Historical Background
Diacylglycerol kinase (DGK) is the enzyme which phosphorylates diacylglycerol (DG) to produce phosphatidic acid (PA) (Goto et al. 2007). Its enzymatic activity was first described in cabbage a half century ago by Hokin and Hokin (1959). Since their report, DGK activity has been found widely in many animal species. The substrate of DGK, DG, is a lipid derived from various sources, including phosphatidylinositol 4, 5-bisphosphate by the action of phospholipase C (PLC), phosphatidylcholine by phospholipase D (PLD), monoacylglycerol (MG) by acyltransferase, and triglyceride (TG) by TG lipase. DGs from different sources have distinct acyl chain composition. At least 50 distinct molecular species of DG have been identified. In the mid-1980s, the biological significance of sn-1,2-DG was highlighted: It is an allosteric activator of protein kinase C (PKC). The PKC family comprises of three classes (conventional, novel, and atypical). Of...
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Nakano, T., Goto, K. (2018). Diacylglycerol Kinase. In: Choi, S. (eds) Encyclopedia of Signaling Molecules. Springer, Cham. https://doi.org/10.1007/978-3-319-67199-4_101585
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DOI: https://doi.org/10.1007/978-3-319-67199-4_101585
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