ArticleMolecular and cellular biology2007
Novel role for Cdc14 sequestration: Cdc14 dephosphorylates factors that promote DNA replication.
Article in Molecular and cellular biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
19 citing papers in PubMed, 42 citations in OpenAlex.
- Site directed mutagenesis reveals functional importance of conserved amino acid residues within the N-terminal domain of Dpb2 in budding yeast.Archives of microbiology · 2024Article
- Analog-sensitive Cdk1 as a tool to study mitotic exit: protein phosphatase 1 is required downstream from Cdk1 inactivation in budding yeast.Chromosome research : an international journal on the molecular, supramolecular and evolutionary aspects of chromosome biology · 2023Article
- Exit from Mitosis in Budding Yeast: Protein Phosphatase 1 is Required Downstream from Cdk1 Inactivation.Research square · 2023Article
- Article
- The Cdc14 Phosphatase Controls Resolution of Recombination Intermediates and Crossover Formation during Meiosis.International journal of molecular sciences · 2021Article
- The Multiple Roles of the Cdc14 Phosphatase in Cell Cycle Control.International journal of molecular sciences · 2020Review
- Control of Eukaryotic DNA Replication Initiation-Mechanisms to Ensure Smooth Transitions.Genes · 2019Review
- Recruitment of the mitotic exit network to yeast centrosomes couples septin displacement to actomyosin constriction.Nature communications · 2018Article
- Diverse roles of Dpb2, the non-catalytic subunit of DNA polymerase ε.Current genetics · 2017Review
- Method for identifying phosphorylated substrates of specific cyclin/cyclin-dependent kinase complexes.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Dependence of Chs2 ER export on dephosphorylation by cytoplasmic Cdc14 ensures that septum formation follows mitosis.Molecular biology of the cell · 2012Article
- Global analysis of Cdc14 phosphatase reveals diverse roles in mitotic processes.The Journal of biological chemistry · 2011Article
- One-hit wonders of genomic instability.Cell division · 2010Article
- Mathematical modelling of DNA replication reveals a trade-off between coherence of origin activation and robustness against rereplication.PLoS computational biology · 2010Article
- An overview of Cdk1-controlled targets and processes.Cell division · 2010Article
- Essential global role of CDC14 in DNA synthesis revealed by chromosome underreplication unrecognized by checkpoints in cdc14 mutants.Proceedings of the National Academy of Sciences of the United States of America · 2009Article
- Efficient protein depletion by genetically controlled deprotection of a dormant N-degron.Molecular systems biology · 2009Article
- Regulation of Sli15/INCENP, kinetochore, and Cdc14 phosphatase functions by the ribosome biogenesis protein Utp7.The Journal of cell biology · 2008Article
- DNA polymerase epsilon: a polymerase of unusual size (and complexity).Progress in nucleic acid research and molecular biology · 2008Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
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.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.