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Exp Cell Res. 1999 Nov 25;253(1):15-24.

Phospholipase C-gamma as a signal-transducing element.

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Department of Biochemistry, Vanderbilt University School of Medicine, Nashville, Tennessee, 37232-0146, USA.


A ubiquitous signaling event in hormonal responses is the phospholipase C (PLC)-catalyzed hydrolysis of phosphatidylinositol 4, 5-bisphosphate to produce the metabolite second messenger molecules inositol 1,4,5-trisphosphate and diacylglycerol. The former provokes a transient increase in intracellular free Ca(2+), while the latter serves as a direct activator of protein kinase C. In tyrosine kinase-dependent signaling pathways this reaction is mediated by the PLC-gamma isozymes. These are direct substrates of many tyrosine kinases in a wide variety of cell types. The mechanism of PLC-gamma activation involves its association with and phosphorylation by receptor and non-receptor tyrosine kinases, as well as interaction with specialized adaptor molecules and, perhaps, other second messenger molecules. However, the biochemistry of PLC-gamma is at a more advanced state than a clear understanding of exactly how this signaling element functions in the generation of a mitogenic response.

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