ArticleThe Journal of biological chemistry2010
Dbf4 regulates the Cdc5 Polo-like kinase through a distinct non-canonical binding interaction.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 39 citations in OpenAlex.
- Exploring the multifaceted Dbf4-dependent kinase from temporal, spatial, and substrate repertoire perspectives.Communications biology · 2026Review
- Cdc5-mediated Ulp2 phosphorylation controls the timing of polySUMOylation during the cell cycle.The Journal of cell biology · 2026Article
- 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
- The prognostic significance and potential mechanism of DBF4 zinc finger in hepatocellular carcinoma.Scientific reports · 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
- The Polo kinase Cdc5 is regulated at multiple levels in the adaptation response to telomere dysfunction.Genetics · 2023Article
- The Spo13/Meikin pathway confines the onset of gamete differentiation to meiosis II in yeast.The EMBO journal · 2022Article
- 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
- Meiosis I Kinase Regulators: Conserved Orchestrators of Reductional Chromosome Segregation.BioEssays : news and reviews in molecular, cellular and developmental biology · 2020Article
- Polo kinase recruitment via the constitutive centromere-associated network at the kinetochore elevates centromeric RNA.PLoS genetics · 2020Article
- Distinct surfaces on Cdc5/PLK Polo-box domain orchestrate combinatorial substrate recognition during cell division.Scientific reports · 2020Article
- Functions and regulation of the Polo-like kinase Cdc5 in the absence and presence of DNA damage.Current genetics · 2018Review
- Randomized CRISPR-Cas Transcriptional Perturbation Screening Reveals Protective Genes against Alpha-Synuclein Toxicity.Molecular cell · 2017Article
- Fundamental cell cycle kinases collaborate to ensure timely destruction of the synaptonemal complex during meiosis.The EMBO journal · 2017Article
- DDK Promotes Tumor Chemoresistance and Survival via Multiple Pathways.Neoplasia (New York, N.Y.) · 2017Article
- Dbf4-dependent kinase and the Rtt107 scaffold promote Mus81-Mms4 resolvase activation during mitosis.The EMBO journal · 2017Article
- Ligand stimulation of CD95 induces activation of Plk3 followed by phosphorylation of caspase-8.Cell research · 2016Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cdc7-Dbf4 is a conserved, two-subunit kinase required for initiating eukaryotic DNA replication. Recent studies have shown that Cdc7-Dbf4 also regulates the mitotic exit network (MEN) and monopolar homolog orientation in meiosis I (Matos, J., Lipp, J. J., Bogdanova, A., Guillot, S., Okaz, E., Junqueira, M., Shevchenko, A., and Zachariae, W. (2008) Cell 135, 662-678 and Miller, C. T., Gabrielse, C., Chen, Y. C., and Weinreich, M. (2009) PLoS Genet. 5, e1000498). Both activities likely involve a Cdc7-Dbf4 interaction with Cdc5, the single Polo-like kinase in budding yeast. We previously showed that Dbf4 binds the Cdc5 polo-box domain (PBD) via an ∼40-residue N-terminal sequence, which lacks a PBD consensus binding site (S(pS/pT)(P/X)), and that Dbf4 inhibits Cdc5 function during mitosis. Here we identify a non-consensus PBD binding site within Dbf4 and demonstrate that the PBD-Dbf4 interaction occurs via a distinct PBD surface from that used to bind phosphoproteins. Genetic and biochemical analysis of multiple dbf4 mutants indicate that Dbf4 inhibits Cdc5 function through direct binding. Surprisingly, mutation of invariant Cdc5 residues required for binding phosphorylated substrates has little effect on yeast viability or growth rate. Instead, cdc5 mutants defective for binding phosphoproteins exhibit enhanced resistance to microtubule disruption and an increased rate of spindle elongation. This study, therefore, details the molecular nature of a new type of PBD binding and reveals that Cdc5 targeting to phosphorylated substrates likely regulates spindle dynamics.
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