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First published online 5 May 2004
doi: 10.1242/jcs.01107
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Research Article |
1 Centro de Investigación del Cáncer, Departamento de Microbiología y Genética, Campus `Miguel de Unamuno', Universidad de Salamanca/CSIC, 37007 Salamanca, Spain
2 Cell Cycle Control Laboratory, Swiss Institute for Experimental Cancer Research (ISREC), Chemin des Boveressess 155, 1066 Epalinges, Switzerland
* Author for correspondence (e-mail: abn{at}usal.es)
Accepted 16 January 2004
The Schizosaccaromyces pombe protein Flp1p belongs to a conserved family of serine-threonine-phosphatases. The founding member of this family, Saccharomyces cerevisiae Cdc14p, is required for inactivation of mitotic CDKs and reversal of CDK mediated phosphorylation at the end of mitosis, thereby bringing about the M-G1 transition. Initial studies of Flp1p suggest that it may play a different role to Cdc14p. Here we show that Flp1p is required for rapid degradation of the mitotic inducer Cdc25p at the end of mitosis, and that Cdc25p is a substrate of Flp1p in vitro. Down-regulation of Cdc25p activity by Flp1p may ensure a prompt inactivation of mitotic CDK complexes to trigger cell division. Our results suggest a regulatory mechanism, and a universal role, for Cdc14p like proteins in coordination of cytokinesis with other cell cycle events.
Key words: flp1+, Cell cycle, Mitotic exit, Fission yeast
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