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
Species
Homo sapiens
Compartment
Locations in the PathwayBrowser
Summation

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
8454637 Cloning, sequencing, purification, and Gq-dependent activation of phospholipase C-beta 3

Jhon, DY, Lee, HH, Park, D, Lee, CW, Lee, KH, Yoo, OJ, Rhee, SG

J Biol Chem 1993
8530101 cDNA sequence and gene locus of the human retinal phosphoinositide-specific phospholipase-C beta 4 (PLCB4)

Alvarez, RA, Ghalayini, AJ, Xu, P, Hardcastle, A, Bhattacharya, S, Rao, PN, Pettenati, MJ, Anderson, RE, Baehr, W

Genomics 1995
15790568 The role of EF-hand domains and C2 domain in regulation of enzymatic activity of phospholipase Czeta

Kouchi, Z, Shikano, T, Nakamura, Y, Shirakawa, H, Fukami, K, Miyazaki, S

J Biol Chem 2005
11118617 Cloning and characterization of the human phosphoinositide-specific phospholipase C-beta 1 (PLC beta 1)

Caricasole, A, Sala, C, Roncarati, R, Formenti, E, Terstappen, GC

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, Park, DJ, Lee, KH, Kim, CG, Rhee, SG

J Biol Chem 1993
15579586 Phospholipase Czeta causes Ca2+ oscillations and parthenogenetic activation of human oocytes

Rogers, NT, Hobson, E, Pickering, S, Lai, FA, Braude, P, Swann, K

Reproduction 2004
1644792 Cloning, sequencing, expression, and Gq-independent activation of phospholipase C-beta 2

Park, D, Jhon, DY, Kriz, R, Knopf, J, Rhee, SG

J Biol Chem 1992
Participants
Participant Of
Catalyst Activity
Catalyst Activity
Title
phosphatidylinositol phospholipase C activity of PLCbz [cytosol]
Physical Entity
Activity
Orthologous Events
Authored