Cell signalling through guanine-nucleotide-binding regulatory proteins (G proteins) and phospholipases

Eur J Biochem. 1997 Jan 15;243(1-2):10-20. doi: 10.1111/j.1432-1033.1997.t01-1-00010.x.

Abstract

Phospholipases are important enzymes in cell signal transduction since they hydrolyze membrane phospholipids to generate signalling molecules. Heterotrimeric guanine-nucleotide-binding regulatory proteins (G proteins) play a major role in their regulation by a variety of agonists that activate receptors with seven membrane-spanning domains. Phospholipases of the C type, which hydrolyze inositol phospholipids to yield inositol trisphosphate and diacylglycerol, are regulated by the alpha and betagamma subunits of certain heterotrimeric G proteins as well as by receptor-associated and non-receptor-associated tyrosine kinases. Phospholipases of the D type, which hydrolyze phosphatidylcholine to phosphatidic acid, are regulated by members of the ADP-ribosylation factor and Rho subfamilies of small G proteins, and by protein kinase C and other factors. This review presents recent information concerning the molecular details of G protein regulation of these phospholipases.

Publication types

  • Review

MeSH terms

  • ADP-Ribosylation Factors
  • Animals
  • Enzyme Activation
  • GTP-Binding Proteins / physiology*
  • Humans
  • Isoenzymes / physiology
  • Phospholipases / physiology*
  • Protein Kinase C / physiology
  • Receptors, Cell Surface / physiology
  • Signal Transduction*
  • rac GTP-Binding Proteins
  • rho GTP-Binding Proteins

Substances

  • Isoenzymes
  • Receptors, Cell Surface
  • Protein Kinase C
  • Phospholipases
  • GTP-Binding Proteins
  • ADP-Ribosylation Factors
  • rac GTP-Binding Proteins
  • rho GTP-Binding Proteins