Phospholipase C-gamma as a signal-transducing element

Exp Cell Res. 1999 Nov 25;253(1):15-24. doi: 10.1006/excr.1999.4671.


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.

Publication types

  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Enzyme Activation
  • Fertilization / physiology
  • Isoenzymes / metabolism*
  • Lymphocytes / immunology
  • Phospholipase C gamma
  • Receptor Protein-Tyrosine Kinases / metabolism
  • Receptors, Antigen / metabolism
  • Signal Transduction*
  • Type C Phospholipases / metabolism*


  • Isoenzymes
  • Receptors, Antigen
  • Receptor Protein-Tyrosine Kinases
  • Type C Phospholipases
  • Phospholipase C gamma