Families of phosphoinositide-specific phospholipase C: structure and function.
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.
Katan
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CRC Centre for Cell and Molecular Biology, Chester Beatty Laboratories, Fulham Road, London SW3 6JB, UK. matilda@icr.ac.uk
D000818:Animals; D006868:Hydrolysis; D007527:Isoenzymes / Q000737:chemistry* / Q000378:metabolism*; D008958:Models, Molecular; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000378:metabolism*; D054801:Phosphoinositide Phospholipase C; D054799:Phospholipase C beta; D051966:Phospholipase C gamma; D010727:Phosphoric Diester Hydrolases / Q000737:chemistry / Q000378:metabolism; D010738:Type C Phospholipases / Q000737:chemistry* / Q000378:metabolism*
D007527:Isoenzymes; D010716:Phosphatidylinositols; D010727:Phosphoric Diester Hydrolases; D010738:Type C Phospholipases; D054801:Phosphoinositide Phospholipase C; D054799:Phospholipase C beta; D051966:Phospholipase C gamma; D043265:Phosphatidylinositol Diacylglycerol-Lyase