At the plasma membrane, a group of phospholipase C (“PLC(bz))” proteins hydrolyse phosphatidylinositol 4,5 bisphosphate (PI(4,5)P2) to inositol 1,4,5 trisphosphate (I(1,4,5)P3) and diacylglycerol (DAG). This group of phospholipase C proteins lack a PH domain and so are is cytosolic. Their C2 domains bind to PI(4,5)P2 at the membrane. The PLC-beta proteins are thought to be responsible for the majority of PI(4,5)P2 hydrolysis.The phospholipase C isoforms involved and their corresponding literature references are: phosphoinositide phospholipase C beta-1 (PLCB1) (Caricasole et al. 2000, Jhon et al. 1993, Park et al. 1992); beta-2 (PLCB2) (Jhon et al. 1993, Park et al. 1992); beta-3 (PLCB3) (Carozzi et al. 1992, Jhon et al. 1993); beta-4 (PLCB4) (Alvarez et al. 1995, Lee et al. 1993); and zeta-1 (PLCZ1) (Kouchi et al. 2005, Rogers et al. 2004).
Alvarez, RA, Rao, PN, Anderson, RE, Pettenati, MJ, Hardcastle, A, Baehr, W, Bhattacharya, S, Xu, P, Ghalayini, AJ
Lee, CW, Park, D, Rhee, SG, Lee, HH, Jhon, DY, Yoo, OJ, Lee, KH
Fukami, K, Miyazaki, S, Shikano, T, Kouchi, Z, Shirakawa, H, Nakamura, Y
Sala, C, Caricasole, A, Terstappen, GC, Roncarati, R, Formenti, E
Carozzi, AJ, Kriz, RW, Webster, C, Parker, PJ
Lee, CW, Rhee, SG, Kim, CG, Lee, KH, Park, DJ
Hobson, E, Swann, K, Braude, P, Lai, FA, Rogers, NT, Pickering, S
Park, D, Rhee, SG, Jhon, DY, Kriz, R, Knopf, J
phosphatidylinositol phospholipase C activity of PLCbz [cytosol]
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