽  
Isabel Mérida
Keyword(s):  
Phosphatidic Acid ◽  
Mammalian Target Of Rapamycin ◽  
Diacylglycerol Kinase ◽  
Target Of Rapamycin

scholarly journals Association of diacylglycerol kinase ζ with protein kinase C α

2003 ◽  
Vol 160 (6) ◽  
pp. 929-937 ◽  
Author(s):  
Bai Luo ◽  
Stephen M. Prescott ◽  
Matthew K. Topham
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Phosphatidic Acid ◽  
Binding Site ◽  
Catalytic Domain ◽  
Diacylglycerol Kinase ◽  
Kinase Substrate ◽  
Signaling Complex ◽  
Kinase C ◽  
Local Accumulation

Activation of PKC depends on the availability of DAG, a signaling lipid that is tightly and dynamically regulated. DAG kinase (DGK) terminates DAG signaling by converting it to phosphatidic acid. Here, we demonstrate that DGKζ inhibits PKCα activity and that DGK activity is required for this inhibition. We also show that DGKζ directly interacts with PKCα in a signaling complex and that the binding site in DGKζ is located within the catalytic domain. Because PKCα can phosphorylate the myristoylated alanine-rich C-kinase substrate (MARCKS) motif of DGKζ, we tested whether this modification could affect their interaction. Phosphorylation of this motif significantly attenuated coimmunoprecipitation of DGKζ and PKCα and abolished their colocalization in cells, indicating that it negatively regulates binding. Expression of a phosphorylation-mimicking DGKζ mutant that was unable to bind PKCα did not inhibit PKCα activity. Together, our results suggest that DGKζ spatially regulates PKCα activity by attenuating local accumulation of signaling DAG. This regulation is impaired by PKCα-mediated DGKζ phosphorylation.

scholarly journals Beyond Lipid Signaling: Pleiotropic Effects of Diacylglycerol Kinases in Cellular Signaling

2020 ◽  
Vol 21 (18) ◽  
pp. 6861
Author(s):  
Jae Ang Sim ◽  
Jaehong Kim ◽  
Dongki Yang
Keyword(s):  
Phosphatidic Acid ◽  
Biological Networks ◽  
Mammalian Cells ◽  
Recent Progress ◽  
Cellular Signaling ◽  
Diacylglycerol Kinase ◽  
Review Article ◽  
Pathological Conditions ◽  
Identification And Characterization

The diacylglycerol kinase family, which can attenuate diacylglycerol signaling and activate phosphatidic acid signaling, regulates various signaling transductions in the mammalian cells. Studies on the regulation of diacylglycerol and phosphatidic acid levels by various enzymes, the identification and characterization of various diacylglycerol and phosphatidic acid-regulated proteins, and the overlap of different diacylglycerol and phosphatidic acid metabolic and signaling processes have revealed the complex and non-redundant roles of diacylglycerol kinases in regulating multiple biochemical and biological networks. In this review article, we summarized recent progress in the complex and non-redundant roles of diacylglycerol kinases, which is expected to aid in restoring dysregulated biochemical and biological networks in various pathological conditions at the bed side.

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