ArticleProceedings of the National Academy of Sciences of the United States of America2011
Independent modulation of the kinase and polo-box activities of Cdc5 protein unravels unique roles in the maintenance of genome stability.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 31 citations in OpenAlex.
- Yeast centrosomes act as organizing centers to promote Polo kinase-mediated adaptation to persistent DNA damage.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Large-scale phenogenomic analysis of human cancers uncovers frequent alterations affecting SMC5/6 complex components in breast cancer.NAR cancer · 2023Article
- The Polo kinase Cdc5 is regulated at multiple levels in the adaptation response to telomere dysfunction.Genetics · 2023Article
- Moonlighting at the Poles: Non-Canonical Functions of Centrosomes.Frontiers in cell and developmental biology · 2022Review
- Distinct surfaces on Cdc5/PLK Polo-box domain orchestrate combinatorial substrate recognition during cell division.Scientific reports · 2020Article
- Adaptation in replicative senescence: a risky business.Current genetics · 2019Review
- Cell cycle-dependent association of polo kinase Cdc5 with CENP-A contributes to faithful chromosome segregation in budding yeast.Molecular biology of the cell · 2019Article
- A unified view of spatio-temporal control of mitotic entry: Polo kinase as the key.Open biology · 2018Review
- 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
- Physical Association of Saccharomyces cerevisiae Polo-like Kinase Cdc5 with Chromosomal Cohesin Facilitates DNA Damage Response.The Journal of biological chemistry · 2016Article
- Polo kinase Cdc5 associates with centromeres to facilitate the removal of centromeric cohesin during mitosis.Molecular biology of the cell · 2016Article
- Understanding the Polo Kinase machine.Oncogene · 2015Review
- Phosphoproteome dynamics of Saccharomyces cerevisiae under heat shock and cold stress.Molecular systems biology · 2015Article
- The yeast polo kinase Cdc5 regulates the shape of the mitotic nucleus.Current biology : CB · 2014Article
- Structural maintenance of chromosome (SMC) proteins link microtubule stability to genome integrity.The Journal of biological chemistry · 2014Article
- Cdk1-dependent regulation of the Mre11 complex couples DNA repair pathways to cell cycle progression.Cell cycle (Georgetown, Tex.) · 2014Article
- The budding yeast Polo-like kinase Cdc5 is released from the nucleus during anaphase for timely mitotic exit.Cell cycle (Georgetown, Tex.) · 2014Article
- Phosphorylation of Chs2p regulates interaction with COPII.Journal of cell science · 2013Article
- Mitotic exit and separation of mother and daughter cells.Genetics · 2012Review
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Polo-like kinases (PLKs) are evolutionarily conserved kinases essential for cell cycle regulation. These kinases are characterized by the presence of a C-terminal phosphopeptide-interaction domain, the polo-box domain (PBD). How the functional domains of PLKs work together to promote cell division is not understood. To address this, we performed a genetic screen to identify mutations that independently modulate the kinase and PBD activities of yeast PLK/Cdc5. This screen identified a mutagenic hotspot in the F-helix region of Cdc5 kinase domain that allows one to control kinase activity in vivo. These mutations can be systematically engineered into other major eukaryotic cell cycle kinases to similarly regulate their activity in live cells. Here, using this approach, we show that the kinase activity of Cdc5 can promote the execution of several stages of mitosis independently of PBD activity. In particular, we observe that the activation of Cdc14 and execution of mitotic exit are uniquely sensitive to the modulation of Cdc5 kinase activity. In contrast, PBD-defective mutants are capable of completing mitosis but are unable to maintain spindle pole body integrity. Consistent with this defect, PBD-deficient cells progressively double the size of their genome and ultimately lose genome integrity. Collectively, these results highlight the specific contributions of Cdc5 functional domains to cell division and reveal unexpected mechanisms controlling spindle pole body behavior and genome stability.
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