Cdc2 Protein Kinase: Structure–Function Relationships

  1. Joan Marsh
  1. M. Jesús Marcote,
  2. Michele Pagano and
  3. Giulio Draetta

Published Online: 28 SEP 2007

DOI: 10.1002/9780470514320.ch4

Ciba Foundation Symposium 170 - Regulation of the Eukaryotic Cell Cycle

Ciba Foundation Symposium 170 - Regulation of the Eukaryotic Cell Cycle

How to Cite

Marcote, M. J., Pagano, M. and Draetta, G. (2007) Cdc2 Protein Kinase: Structure–Function Relationships, in Ciba Foundation Symposium 170 - Regulation of the Eukaryotic Cell Cycle (ed J. Marsh), John Wiley & Sons, Ltd., Chichester, UK. doi: 10.1002/9780470514320.ch4

Author Information

  1. Differentiation Programme, European Molecular Biology Laboratory, Postfach 10 2209, Meyerhofstrasse 1, D-6900 Heidelberg, Germany

Publication History

  1. Published Online: 28 SEP 2007

ISBN Information

Print ISBN: 9780471934462

Online ISBN: 9780470514320

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Keywords:

  • CDC2 protein kinase;
  • phosphorylation;
  • activating factor;
  • cell cycle regulatory pathway;
  • kinase activity

Summary

Activation of the cdc2 kinase in the cell cycle occurs upon binding to a regulatory subunit called cyclin. Cyclin A associates with both Cdc2 and its homologue Cdk2. The two complexes appear in S phase but cyclin A/Cdk2 is activated earlier than cyclin A/Cdc2. Several regions in Cdc2 are involved in binding cyclins A and B. Phosphorylation of cyclin/Cdk complexes ensures that the kinase activity peaks at a specific time in the cell cycle. Phosphorylation of Thrl61 in Cdc2 is required for strong cyclin binding and kinase activity in vitro; its dephosphorylation is necessary for cells to exit mitosis. We have identified a novel ‘Activating factor’ that stimulates binding between cyclin and Cdc2 by inducing phosphorylation of Cdc2 on Thrl61. We propose that Thrl61 is targeted by an additional cell cycle regulatory pathway.