4.6.1.13	malfunction	with PLC2 and PLC6, RNAi phenotypes show strong defects in release of GPI-anchored surface proteins in vivo	-, 708374	
4.6.1.13	metabolism	the enzyme is implicated in direct regulation of lipid biosynthesis	729728	
4.6.1.13	additional information	the enzyme can form a dimer via helix B, a structural feature present in all secreted, bacterial phosphatidylinositol-specific phospholipases C that is important for membrane binding. The small interface is critical for optimal enzyme activity. The enzyme dimerization is enhanced in membranes containing phosphatidylcholine, the zwitterionic phospholipid acts not by specific binding to the protein, but rather by reducing anionic lipid interactions with a cationic pocket on the surface of the enzyme that stabilizes monomeric protein. Staphylococcus aureus phosphatidylinositol-specific phospholipase C appears to have a unique mechanism where enzyme activity is modulated by competition between binding of soluble anions or anionic lipids to the cationic sensor and transient dimerization on the membrane	730001	
4.6.1.13	physiological function	acute incubation of Cos-7 cells for 1 h with PI-PLC significantly reduces the amount of cell-surface expression, both of 5'-nucleotidase by 31.9% and of expressed alpha2delta-2 by 49.4%. PI-PLC treatment reduces calcium current density when alpha2delta subunits are coexpressed. PI-PLC treatment of hippocampal lysates reduces the detergent-resistant membrane association of alpha2delta-1 from 68.3% to 8.3%, and also resultes in recovery of alpha2-1 in the aqueous phase after Triton X-114 separation. Incubation of cultured dorsal root-ganglion neurons for 60 min with PI-PLC substantially reduces cell surface alpha2delta-1 immunofluorescence. It does not reduce that for the transmembrane p75 nerve growth-factor receptor	710429	
4.6.1.13	physiological function	for highly anionic membranes, but not phosphatidylcholine-rich vesicles, binding correlates well with relative activity	707504	
4.6.1.13	physiological function	PI-PLC pathway is involved in the stimulatory effect of heme on (Na+ + K+)ATPase via PKC-like activation	708443	
4.6.1.13	physiological function	the enzyme is a virulence factor	-, 729893	
4.6.1.13	physiological function	the enzyme is a virulence factor in the pathogenicity of Staphylococcus aureus	730001