Regulation of Cdc2 activity by phosphorylation at T14/Y15

Prog Cell Cycle Res. 1996;2:99-105. doi: 10.1007/978-1-4615-5873-6_10.

Abstract

The highly conserved Cdc2 serine/threonine kinase plays a central role in cell cycle progression. Although Cdc2 levels remain constant throughout the cell cycle, Cdc2 kinase activity peaks at the G2/M boundary, in order to drive entry into mitosis. In the model organism Schizosaccharomysces pombe, potentially active Cdc2/Cdc13 kinase complex accumulates throughout the S and G2 phases of the cell cycle. This complex, however, is maintained in an active state by Wee1/Mik1-mediated phosphorylation at Y15 (and, possibly, T14). At the G2/M boundary, the Cdc25 protein phosphatase is activated to dephosphorylate the Cdc2/Cdc13 complex, resulting in abrupt activation of Cdc2 kinase activity and entry into mitosis.

Publication types

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

MeSH terms

  • Animals
  • Binding Sites
  • CDC2 Protein Kinase / chemistry
  • CDC2 Protein Kinase / metabolism*
  • Cell Cycle / physiology
  • Cell Cycle Proteins*
  • Cyclin-Dependent Kinases / metabolism
  • Enzyme Activation
  • Humans
  • Nuclear Proteins*
  • Phosphorylation
  • Protein-Tyrosine Kinases / metabolism
  • Schizosaccharomyces / cytology
  • Schizosaccharomyces / enzymology
  • Schizosaccharomyces / genetics
  • Schizosaccharomyces pombe Proteins

Substances

  • Cell Cycle Proteins
  • Nuclear Proteins
  • Schizosaccharomyces pombe Proteins
  • wee1 protein, S pombe
  • Protein-Tyrosine Kinases
  • WEE1 protein, human
  • CDC2 Protein Kinase
  • Cyclin-Dependent Kinases