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Regulation of Cdc2 activity by phosphorylation at T14/Y15

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Progress in Cell Cycle Research

Part of the book series: Progress in Cell Cycle Research ((PCCR))

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.

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Authors and Affiliations

  1. Howard Hughes Medical Institute, Department of Cell Biology, Vanderbilt University, 37212, Nashville, TN, USA

    Lynne D. Berry & Kathleen L. Gould

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  1. Lynne D. Berry
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  2. Kathleen L. Gould
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Editors and Affiliations

  1. Centre National de la Recherche Scientifique, Roscoff, France

    Laurent Meijer , Silvana Guidet  & Lee Vogel ,  & 

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Berry, L.D., Gould, K.L. (1996). Regulation of Cdc2 activity by phosphorylation at T14/Y15. In: Meijer, L., Guidet, S., Vogel, L. (eds) Progress in Cell Cycle Research. Progress in Cell Cycle Research. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-5873-6_10

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  • DOI: https://doi.org/10.1007/978-1-4615-5873-6_10

  • Publisher Name: Springer, Boston, MA

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