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Cleavage sites of phospholipases. Phospholipase C enzymes cut just before the phosphate attached to the R3 moiety.

Phospholipase C is a class of enzymes that cleave phospholipids just before the phosphate group (see figure). It is most commonly taken to be synonymous with the human forms of this enzyme, which plays an important role in eukaryotic cell physiology, in particular signal transduction pathways. Thirteen kinds of mammalian phospholipase C are classified into six models (β, γ, δ, ε, ζ, η) according to structure.

Human variant

The human variant has EC


Receptors that activate this pathway are mainly G protein-coupled receptors coupled to the Gαq subunit, including:

Other, minor, activators than Gαq are:


PLC cleaves a phospholipid. In the process, phosphatidylinositol 4,5-bisphosphate (PIP2) is cleaved into diacyl glycerol (DAG) and inositol 1,4,5-trisphosphate (IP3). DAG remains bound to the membrane, and IP3 is released as a soluble structure into the cytosol. IP3 then diffuses through the cytosol to bind to IP3 receptors, particular calcium channels in the endoplasmic reticulum (ER). This causes the cytosolic concentration of calcium to increase, causing a cascade of intracellular changes and activity.[4] In addition, calcium and DAG together work to activate protein kinase C, which goes on to phosphorylate other molecules, leading to altered cellular activity.[4] End effects include taste, tumor promotion, etc.[4]

Further information: Calcium function in vertebrates, Function of protein kinase C


  1. 1.0 1.1 1.2 1.3 1.4 Gq alpha subunit. Wikipedia. URL accessed on 2009-03-03.
  2. 2.0 2.1 Walter F., PhD. Boron (2003). Medical Physiology: A Cellular And Molecular Approaoch, 1300, Elsevier/Saunders. Page 104
  3. GeneGlobe -> GHRH Signaling Retrieved on May 31, 2009
  4. 4.0 4.1 4.2 Alberts B, Lewis J, Raff M, Roberts K, Walter P (2002). Molecular biology of the cell, 4th, New York: Garland Science.

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