Specificity of receptor tyrosine kinase signaling: transient versus sustained extracellular signal-regulated kinase activation

Cell. 1995 Jan 27;80(2):179-85. doi: 10.1016/0092-8674(95)90401-8.

Abstract

A number of different intracellular signaling pathways have been shown to be activated by receptor tyrosine kinases. These activation events include the phosphoinositide 3-kinase, 70 kDa S6 kinase, mitogen-activated protein kinase (MAPK), phospholipase C-gamma, and the Jak/STAT pathways. The precise role of each of these pathways in cell signaling remains to be resolved, but studies on the differentiation of mammalian PC12 cells in tissue culture and the genetics of cell fate determination in Drosophila and Caenorhabditis suggest that the extracellular signal-regulated kinase (ERK-regulated) MAPK pathway may be sufficient for these cellular responses. Experiments with PC12 cells also suggest that the duration of ERK activation is critical for cell signaling decisions.

Publication types

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

MeSH terms

  • Animals
  • Caenorhabditis
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Drosophila
  • Enzyme Activation
  • Humans
  • Mitogen-Activated Protein Kinase Kinases
  • PC12 Cells
  • Phosphatidylinositol 3-Kinases
  • Phosphotransferases (Alcohol Group Acceptor) / metabolism
  • Protein Kinases / metabolism
  • Protein-Serine-Threonine Kinases / metabolism
  • Protein-Tyrosine Kinases / metabolism
  • Rats
  • Receptor Protein-Tyrosine Kinases / metabolism*
  • Ribosomal Protein S6 Kinases
  • Signal Transduction*
  • Substrate Specificity
  • Type C Phospholipases / metabolism

Substances

  • Protein Kinases
  • Phosphatidylinositol 3-Kinases
  • Phosphotransferases (Alcohol Group Acceptor)
  • Protein-Tyrosine Kinases
  • Receptor Protein-Tyrosine Kinases
  • Protein-Serine-Threonine Kinases
  • Ribosomal Protein S6 Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Mitogen-Activated Protein Kinase Kinases
  • Type C Phospholipases