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PMID: 18762578 Published · ppublish English Journal Article

Separase cooperates with Zds1 and Zds2 to activate Cdc14 phosphatase in early anaphase.

The Journal of cell biology ·Vol. 182 ·No. 5 ·2008-09-08 ·Pages 873-83

Queralt E, Uhlmann F

Abstract

Completion of mitotic exit and cytokinesis requires the inactivation of mitotic cyclin-dependent kinase (Cdk) activity. A key enzyme that counteracts Cdk during budding yeast mitotic exit is the Cdc14 phosphatase. Cdc14 is inactive for much of the cell cycle, sequestered by its inhibitor Net1 in the nucleolus. At anaphase onset, separase-dependent down-regulation of PP2A(Cdc55) allows phosphorylation of Net1 and consequent Cdc14 release. How separase causes PP2A(Cdc55) down-regulation is not known. Here, we show that two Cdc55-interacting proteins, Zds1 and Zds2, contribute to timely Cdc14 activation during mitotic exit. Zds1 and Zds2 are required downstream of separase to facilitate nucleolar Cdc14 release. Ectopic Zds1 expression in turn is sufficient to down-regulate PP2A(Cdc55) and promote Net1 phosphorylation. These findings identify Zds1 and Zds2 as new components of the mitotic exit machinery, involved in activation of the Cdc14 phosphatase at anaphase onset. Our results suggest that these proteins may act as separase-regulated PP2A(Cdc55) inhibitors.

MeSH Terms
Adaptor Proteins, Signal Transducing Anaphase Cell Cycle Proteins/metabolism,physiology Cell Nucleolus/metabolism Down-Regulation Endopeptidases/metabolism,physiology Enzyme Activation Nuclear Proteins/metabolism Phosphorylation Protein Phosphatase 2/metabolism Protein Transport Protein Tyrosine Phosphatases/metabolism Saccharomyces cerevisiae/cytology,enzymology,genetics Saccharomyces cerevisiae Proteins/metabolism,physiology Separase p21-Activated Kinases/metabolism,physiology
Chemicals
Adaptor Proteins, Signal Transducing CDC14 protein, S cerevisiae CDC55 protein, S cerevisiae Cell Cycle Proteins Net1 protein, S cerevisiae Nuclear Proteins Saccharomyces cerevisiae Proteins ZDS1 protein, S cerevisiae ZDS2 protein, S cerevisiae p21-Activated Kinases Protein Phosphatase 2 Protein Tyrosine Phosphatases Endopeptidases ESP1 protein, S cerevisiae Separase
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Queralt Ethel
Chromosome Segregation Laboratory, Cancer Research UK London Research Institute, London, England, UK. [email protected]
Uhlmann Frank
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
1540-8140
Published
2008-09-08
Epub
2008-00-01
Pages
873-83
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2528575
Subset
IM
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