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DGKQ  -  diacylglycerol kinase, theta 110kDa

Homo sapiens

Synonyms: DAG kinase theta, DAGK, DAGK4, DAGK7, DGK-theta, ...
 
 
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Disease relevance of DGKQ

  • DAGK with an I110P or I110R mutation in the third transmembrane helix could not be purified because its expression was toxic to the E. coli host, most likely because of severe folding defects [1].
  • The present results show that the DAG kinase inhibitor, R 59022, suppressed tumor cell polarity and strongly inhibited cell locomotion at a concentration of 10(-4), thus supporting the earlier finding that an increased availability of DAGs can suppress the locomotor activity of Walker carcinosarcoma cells [2].
 

High impact information on DGKQ

  • Surprisingly, many commonly available human RhoA constructs contain an uncharacterized mutation that severely reduces binding of RhoA to DAG kinase [3].
  • In one, presynaptic Rho increases acetylcholine (ACh) release by stimulating the accumulation of diacylglycerol (DAG) and the DAG-binding protein UNC-13 at sites of neurotransmitter release; this pathway requires binding of Rho to the DAG kinase DGK-1 [3].
  • Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C [4].
  • Taken together, these data are the first to demonstrate an agonist-induced activity of nuclear DGK-theta activity and a nuclear localization of DGK-delta [5].
  • We may speculate that nuclear speckle-located DGK-theta, on cell stimulation with an agonist, converts to PA the DAG derived from PLCbeta1-dependent PIP(2) hydrolysis [6].
 

Chemical compound and disease context of DGKQ

  • Escherichia coli diacylglycerol kinase (DAGK) is a homotrimeric helical integral membrane protein in which a number of single-site mutations to cysteine are known to promote misfolding [1].
 

Biological context of DGKQ

 

Anatomical context of DGKQ

 

Associations of DGKQ with chemical compounds

  • Nuclear DGK-theta co-localizes with phosphatidylinositol 4,5-bisphosphate (PIP(2)) in domains that correspond to nuclear speckles, as revealed by the use of an antibody to the splicing factor SC-35, a well-established marker for these structures [6].
  • Here, effects of other amino acid replacements have been explored using a folding assay based on the dilution of acidic urea/DAGK stock solutions into detergent/lipid mixed micelles [1].
  • ADH also increased the prostaglandin E (PGE) secretion into serosal medium 3.5-fold and the release of arachidonic acid (AA) from 1,2-DAG, which was intensified in the presence of DAG kinase inhibitor R59022 [12].
  • Phosphatidic acid, a product of DAG kinase, had no effect on TREK-2 [13].
  • DiC8 (1,2-dioctanoyl-sn-glycerol, C8:0, Sigma Chemical Co., St. Louis, MO) induced spreading but only if DAG kinase inhibitor and A-23187 were also present; in their absence cells adhered but did not spread [14].
 

Other interactions of DGKQ

 

Analytical, diagnostic and therapeutic context of DGKQ

  • Immunoprecipitation experiments with an antibody to PLCbeta1 revealed in MDA-MB-453 cells an association between this enzyme and both DGK-theta and phosphatidylinositol phosphate kinase Ialpha (PIPKIalpha) [6].

References

  1. Irreversible misfolding of diacylglycerol kinase is independent of aggregation and occurs prior to trimerization and membrane association. Mi, D., Kim, H.J., Hadziselimovic, A., Sanders, C.R. Biochemistry (2006) [Pubmed]
  2. Shape changes and chemokinesis of Walker carcinosarcoma cells: effects of protein kinase inhibitors (HA-1004, polymyxin B, sangivamycin and tamoxifen) and an inhibitor of diacylglycerol kinase (R 59022). Zimmermann, A., Keller, H. Anticancer Res. (1993) [Pubmed]
  3. Rho is a presynaptic activator of neurotransmitter release at pre-existing synapses in C. elegans. McMullan, R., Hiley, E., Morrison, P., Nurrish, S.J. Genes Dev. (2006) [Pubmed]
  4. Translocation of diacylglycerol kinase theta from cytosol to plasma membrane in response to activation of G protein-coupled receptors and protein kinase C. van Baal, J., de Widt, J., Divecha, N., van Blitterswijk, W.J. J. Biol. Chem. (2005) [Pubmed]
  5. Nuclear diacylglycerol kinase-theta is activated in response to alpha-thrombin. Bregoli, L., Baldassare, J.J., Raben, D.M. J. Biol. Chem. (2001) [Pubmed]
  6. Diacylglycerol kinase-theta is localized in the speckle domains of the nucleus. Tabellini, G., Bortul, R., Santi, S., Riccio, M., Baldini, G., Cappellini, A., Billi, A.M., Berezney, R., Ruggeri, A., Cocco, L., Martelli, A.M. Exp. Cell Res. (2003) [Pubmed]
  7. Assignment of the human diacylglycerol kinase 4 (DAGK4) gene to chromosome 4p16.3. Endele, S., Zabel, B., Winterpacht, A. Genomics (1996) [Pubmed]
  8. Structure-activity relationship of diacylglycerol kinase theta. Los, A.P., van Baal, J., de Widt, J., Divecha, N., van Blitterswijk, W.J. Biochim. Biophys. Acta (2004) [Pubmed]
  9. TGF-beta signaling in A549 lung carcinoma cells: lipid second messengers. Ignotz, R.A., Honeyman, T. J. Cell. Biochem. (2000) [Pubmed]
  10. Insulin promotes diacylglycerol kinase activation by different mechanisms in rat cerebral cortex synaptosomes. Zulian, S.E., Ilincheta de Boschero, M.G., Giusto, N.M. J. Neurosci. Res. (2006) [Pubmed]
  11. A diacylglycerol kinase is involved in the regulation of interleukin-2 synthesis in Jurkat T cells. Aussel, C., Pelassy, C., Breittmayer, J.P. Cell. Immunol. (1992) [Pubmed]
  12. ADH-dependent phosphoinositide signalling system and prostaglandin E production in the frog urinary bladder. Parnova, R.G., Firsov, D.L. Cell. Signal. (1991) [Pubmed]
  13. Mechanism of inhibition of TREK-2 (K2P10.1) by the Gq-coupled M3 muscarinic receptor. Kang, D., Han, J., Kim, D. Am. J. Physiol., Cell Physiol. (2006) [Pubmed]
  14. Two-step mechanism for actin polymerization in human erythroleukemia cells induced by phorbol ester. Niu, M.Y., Nachmias, V.T. Cell Motil. Cytoskeleton (1994) [Pubmed]
  15. Molecules in focus: diacylglycerol kinase. Sakane, F., Kanoh, H. Int. J. Biochem. Cell Biol. (1997) [Pubmed]
  16. Analysis of a novel diacylglycerol kinase from Dictyostelium discoideum: DGKA. Ostroski, M., Tu-Sekine, B., Raben, D.M. Biochemistry (2005) [Pubmed]
 
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