Families of phosphoinositide-specific phospholipase C: structure and function

Biochim Biophys Acta. 1998 Dec 8;1436(1-2):5-17. doi: 10.1016/s0005-2760(98)00125-8.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Animals
  • Hydrolysis
  • Isoenzymes / chemistry*
  • Isoenzymes / metabolism*
  • Models, Molecular
  • Phosphatidylinositol Diacylglycerol-Lyase
  • Phosphatidylinositols / metabolism*
  • Phosphoinositide Phospholipase C
  • Phospholipase C beta
  • Phospholipase C gamma
  • Phosphoric Diester Hydrolases / chemistry
  • Phosphoric Diester Hydrolases / metabolism
  • Type C Phospholipases / chemistry*
  • Type C Phospholipases / metabolism*

Substances

  • Isoenzymes
  • Phosphatidylinositols
  • Phosphoric Diester Hydrolases
  • Type C Phospholipases
  • Phosphoinositide Phospholipase C
  • Phospholipase C beta
  • Phospholipase C gamma
  • Phosphatidylinositol Diacylglycerol-Lyase