PLC-beta hydrolyses PIP2 to DAG and IP3

Stable Identifier
Reaction [transition]
Homo sapiens
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Phospholipase C (PLC) isozymes are a group of related proteins that cleave the polar head group from inositol phospholipids, typically in response to signals from cell surface receptors. They hydrolyze the highly phosphorylated lipid phosphatidylinositol 4,5-bisphosphate (PIP2) generating two products: inositol 1,4,5-trisphosphate (IP3), a universal calcium-mobilizing second messenger, and diacylglycerol (DAG), an activator of protein kinase C. PLC-beta isoforms are regulated by heterotrimeric GTP-binding proteins. PLC-beta 1 and 3 are widely expressed, with the highest concentrations found in (differing) specific regions of the brain. PLC-beta 2 is expressed at highest levels in cells of hematopoeitic origin; it is involved in leukocyte signaling and host defense. PLC-beta 4 is highly concentrated in cerebellar Purkinje and granule cells, the median geniculate body, whose axons terminate in the auditory cortex, and the lateral geniculate nucleus, where most retinal axons terminate in a visuotopic representation of each half of the visual field.

Literature References
PubMed ID Title Journal Year
11015615 Structure, function, and control of phosphoinositide-specific phospholipase C

Rebecchi, MJ, Pentyala, SN

Physiol Rev 2000
2841328 Purification and characterization of membrane-bound phospholipase C specific for phosphoinositides from human platelets

Banno, Y, Yada, Y, Nozawa, Y

J Biol Chem 1988
Participant Of
Catalyst Activity
Catalyst Activity
phospholipase C activity of PLC beta:G alpha (q/11) [plasma membrane]
Physical Entity
Orthologous Events
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