Reactome | PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by cytosolic PLC[2] at the plasma membrane

PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by cytosolic PLC[2] at the plasma membrane

Stable Identifier

R-HSA-1855177

Type

Reaction [transition]

Species

Homo sapiens

Compartment

cytosol, plasma membrane

ReviewStatus

5/5

Locations in the PathwayBrowser

Expand all

General

SBML | | PDF

SVG | | PPTX | SBGN

PI(4,5)P2 is hydrolysed to I(1,4,5)P3 and DAG by cytosolic PLC[2] at the plasma membrane

Click the image above or here to open this reaction in the Pathway Browser
The layout of this reaction may differ from that in the pathway view due to the constraints in pathway layout

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).

Literature References

PubMed ID	Title	Journal	Year
8530101	cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4) Alvarez, RA, Rao, PN, Anderson, RE, Pettenati, MJ, Hardcastle, A, Baehr, W, Bhattacharya, S, Xu, P, Ghalayini, AJ	Genomics	1995
8454637	Cloning, sequencing, purification, and Gq-dependent activation of phospholipase C-beta 3 Lee, CW, Park, D, Rhee, SG, Lee, HH, Jhon, DY, Yoo, OJ, Lee, KH	J Biol Chem	1993
15790568	The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta Fukami, K, Miyazaki, S, Shikano, T, Kouchi, Z, Shirakawa, H, Nakamura, Y	J Biol Chem	2005
11118617	Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1) Sala, C, Caricasole, A, Terstappen, GC, Roncarati, R, Formenti, E	Biochim Biophys Acta	2000
1333955	Identification, purification and characterization of a novel phosphatidylinositol-specific phospholipase C, a third member of the beta subfamily Carozzi, AJ, Kriz, RW, Webster, C, Parker, PJ	Eur J Biochem	1992
8407970	Purification, molecular cloning, and sequencing of phospholipase C-beta 4 Lee, CW, Rhee, SG, Kim, CG, Lee, KH, Park, DJ	J Biol Chem	1993
15579586	Phospholipase Czeta causes Ca2+ oscillations and parthenogenetic activation of human oocytes Hobson, E, Swann, K, Braude, P, Lai, FA, Rogers, NT, Pickering, S	Reproduction	2004
1644792	Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2 Park, D, Rhee, SG, Jhon, DY, Kriz, R, Knopf, J	J Biol Chem	1992