ArticleMolecular biology of the cell2006
Phosphorylation- and polo-box-dependent binding of Plk1 to Bub1 is required for the kinetochore localization of Plk1.
Article in Molecular biology of the cell, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 97 papers.
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Who cites it
97 citing papers in PubMed, 155 citations in OpenAlex.
- GSK3β and Plk1 sequentially phosphorylate ATP-citrate lyase to promote homologous recombination.Science advances · 2026Article
- PKMYT1 has an important role in the timing and fidelity of chromosome segregation.EMBO reports · 2026Article
- Molecular anatomy of PLK1 master docking motifs.Nature communications · 2026Article
- Self-priming of Plk1 binding to BubR1 ensures accurate mitotic progression.Communications biology · 2024Article
- The Eyes Absent family members EYA4 and EYA1 promote PLK1 activation and successful mitosis through tyrosine dephosphorylation.Nature communications · 2024Article
- Phosphorylation of Bub1 by Mph1 promotes Bub1 signaling at the kinetochore to ensure accurate chromosome segregation.The Journal of biological chemistry · 2024Article
- Dissecting the Multiple Functions of the Polo-Like Kinase 1 in the C. elegans Zygote.Methods in molecular biology (Clifton, N.J.) · 2024Article
- A bifunctional kinase-phosphatase module balances mitotic checkpoint strength and kinetochore-microtubule attachment stability.The EMBO journal · 2023Article
- Dynamic Phosphorylation of G9a Regulates its Repressive Activity on Chromatin Accessibility and Mitotic Progression.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023Article
- Specific inhibition of an anticancer target, polo-like kinase 1, by allosterically dismantling its mechanism of substrate recognition.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- UBAP2L-dependent coupling of PLK1 localization and stability during mitosis.EMBO reports · 2023Article
- BUB-1-bound PLK-1 directs CDC-20 kinetochore recruitment to ensure timely embryonic mitoses.Current biology : CB · 2023Article
- BUB-1 and CENP-C recruit PLK-1 to control chromosome alignment and segregation during meiosis I ineLife · 2023Article
- Spatial separation of phosphatase and kinase activity within the Bub complex is required for proper mitosis.Journal of molecular cell biology · 2023Article
- Master mitotic kinases regulate viral genome delivery during papillomavirus cell entry.Nature communications · 2023Article
- Zombies Never Die: The Double Life Bub1 Lives in Mitosis.Frontiers in cell and developmental biology · 2022Review
- Kinase PLK1 regulates the disassembly of the lateral elements and the assembly of the inner centromere during the diakinesis/metaphase I transition in male mouse meiosis.Frontiers in cell and developmental biology · 2022Article
- The Role of Mitotic Kinases and the RZZ Complex in Kinetochore-Microtubule Attachments: Doing the Right Link.Frontiers in cell and developmental biology · 2022Review
- Spatiotemporal coordination of the RSF1-PLK1-Aurora B cascade establishes mitotic signaling platforms.Nature communications · 2021Article
- HN1 interacts with γ-tubulin to regulate centrosomes in advanced prostate cancer cells.Cell cycle (Georgetown, Tex.) · 2021Article
37 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Polo-like kinase 1 (Plk1) is required for the generation of the tension-sensing 3F3/2 kinetochore epitope and facilitates kinetochore localization of Mad2 and other spindle checkpoint proteins. Here, we investigate the mechanism by which Plk1 itself is recruited to kinetochores. We show that Plk1 binds to budding uninhibited by benzimidazole 1 (Bub1) in mitotic human cells. The Plk1-Bub1 interaction requires the polo-box domain (PBD) of Plk1 and is enhanced by cyclin-dependent kinase 1 (Cdk1)-mediated phosphorylation of Bub1 at T609. The PBD-dependent binding of Plk1 to Bub1 facilitates phosphorylation of Bub1 by Plk1 in vitro. Depletion of Bub1 in HeLa cells by RNA interference (RNAi) diminishes the kinetochore localization of Plk1. Ectopic expression of the wild-type Bub1, but not the Bub1-T609A mutant, in Bub1-RNAi cells restores the kinetochore localization of Plk1. Our results suggest that phosphorylation of Bub1 at T609 by Cdk1 creates a docking site for the PBD of Plk1 and facilitates the kinetochore recruitment of Plk1.
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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.