ArticleThe Journal of biological chemistry2011
PLK1 phosphorylates mitotic centromere-associated kinesin and promotes its depolymerase activity.
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 59 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
59 citing papers in PubMed, 89 citations in OpenAlex.
- PLK-1 suppresses centrosome maturation and microtubule polymerization to ensure faithful oocyte meiosis.The Journal of cell biology · 2025Article
- KIF2C condensation concentrates PLK1 and phosphorylated BRCA2 on kinetochore microtubules in mitosis.Nucleic acids research · 2025Article
- TheLife (Basel, Switzerland) · 2025Article
- Polo-like kinase 1 prevents excess microtubule polymerization inbioRxiv : the preprint server for biology · 2024Article
- PLK1 phosphorylation of ZW10 guides accurate chromosome segregation in mitosis.Journal of molecular cell biology · 2024Article
- Nek2A prevents centrosome clustering and induces cell death in cancer cells via KIF2C interaction.Cell death & disease · 2024Article
- BUB-1 and CENP-C recruit PLK-1 to control chromosome alignment and segregation during meiosis I ineLife · 2023Article
- Mitotic protein kinase-driven crosstalk of machineries for mitosis and metastasis.Experimental & molecular medicine · 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
- Identification of prognostic markers by weighted gene co-expression network analysis in non-small cell lung cancer.Bioengineered · 2021Article
- Review
- SCFThe EMBO journal · 2021Article
- Identification of novel microtubule inhibitors effective in fission yeast and human cells and their effects on breast cancer cell lines.Open biology · 2021Article
- Article
- Feedback control of PLK1 by Apolo1 ensures accurate chromosome segregation.Cell reports · 2021Article
- The CINs of Polo-Like Kinase 1 in Cancer.Cancers · 2020Review
- Methylation of PLK1 by SET7/9 ensures accurate kinetochore-microtubule dynamics.Journal of molecular cell biology · 2020Article
- Co-expression network analysis identified KIF2C in association with progression and prognosis in lung adenocarcinoma.Cancer biomarkers : section A of Disease markers · 2019Article
- Phosphatidylinositol-5-phosphate 4-kinase gamma accumulates at the spindle pole and prevents microtubule depolymerization.Cell division · 2019Article
- The kinetochore-microtubule interface at a glance.Journal of cell science · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
12 authors at 3 institutions in 2 countries.
Funding
Abstract
During cell division, interaction between kinetochores and dynamic spindle microtubules governs chromosome movements. The microtubule depolymerase mitotic centromere-associated kinesin (MCAK) is a key regulator of mitotic spindle assembly and dynamics. However, the regulatory mechanisms underlying its depolymerase activity during the cell cycle remain elusive. Here, we showed that PLK1 is a novel regulator of MCAK in mammalian cells. MCAK interacts with PLK1 in vitro and in vivo. The neck and motor domain of MCAK associates with the kinase domain of PLK1. MCAK is a novel substrate of PLK1, and the phosphorylation stimulates its microtubule depolymerization activity of MCAK in vivo. Overexpression of a polo-like kinase 1 phosphomimetic mutant MCAK causes a dramatic increase in misaligned chromosomes and in multipolar spindles in mitotic cells, whereas overexpression of a nonphosphorylatable MCAK mutant results in aberrant anaphase with sister chromatid bridges, suggesting that precise regulation of the MCAK activity by PLK1 phosphorylation is critical for proper microtubule dynamics and essential for the faithful chromosome segregation. We reasoned that dynamic regulation of MCAK phosphorylation by PLK1 is required to orchestrate faithful cell division, whereas the high levels of PLK1 and MCAK activities seen in cancer cells may account for a mechanism underlying the pathogenesis of genomic instability.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
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.