ArticleScientific reports2020
Distinct surfaces on Cdc5/PLK Polo-box domain orchestrate combinatorial substrate recognition during cell division.
Article in Scientific reports, 2020. 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, 16 citations in OpenAlex.
- Mechanisms of formic acid stress response in evolved yeast for microbial-electrocatalytic systems.Biodesign research · 2026Article
- A coordinated kinase and phosphatase network regulates Stu2 recruitment to yeast kinetochores.The Journal of cell biology · 2025Article
- A minimal deterministic model reveals integration of spindle assembly and position checkpoints in mitosis.Scientific reports · 2025Article
- Proteome-wide forced interactions reveal a functional map of cell-cycle phospho-regulation inNucleus (Austin, Tex.) · 2024Article
- Article
- An acidic loop in the FHA domain of the yeast meiosis-specific kinase Mek1 interacts with a specific motif in a subset of Mek1 substrates.bioRxiv : the preprint server for biology · 2024Article
- Rewiring of the phosphoproteome executes two meiotic divisions in budding yeast.The EMBO journal · 2024Article
- Spo13/MEIKIN ensures a Two-Division meiosis by preventing the activation of APC/CThe EMBO journal · 2023Article
- Gene expression profiling and protein-protein interaction analysis reveals the dynamic role of MCM7 in Alzheimer's disorder and breast cancer.3 Biotech · 2022Article
- The Spo13/Meikin pathway confines the onset of gamete differentiation to meiosis II in yeast.The EMBO journal · 2022Article
- Article
- Cell-cycle phospho-regulation of the kinetochore.Current genetics · 2021Review
- Exo1 recruits Cdc5 polo kinase to MutLγ to ensure efficient meiotic crossover formation.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
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Authors and funding
7 authors at 4 institutions in 1 country.
Funding
Abstract
Polo-like kinases (Plks) are key cell cycle regulators. They contain a kinase domain followed by a polo-box domain that recognizes phosphorylated substrates and enhances their phosphorylation. The regulatory subunit of the Dbf4-dependent kinase complex interacts with the polo-box domain of Cdc5 (the sole Plk in Saccharomyces cerevisiae) in a phosphorylation-independent manner. We have solved the crystal structures of the polo-box domain of Cdc5 on its own and in the presence of peptides derived from Dbf4 and a canonical phosphorylated substrate. The structure bound to the Dbf4-peptide reveals an additional density on the surface opposite to the phospho-peptide binding site that allowed us to propose a model for the interaction. We found that the two peptides can bind simultaneously and non-competitively to the polo-box domain in solution. Furthermore, point mutations on the surface opposite to the phosphopeptide binding site of the polo-box domain disrupt the interaction with the Dbf4 peptide in solution and cause an early anaphase arrest phenotype distinct from the mitotic exit defect typically observed in cdc5 mutants. Collectively, our data illustrates the importance of non-canonical interactions mediated by the polo-box domain and provide key mechanistic insights into the combinatorial recognition of substrates by Polo-like kinases.
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