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....

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Bibliographic Details
Published in:The Journal of cell biology 2009-02, Vol.184 (4), p.527-539
Main Authors: Mohl, Dane A., Huddleston, Michael J., Collingwood, Therese S., Annan, Roland S., Deshaies, Raymond J.
Format: Article
Language:English
Subjects:
Anaphase
Biochemistry
Cell cycle
Cell Cycle Proteins - metabolism
Cell division
Cell nucleus
Cell Nucleus - metabolism
Chromosome Segregation
Cytoplasm
Cytoplasm - metabolism
Daughter cells
Enzymes
GTP-Binding Proteins - metabolism
Kinases
Mitosis
Mother cells
Mutation
Nuclear Localization Signals
Phosphoprotein Phosphatases - metabolism
Phosphoproteins - metabolism
Phosphorylation
Protein Tyrosine Phosphatases - metabolism
Protein-Serine-Threonine Kinases - metabolism
Proteins
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - metabolism
Saccharomyces cerevisiae Proteins - metabolism
Schizosaccharomyces - cytology
Schizosaccharomyces - metabolism
Schizosaccharomyces pombe Proteins - metabolism
Yeast
Yeasts
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Summary: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.
ISSN:0021-9525
1540-8140
DOI:10.1083/jcb.200812022