Role of phospholipase Cε in physiological phosphoinositide signaling networks

Cell Signal. 2012 Jun;24(6):1333-43. doi: 10.1016/j.cellsig.2012.01.009. Epub 2012 Jan 20.


Receptor-initiated phospholipase C activation and generation of IP(3) and DAG are important common triggers for a diversity of signal transduction processes in many cell types. Contributing to this diversity is the existence and differential cellular and subcellular distribution of distinct phospholipase C isoforms with distinct regulatory properties. The recently identified PLCε enzyme is an isoform that is uniquely regulated by multiple upstream signals including ras-family GTP binding proteins as well as heterotrimeric G-proteins. In this review we will consider the well documented biochemical regulation of this isoform in the context of cell and whole animal physiology and in the context of other G protein-regulated PLC isoforms. These studies together reveal a surprisingly wide range of unexpected functions for PLCε in cellular signaling, physiology and disease.

Publication types

  • Research Support, N.I.H., Extramural
  • Review

MeSH terms

  • Animals
  • Humans
  • Inflammation / enzymology
  • Models, Molecular
  • Myocardium / enzymology
  • Neoplasms / enzymology
  • Pancreas / enzymology
  • Phosphatidylinositols / metabolism*
  • Phosphoinositide Phospholipase C / chemistry
  • Phosphoinositide Phospholipase C / metabolism*
  • Protein Isoforms / chemistry
  • Protein Isoforms / metabolism
  • Signal Transduction


  • Phosphatidylinositols
  • Protein Isoforms
  • Phosphoinositide Phospholipase C
  • phospholipase C epsilon