Cdc2 protein kinase is complexed with both cyclin A and B: evidence for proteolytic inactivation of MPF

G Draetta1, F Luca, J Westendorf

  • 1Cold Spring Harbor Laboratory, New York 11724.

Cell
|March 10, 1989
PubMed

Insights

Clam oocytes and embryos contain cdc2 protein kinase associated with cyclins A and B. Cyclin proteolysis inactivates the M phase promoting factor (MPF), enabling exit from mitosis.

Area of Science:

  • Cell Biology
  • Molecular Biology
  • Developmental Biology

Background:

  • Cyclins A and B in Spisula clams undergo degradation post-mitosis.
  • cdc2 protein kinase is a key regulator of cell cycle progression.

Purpose of the Study:

  • To investigate the role of cdc2 protein kinase and its association with cyclins in clam mitosis.
  • To elucidate the mechanism of M phase promoting factor (MPF) regulation in clam oocytes and embryos.

Main Methods:

  • Biochemical analysis of cdc2 protein kinase and cyclin interactions.
  • Assay of histone H1 kinase activity in cell cycle-dependent complexes.
  • Use of p13suc1-Sepharose and immunoprecipitation techniques.

Main Results:

  • Clam oocytes and embryos possess cdc2 protein kinase activity.
  • Clam cdc2 associates with both cyclin A and cyclin B, forming distinct complexes.
  • These complexes exhibit cell cycle-dependent histone H1 kinase activity.

Conclusions:

  • Cyclins A and B are integral components of the clam M phase promoting factor (MPF).
  • Proteolytic degradation of cyclins is the likely mechanism for MPF inactivation.
  • This process facilitates the exit from mitosis in clam oocytes and embryos.

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