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A more recent version of this article appeared on January 1, 2006
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Submitted on December 22, 2004
Revised on June 16, 2005
Accepted on July 21, 2005
Department of Biomedical Sciences, College of Medicine, Florida State University, FL 32306
Monitoring Editor: Tim Stearns
In budding yeast S. cerevisiae, Cdc5 kinase is a component of mitotic exit network (MEN), which inactivates cyclin dependent kinase (CDK) after chromosome segregation. cdc5-1 mutants arrest at telophase at the nonpermissive temperature due to the failure of CDK inactivation. To identify more negative regulators of MEN, we carried out a genetic screen for genes that are toxic to cdc5-1 mutants when overexpressed. Genes that encode the B-regulatory subunit (Cdc55) and the three catalytic subunits (Pph21, Pph22 and Pph3) of phosphatase 2A (PP2A) were isolated. In addition to cdc5-1, overexpression of CDC55, PPH21 or PPH22 is also toxic to other temperature sensitive mutants that display defects in mitotic exit. Consistently, deletion of CDC55 partially suppresses the temperature sensitivity of these mutants. Moreover, in the presence of spindle damage, PP2A mutants display nuclear localized Cdc14, the key player in MEN pathway, indicative of MEN activation. All the evidence suggests the negative role of PP2A in mitotic exit. Finally, our genetic and biochemical data suggest that PP2A regulates the phosphorylation of Tem1, which acts at the very top of MEN pathway.
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