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Published online
doi:10.1083/jcb.200812022
The Journal of Cell Biology, Vol. 184, No. 4, 527-539
The Rockefeller University Press, 0021-9525 $30.00
© Mohl et al.
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Article

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



Dane A. Mohl2, Michael J. Huddleston3, Therese S. Collingwood3, Roland S. Annan3, and Raymond J. Deshaies1,2

1 Howard Hughes Medical Institute and 2 Division of Biology, California Institute of Technology, Pasadena, CA 91125
3 Proteomics and Biological Mass Spectrometry Laboratory, GlaxoSmithKline, King of Prussia, PA 19406

Correspondence to Dane A. Mohl: mohld{at}caltech.edu; or Raymond J. Deshaies: deshaies{at}caltech.edu

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.

Abbreviations used in this paper: APC, anaphase-promoting complex; BP, basic patch; DIC, differential interference contrast; LC, liquid chromatography; LMP, low melting point; MEN, mitotic exit network; MS, mass spectrometry; NES, nuclear export signal; PS, phosphosite.

© 2009 Mohl et al.
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