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- W2583752212 abstract "Diacylglycerol kinases are expressed in all multicellular organisms that have been studied. Their structural diversity and complexity indicate that they are functionally important in a variety of cellular signaling events. Since they can affect both DAG and PA signals, DGK activity plays a central role in many lipid signaling pathways. Many signaling cascades are initiated by phospholipase C (PLC) isozymes. One product of this reaction is diacylglycerol (DAG), a prolific sencond messenger that activates proteins involved in a variety signaling cascades. The protein kinase Cs (PKCs) are the best-characterized DAG-activated proteins, but diacylglycerol also activates other proteins, including RasGRP and two guanine nucleotide exchange factors (GEFs), CalDAG GEFs I and III. The chimaerins, which are GTPase-activating proteins (GAPs) for Rac, and the Unc-13 gene product from Caenorhabditis elegans also bind to DAG. Because it can associate with a diverse set of proteins, DAG potentially activates numerous signaling cascades. Thus, its accumulation needs to be strictly regulated. Diacylglycerol kinases (DGKs), which phosphorylate DAG, are widely considered to be responsible for terminating diacylglycerol signaling [2,3]. But the product of the DGK reaction, phosphatidic acid (PA), also can be a signal: it can activate phosphatidylinositol 4-phosphate 5-kinases and PKCσ, participates in recruiting Raf1 to the plasma membrane, and is involved in vesicle trafficking. Because they manipulate both DAG and PA signaling, the DGKs can reulate numerous signaling events." @default.
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- W2583752212 date "2003-01-01" @default.
- W2583752212 modified "2023-10-16" @default.
- W2583752212 title "Diacylglycerol Kinases" @default.
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- W2583752212 doi "https://doi.org/10.1016/b978-012124546-7/50523-4" @default.
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