Phosphorylation of DGK

Diacylglycerol (DAG) and phosphatidic acid (PtdOH) play important roles in a variety of signaling cascades (Carrasco and Merida, 2007; Stace and Ktistakis, 2006). Therefore, the physiological roles and regulatory mechanisms controlling the levels of these lipids are important. One class of enzymes capable of coordinating the levels of these two lipids are the diacylglycerol kinases (DGKs). DGKs catalyze the transfer of the γ-phosphate of ATP to the hydroxyl group of DAG which generates PtdOH(Merida et al., 2008; Sakane et al., 2007). As DGKs reciprocally modulate the relative levels of these two signaling lipids, it is not surprising that there is increasing interest in understanding the mechanism underlying the catalysis and regulation of these kinases. While post-translational modifications (PTMs) are often involved in enzyme regulation, there is surprisingly little information regarding the PTMs on these enzymes and their roles in modulating their activity and function. In this review, we will summarize what is known about one PTM on DGKs, phosphorylation, and the possible functions of this modification.