ArticleThe Journal of biological chemistry2011
Mammalian polo-like kinase 1-dependent regulation of the PBIP1-CENP-Q complex at kinetochores.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 53 citations in OpenAlex.
- Molecular anatomy of PLK1 master docking motifs.Nature communications · 2026Article
- CENP-C-targeted PLK-1 regulates kinetochore function in C. elegans embryos.Journal of cell science · 2024Article
- 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
- BUB-1 and CENP-C recruit PLK-1 to control chromosome alignment and segregation during meiosis I ineLife · 2023Article
- Master mitotic kinases regulate viral genome delivery during papillomavirus cell entry.Nature communications · 2023Article
- The Four Causes: The Functional Architecture of Centromeres and Kinetochores.Annual review of genetics · 2022Review
- Recent Progress on the Localization of PLK1 to the Kinetochore and Its Role in Mitosis.International journal of molecular sciences · 2022Review
- The Role of Mitotic Kinases and the RZZ Complex in Kinetochore-Microtubule Attachments: Doing the Right Link.Frontiers in cell and developmental biology · 2022Review
- Kinetochore Architecture Employs Diverse Linker Strategies Across Evolution.Frontiers in cell and developmental biology · 2022Review
- Mitosis-related geneAnnals of translational medicine · 2021Article
- Regulation of mitotic chromosome architecture and resolution of ultrafine anaphase bridges by PICH.Cell cycle (Georgetown, Tex.) · 2021Article
- Kinetochore assembly throughout the cell cycle.Seminars in cell & developmental biology · 2021Article
- Differential requirements for the CENP-O complex reveal parallel PLK1 kinetochore recruitment pathways.Molecular biology of the cell · 2021Article
- Article
- BUB1 and CENP-U, Primed by CDK1, Are the Main PLK1 Kinetochore Receptors in Mitosis.Molecular cell · 2021Article
- Biochemical evidence for diverse strategies in the inner kinetochore.Open biology · 2020Review
- Conservation of centromeric histone 3 interaction partners in plants.Journal of experimental botany · 2020Article
- Polo kinase recruitment via the constitutive centromere-associated network at the kinetochore elevates centromeric RNA.PLoS genetics · 2020Article
- RZZ-SPINDLY-DYNEIN: you got to keep 'em separated.Cell cycle (Georgetown, Tex.) · 2020Review
- Reconstitution of a 26-Subunit Human Kinetochore Reveals Cooperative Microtubule Binding by CENP-OPQUR and NDC80.Molecular cell · 2018Article
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Authors and funding
8 authors at 4 institutions in 2 countries.
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Abstract
Mammalian polo-like kinase 1 (Plk1) plays a pivotal role during M-phase progression. Plk1 localizes to specific subcellular structures through the targeting activity of the C-terminal polo-box domain (PBD). Disruption of the PBD function results in improper bipolar spindle formation, chromosome missegregation, and cytokinesis defect that ultimately lead to the generation of aneuploidy. It has been shown that Plk1 recruits itself to centromeres by phosphorylating and binding to a centromere scaffold, PBIP1 (also called MLF1IP and CENP-U[50]) through its PBD. However, how PBIP1 itself is targeted to centromeres and what roles it plays in the regulation of Plk1-dependent mitotic events remain unknown. Here, we demonstrated that PBIP1 directly interacts with CENP-Q, and this interaction was mutually required not only for their stability but also for their centromere localization. Plk1 did not appear to interact with CENP-Q directly. However, Plk1 formed a ternary complex with PBIP1 and CENP-Q through a self-generated p-T78 motif on PBIP1. This complex formation was central for Plk1-dependent phosphorylation of PBIP1-bound CENP-Q and delocalization of the PBIP1-CENP-Q complex from mitotic centromeres. This study reveals a unique mechanism of how PBIP1 mediates Plk1-dependent phosphorylation event onto a third protein, and provides new insights into the mechanism of how Plk1 and its recruitment scaffold, PBIP1-CENP-Q complex, are localized to and delocalized from centromeres.
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