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Published February 23, 2009 | Published
Journal Article Open

Dbf2-Mob1 drives relocalization of protein phosphatase Cdc14 to the cytoplasm during exit from mitosis


Exit from mitosis is characterized by a precipitous decline in cyclin-dependent kinase (Cdk) activity, dissolution of mitotic structures, and cytokinesis. In Saccharomyces cerevisiae, mitotic exit is driven by a protein phosphatase, Cdc14, which is in part responsible for counteracting Cdk activity. Throughout interphase, Cdc14 is sequestered in the nucleolus, but successful anaphase activates the mitotic exit network (MEN), which triggers dispersal of Cdc14 throughout the cell by a mechanism that has remained unknown. In this study, we show that a MEN component, protein kinase Dbf2–Mob1, promotes transfer of Cdc14 to the cytoplasm and consequent exit from mitosis by direct phosphorylation of Cdc14 on serine and threonine residues adjacent to a nuclear localization signal (NLS), thereby abrogating its NLS activity. Our results define a mechanism by which the MEN promotes exit from mitosis.

Additional Information

© 2009 Mohl et al. Submitted: 3 December 2008. Accepted: 21 January 2009. Published online February 16, 2009. We thank the Caltech Protein Expression Facility for technical assistance, T. Stearns, M. Cyert, and E. Schiebel for plasmids, and members of the Deshaies Laboratory, especially W. Shou, R. Azzam, and A. Mah, for their valuable assistance. R.J. Deshaies is a Howard Hughes Medical Institute investigator. This work was supported by a National Institutes of Health grant (GM059940) to R.J. Deshaies. D.A. Mohl was supported in part by a postdoctoral fellowship from the American Cancer Society.

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