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spinqualitylabelsall models Structure of phosphatidylinositol-specific phospholipase C complex with myo-inositol (PDB code 1ptg). Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Function Phospholipase C (PLC) cleaves phospholipids before the phosphate group. Phospholipase C β,γ,δ,ε catalyze the conversion of phosphatidylinositol 4,5-bisphosphate to inositol 1,4,5-trisphosphate and diacylglycerol.[1] For more details on phospholipase C β see PLC beta 3 Gq. Phosphatidylinositol-specific phospholipase C (PIPLC) catalyzes the hydrolysis of phosphatidylinositol into inositol triphosphate and deacylglycerol. PIPLC functions at the plasma membrane. PIPLC can release phosphatidylinositol-linked proteins (i.e., acetylcholinesterase) from the membrane by enzymatically cleaving their GPI anchor. [2] Disease Phospholipase C γ gene blocking can stop breast cancer.[3] Phospholipase C δ has important suppressive role in the development and progression of esophageal carcinoma. Structural highlights The active site of PIPLC is located at a solvent-accessible cleft at the C-terminal.[4]

3D structures of phosphatidylinositol-specific phospholipase C

Updated on 10-January-2016

References

1. ↑ Barr AJ, Marjoram R, Xu J, Snyderman R. Phospholipase C-beta 2 interacts with mitogen-activated protein kinase kinase 3. Biochem Biophys Res Commun. 2002 Apr 26;293(1):647-52. PMID:12054652 doi:http://dx.doi.org/10.1016/S0006-291X(02)00259-0
2. ↑ Mortara RA, Minelli LM, Vandekerckhove F, Nussenzweig V, Ramalho-Pinto FJ. Phosphatidylinositol-specific phospholipase C (PI-PLC) cleavage of GPI-anchored surface molecules of Trypanosoma cruzi triggers in vitro morphological reorganization of trypomastigotes. J Eukaryot Microbiol. 2001 Jan-Feb;48(1):27-37. PMID:11249190
3. ↑ Sala G, Dituri F, Raimondi C, Previdi S, Maffucci T, Mazzoletti M, Rossi C, Iezzi M, Lattanzio R, Piantelli M, Iacobelli S, Broggini M, Falasca M. Phospholipase Cgamma1 is required for metastasis development and progression. Cancer Res. 2008 Dec 15;68(24):10187-96. doi: 10.1158/0008-5472.CAN-08-1181. PMID:19074886 doi:http://dx.doi.org/10.1158/0008-5472.CAN-08-1181
4. ↑ Heinz DW, Ryan M, Bullock TL, Griffith OH. Crystal structure of the phosphatidylinositol-specific phospholipase C from Bacillus cereus in complex with myo-inositol. EMBO J. 1995 Aug 15;14(16):3855-63. PMID:7664726