We have updated our privacy policy. If you have any question, contact us at privacy@scicrunch.org. Dismiss and don't show again

Searching across hundreds of databases

Our searching services are busy right now. Your search will reload in five seconds.

Forgot Password

If you have forgotten your password you can enter your email here and get a temporary password sent to your email.

Novel role for Cdc14 sequestration: Cdc14 dephosphorylates factors that promote DNA replication.

The phosphatase Cdc14 is required for mitotic exit in budding yeast. Cdc14 promotes Cdk1 inactivation by targeting proteins that, when dephosphorylated, trigger degradation of mitotic cyclins and accumulation of the Cdk1 inhibitor, Sic1. Cdc14 is sequestered in the nucleolus during most of the cell cycle but is released into the nucleus and cytoplasm during anaphase. When Cdc14 is not properly sequestered in the nucleolus, expression of the S-phase cyclin Clb5 is required for viability, suggesting that the antagonizing activity of Clb5-dependent Cdk1 specifically is necessary when Cdc14 is delocalized. We show that delocalization of Cdc14 combined with loss of Clb5 causes defects in DNA replication. When Cdc14 is not sequestered, it efficiently dephosphorylates a subset of Cdk1 substrates including the replication factors, Sld2 and Dpb2. Mutations causing Cdc14 mislocalization interact genetically with mutations affecting the function of DNA polymerase epsilon and the S-phase checkpoint protein Mec1. Our findings suggest that Cdc14 is retained in the nucleolus to support a favorable kinase/phosphatase balance while cells are replicating their DNA, in addition to the established role of Cdc14 sequestration in coordinating nuclear segregation with mitotic exit.

Pubmed ID: 17116692 RIS Download

Mesh terms: CDC2 Protein Kinase | Cell Cycle Proteins | Cyclin B | DNA Polymerase II | DNA Replication | Gene Deletion | Genes, Fungal | Green Fluorescent Proteins | Intracellular Signaling Peptides and Proteins | Mutation | Nuclear Proteins | Phosphoprotein Phosphatases | Phosphorylation | Protein Subunits | Protein Transport | Protein Tyrosine Phosphatases | Protein-Serine-Threonine Kinases | Recombinant Fusion Proteins | S Phase | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Substrate Specificity

Research resources used in this publication

None found

Research tools detected in this publication

None found

Data used in this publication

None found

Associated grants

  • Agency: NIGMS NIH HHS, Id: R01 GM047238
  • Agency: NCI NIH HHS, Id: T32 CA009673
  • Agency: NIGMS NIH HHS, Id: GM 047238
  • Agency: NCI NIH HHS, Id: T32 CA 009673-29

Publication data is provided by the National Library of Medicine ® and PubMed ®. Data is retrieved from PubMed ® on a weekly schedule. For terms and conditions see the National Library of Medicine Terms and Conditions.

We have not found any resources mentioned in this publication.