Literature DB >> 9552387

Regulation of Cdc2 activity by phosphorylation at T14/Y15.

L D Berry1, K L Gould.   

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 Schizosaccharomysces 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 active state by Wee1/Mik1-mediated phosphorylation at Y15 (and, possibly, T14). At the G2/M boundary, the Cdc25 protein phosphatase is activated to dephosphorylate the Cdc2/Cdc13 complex, resulting in abrupt activation of Cdc2 kinase activity and entry into mitosis.

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Year:  1996        PMID: 9552387     DOI: 10.1007/978-1-4615-5873-6_10

Source DB:  PubMed          Journal:  Prog Cell Cycle Res        ISSN: 1087-2957


  40 in total

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5.  Phosphorylation of Cdc28 and regulation of cell size by the protein kinase CKII in Saccharomyces cerevisiae.

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9.  Sharp-1 modulates the cellular response to DNA damage.

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Review 10.  Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae.

Authors:  M D Mendenhall; A E Hodge
Journal:  Microbiol Mol Biol Rev       Date:  1998-12       Impact factor: 11.056

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