ArticleeLife2016
The Ki-67 and RepoMan mitotic phosphatases assemble via an identical, yet novel mechanism.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
What it found
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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.
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Who cites it
39 citing papers in PubMed, 63 citations in OpenAlex.
- Overexpression ofInternational journal of molecular sciences · 2025Article
- PPP1R2 stimulates protein phosphatase-1 through stabilisation of dynamic subunit interactions.Nature communications · 2024Article
- A protein phosphatase 1 specificProceedings of the National Academy of Sciences of the United States of America · 2024Article
- The Aurora B-controlled PP1/RepoMan complex determines the spatial and temporal distribution of mitotic H2B S6 phosphorylation.Open biology · 2024Article
- Ki-67 is necessary during DNA replication for fork protection and genome stability.Genome biology · 2024Article
- Leishmania PNUTS discriminates between PP1 catalytic subunits through an RVxF-ΦΦ-F motif and polymorphisms in the PP1 C-tail and catalytic domain.The Journal of biological chemistry · 2023Article
- Substrate and phosphorylation site selection by phosphoprotein phosphatases.Trends in biochemical sciences · 2023Review
- Inhibitor-3 inhibits Protein Phosphatase 1 via a metal binding dynamic protein-protein interaction.Nature communications · 2023Article
- Tryptophan mutations in G3BP1 tune the stability of a cellular signaling hub by weakening transient interactions with Caprin1 and USP10.The Journal of biological chemistry · 2022Article
- The ribosomal RNA processing 1B:protein phosphatase 1 holoenzyme reveals non-canonical PP1 interaction motifs.Cell reports · 2022Article
- Structure of the SHOC2-MRAS-PP1C complex provides insights into RAF activation and Noonan syndrome.Nature structural & molecular biology · 2022Article
- Orchestrating serine/threonine phosphorylation and elucidating downstream effects by short linear motifs.The Biochemical journal · 2022Review
- Chromosome clustering in mitosis by the nuclear protein Ki-67.Biochemical Society transactions · 2021Article
- Structural Insights into Protein Regulation by Phosphorylation and Substrate Recognition of Protein Kinases/Phosphatases.Life (Basel, Switzerland) · 2021Review
- The intrinsically disorderly story of Ki-67.Open biology · 2021Review
- Regulation of Synaptic Transmission and Plasticity by Protein Phosphatase 1.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2021Review
- Article
- Turn and Face the Strange: A New View on Phosphatases.ACS central science · 2020Review
- Article
- Co-regulation of the antagonistic RepoMan:Aurora-B pair in proliferating cells.Molecular biology of the cell · 2020Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 3 institutions in 3 countries.
Funding
Abstract
Ki-67 and RepoMan have key roles during mitotic exit. Previously, we showed that Ki-67 organizes the mitotic chromosome periphery and recruits protein phosphatase 1 (PP1) to chromatin at anaphase onset, in a similar manner as RepoMan (Booth et al., 2014). Here we show how Ki-67 and RepoMan form mitotic exit phosphatases by recruiting PP1, how they distinguish between distinct PP1 isoforms and how the assembly of these two holoenzymes are dynamically regulated by Aurora B kinase during mitosis. Unexpectedly, our data also reveal that Ki-67 and RepoMan bind PP1 using an identical, yet novel mechanism, interacting with a PP1 pocket that is engaged only by these two PP1 regulators. These findings not only show how two distinct mitotic exit phosphatases are recruited to their substrates, but also provide immediate opportunities for the design of novel cancer therapeutics that selectively target the Ki-67:PP1 and RepoMan:PP1 holoenzymes.
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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.