Regulation of p34cdc2 protein kinase during mitosis

Cell. 1989 Jul 28;58(2):361-72. doi: 10.1016/0092-8674(89)90850-7.


The cell-cycle timing of mitosis in fission yeast is determined by the cdc25+ gene product activating the p34cdc2 protein kinase leading to mitotic initiation. Protein kinase activity remains high in metaphase and then declines during anaphase. Activation of the protein kinase also requires the cyclin homolog p56cdc13, which also functions post activation at a later stage of mitosis. The continuing function of p56cdc13 during mitosis is consistent with its high level until the metaphase/anaphase transition. At anaphase the p56cdc13 level falls dramatically just before the decline in p34cdc2 protein kinase activity. The behavior of p56cdc13 is similar to that observed for cyclins in oocytes. p13suc1 interacts closely with p34cdc2; it is required during the process of mitosis and may play a role in the inactivation of the p34cdc2 protein kinase. Therefore, the cdc25+, cdc13+, and suc1+ gene products are important for regulating p34cdc2 protein kinase activity during entry into, progress through, and exit from mitosis.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • CDC2 Protein Kinase
  • Cell Cycle Proteins*
  • Eukaryotic Cells / cytology
  • Eukaryotic Cells / enzymology
  • Fungal Proteins / genetics
  • Fungal Proteins / metabolism
  • Fungal Proteins / physiology
  • Gene Expression Regulation
  • Genes, Regulator
  • Mitosis*
  • Phosphoproteins / analysis
  • Phosphoproteins / genetics*
  • Phosphoproteins / metabolism
  • Schizosaccharomyces
  • Schizosaccharomyces pombe Proteins*
  • ras-GRF1*


  • Cell Cycle Proteins
  • Fungal Proteins
  • Phosphoproteins
  • Schizosaccharomyces pombe Proteins
  • Suc1 protein, S pombe
  • ras-GRF1
  • CDC2 Protein Kinase