Image from: Proteopedia (2020). An animated image of Phospholipase C Beta illustrating its one chain structure. [image] Available at: https://proteopedia.org/wiki/index.php/2zkm [Accessed 8 Mar. 2020].

Image from: Proteopedia (2020). An animated image of Phospholipase C Beta illustrating its one chain structure. [image] Available at: https://proteopedia.org/wiki/index.php/2zkm [Accessed 8 Mar. 2020].

Phospholipase C is an enzyme responsible for the hydrolisation of phosphatidylinsoditol 4,5-bisphospate (Liao and Carpenter, 2010). Phospholipase C beta is one of the 4 main families as it has a distinctive domain for regulation (Liao and Carpenter, 2010). This domain allows it to respond to specific hormones and elicit a response by producing secondary messenger cascades (Liao and Carpenter, 2010). PLCβ produces diacylglycerol and inositol 4,5-trisphosphate which influence the levels of calcium within the cell and control protein kinase C activity (Liao and Carpenter, 2010). PLCβ has no catalytic activity. Its activation is controlled by a G protein coupled receptor, so the alpha subunit of the GPCR switches GDP for GTP and separates from the beta/gamma subunit (Liao and Carpenter, 2010). Both of these active subunits will go on to activate the phospholipase C beta isoforms for a maximal response within the cell (Liao and Carpenter, 2010).

References: LIAO, H. & CARPENTER, G., 2010. Phospholipase C. Handbook of Cell Signalling. , pp.887-891. Available from: https://www.sciencedirect.com/science/article/pii/B9780123741455001108.