MAP kinase and the activation of quiescent cells

Curr Opin Cell Biol. 1993 Apr;5(2):207-13. doi: 10.1016/0955-0674(93)90104-x.

Abstract

Virtually all mitogens lead to the rapid activation of one or more mitogen-activated protein (MAP) kinases. In almost all cases, mitogen-activated surface signaling complexes transmit an essential signal via ras on to a protein kinase cascade that involves the serine/threonine kinase raf. Raf appears to be a MAP kinase kinase kinase, activating MAP kinase kinase which, in turn, activates MAP kinase. Among the targets of MAP kinase are other kinases, nuclear transcription factors and other proteins with roles in cell cycle activation. Both G0-arrested somatic cells and G2-arrested oocytes use many of the same signaling mechanisms to break cell cycle arrest; this is a useful concept in light of newly developed cell-free systems from quiescent oocytes that can be used to study signal transduction in vitro.

Publication types

  • Comparative Study
  • Review

MeSH terms

  • Animals
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Cell Cycle*
  • Enzyme Activation
  • Female
  • Oocytes
  • Phospholipases A
  • Protein Kinases*
  • Yeasts

Substances

  • Protein Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Phospholipases A