1601313

11637

A large number of extracellular signals stimulate hydrolysis of phosphatidylinositol 4,5-bisphosphate by phosphoinositide-specific phospholipase C (PI-PLC). PI-PLC isozymes have been found in a broad spectrum of organisms and although they have common catalytic properties, their regulation involves different signalling pathways. A number of recent studies provided an insight into domain organisation of PI-PLC isozymes and contributed towards better understanding of the structural basis for catalysis, cellular localisation and molecular changes that could underlie the process of their activation.

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EF hand domain , SH2 domain , 5-bisphosphate , G-protein , Phosphatidylinositol 4 , catalysis , 4 , phosphatidylinositol 3-kinase , 4 , Phospholipase C-L , inositol 1 , Phospholipase C-Q , Phospholipase C-N , pH domain , 5-trisphosphate , 5-trisphosphate , Phosphatidylinositol 3 , tyrosine kinase , Phosphoinositide-speci¢c phospholipase C , SH3 domain , C2 domain

Studia Iranica

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