ArticleThe Journal of biological chemistry2011
Global analysis of Cdc14 phosphatase reveals diverse roles in mitotic processes.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 71 citations in OpenAlex.
- Central Role of the Actomyosin Ring in Coordinating Cytokinesis Steps in Budding Yeast.Journal of fungi (Basel, Switzerland) · 2024Review
- Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024Review
- Saccharomyces cerevisiae deficient in the early anaphase release of Cdc14 can traverse anaphase I without ribosomal DNA disjunction and successfully complete meiosis.Biology open · 2023Article
- Regulation of Rim4 distribution, function, and stability during meiosis by PKA, Cdc14, and 14-3-3 proteins.Cell reports · 2023Article
- 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
- Phosphoproteomic Approaches for Identifying Phosphatase and Kinase Substrates.Molecules (Basel, Switzerland) · 2023Review
- Exit from Mitosis in Budding Yeast: Protein Phosphatase 1 is Required Downstream from Cdk1 Inactivation.Research square · 2023Article
- Cdc14 spatiotemporally dephosphorylates Atg13 to activate autophagy during meiotic divisions.The Journal of cell biology · 2022Article
- Article
- Cdk1 phosphorylation of fission yeast paxillin inhibits its cytokinetic ring localization.Molecular biology of the cell · 2021Article
- Article
- The regulation of Net1/Cdc14 by the Hog1 MAPK upon osmostress unravels a new mechanism regulating mitosis.Cell cycle (Georgetown, Tex.) · 2020Review
- Article
- Hog1 activation delays mitotic exit via phosphorylation of Net1.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Review
- Proteins that physically interact with the phosphatase Cdc14 in Candida albicans have diverse roles in the cell cycle.Scientific reports · 2019Article
- How the cell cycle clock ticks.Molecular biology of the cell · 2019Article
- Helicase/SUMO-targeted ubiquitin ligase Uls1 interacts with the Holliday junction resolvase Yen1.PloS one · 2019Article
- A PxL motif promotes timely cell cycle substrate dephosphorylation by the Cdc14 phosphatase.Nature structural & molecular biology · 2018Article
- Recruitment of the mitotic exit network to yeast centrosomes couples septin displacement to actomyosin constriction.Nature communications · 2018Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Cdc14 phosphatase regulates multiple events during anaphase and is essential for mitotic exit in budding yeast. Cdc14 is regulated in both a spatial and temporal manner. It is sequestered in the nucleolus for most of the cell cycle by the nucleolar protein Net1 and is released into the nucleus and cytoplasm during anaphase. To identify novel binding partners of Cdc14, we used affinity purification of Cdc14 and mass spectrometric analysis of interacting proteins from strains in which Cdc14 localization or catalytic activity was altered. To alter Cdc14 localization, we used a strain deleted for NET1, which causes full release of Cdc14 from the nucleolus. To alter Cdc14 activity, we generated mutations in the active site of Cdc14 (C283S or D253A), which allow binding of substrates, but not dephosphorylation, by Cdc14. Using this strategy, we identified new interactors of Cdc14, including multiple proteins involved in mitotic events. A subset of these proteins displayed increased affinity for catalytically inactive mutants of Cdc14 compared with the wild-type version, suggesting they are likely substrates of Cdc14. We have also shown that several of the novel Cdc14-interacting proteins, including Kar9 (a protein that orients the mitotic spindle) and Bni1 and Bnr1 (formins that nucleate actin cables and may be important for actomyosin ring contraction) are specifically dephosphorylated by Cdc14 in vitro and in vivo. Our findings suggest the dephosphorylation of the formins may be important for their observed localization change during exit from mitosis and indicate that Cdc14 targets proteins involved in wide-ranging mitotic events.
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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.