Chapter

Progress in Cell Cycle Research

Part of the series Progress in Cell Cycle Research pp 99-105

Regulation of Cdc2 activity by phosphorylation at T14/Y15

  • Lynne D. BerryAffiliated withHoward Hughes Medical Institute, Department of Cell Biology, Vanderbilt University
  • , Kathleen L. GouldAffiliated withHoward Hughes Medical Institute, Department of Cell Biology, Vanderbilt University

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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 Schizosaccharotnysces 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 inactive state by Weel/Mik1-mediated phosphorylation at Y15 (and, possibly, T14). At the G2/M boundary, the Cdc25 protein phosphatase is activated to dephosphorylate the Cdc2/Cdcl3 complex, resulting in abrupt activation of Cdc2 kinase activity and entry into mitosis.