ArticleCell cycle (Georgetown, Tex.)2014
The budding yeast Polo-like kinase Cdc5 is released from the nucleus during anaphase for timely mitotic exit.
Article in Cell cycle (Georgetown, Tex.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 17 citations in OpenAlex.
- A coordinated kinase and phosphatase network regulates Stu2 recruitment to yeast kinetochores.The Journal of cell biology · 2025Article
- Decoding the Nucleolar Role in Meiotic Recombination and Cell Cycle Control: Insights into Cdc14 Function.International journal of molecular sciences · 2024Review
- Article
- Designer membraneless organelles sequester native factors for control of cell behavior.Nature chemical biology · 2021Article
- Article
- Unifying the mechanism of mitotic exit control in a spatiotemporal logical model.PLoS biology · 2020Article
- Proline-Rich Motifs Control G2-CDK Target Phosphorylation and Priming an Anchoring Protein for Polo Kinase Localization.Cell reports · 2020Article
- Review
- Functions and regulation of the Polo-like kinase Cdc5 in the absence and presence of DNA damage.Current genetics · 2018Review
- The budding yeast Polo-like kinase localizes to distinct populations at centrosomes during mitosis.Molecular biology of the cell · 2017Article
- Cell cycle-dependent phosphorylation of Sec4p controls membrane deposition during cytokinesis.The Journal of cell biology · 2016Article
- Polo kinase Cdc5 associates with centromeres to facilitate the removal of centromeric cohesin during mitosis.Molecular biology of the cell · 2016Article
- The eukaryotic protein kinase superfamily of the necrotrophic fungal plant pathogen, Sclerotinia sclerotiorum.Molecular plant pathology · 2016Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Polo-like kinases are important regulators of multiple mitotic events; however, how Polo-like kinases are spatially and temporally regulated to perform their many tasks is not well understood. Here, we examined the subcellular localization of the budding yeast Polo-like kinase Cdc5 using a functional Cdc5-GFP protein expressed from the endogenous locus. In addition to the well-described localization of Cdc5 at the spindle pole bodies (SPBs) and the bud neck, we found that Cdc5-GFP accumulates in the nucleus in early mitosis but is released to the cytoplasm in late mitosis in a manner dependent on the Cdc14 phosphatase. This Cdc5 release from the nucleus is important for mitotic exit because artificial sequestration of Cdc5 in the nucleus by addition of a strong nuclear localization signal (NLS) resulted in mitotic exit defects. We identified a key cytoplasmic target of Cdc5 as Bfa1, an inhibitor of mitotic exit. Our study revealed a novel layer of Cdc5 regulation and suggests the existence of a possible coordination between Cdc5 and Cdc14 activity.
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