Phosphoinositide-specific phospholipase C C

Unless otherwise stated all data on this page refer to the human proteins. Gene information is provided for human (Hs), mouse (Mm) and rat (Rn).

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Phosphoinositide-specific phospholipase C (PLC, EC, catalyses the hydrolysis of PIP2 to IP3 and 1,2-diacylglycerol, each of which have major second messenger functions. Two domains, X and Y, essential for catalytic activity, are conserved in the different forms of PLC. Isoforms of PLC-β are activated primarily by G protein-coupled receptors through members of the Gq/11 family of G proteins. The receptor-mediated activation of PLC-γ involves their phosphorylation by receptor tyrosine kinases (RTK) in response to activation of a variety of growth factor receptors and immune system receptors. PLC-ε1 may represent a point of convergence of signalling via both G protein-coupled and catalytic receptors. Ca2+ ions are required for catalytic activity of PLC isoforms and have been suggested to be the major physiological form of regulation of PLC-δ activity. PLC has been suggested to be activated non-selectively by the small molecule m3M3FBS [2], although this mechanism of action has been questioned [12]. The aminosteroid U73122 has been described as an inhibitor of phosphoinositide-specific PLC [21], although its selectivity among the isoforms is untested and it has been reported to occupy the H1 histamine receptor [8].


PLCβ1 C Show summary »

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PLCβ3 C Show summary »

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PLCγ1 C Show summary » More detailed page

PLCγ2 C Show summary » More detailed page

PLCδ1 C Show summary »

PLCδ3 C Show summary »

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PLCε1 C Show summary »

PLCζ1 C Show summary »

PLCη1 C Show summary »

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How to cite this family page

Database page citation:

Phosphoinositide-specific phospholipase C. Accessed on 23/11/2017. IUPHAR/BPS Guide to PHARMACOLOGY,

Concise Guide to PHARMACOLOGY citation:

Alexander SPH, Fabbro D, Kelly E, Marrion N, Peters JA, Benson HE, Faccenda E, Pawson AJ, Sharman JL, Southan C, Davies JA and CGTP Collaborators (2015) The Concise Guide to PHARMACOLOGY 2015/16: Enzymes. Br J Pharmacol. 172: 6024-6109.