ArticleJournal of cell science2016
PP1 initiates the dephosphorylation of MASTL, triggering mitotic exit and bistability in human cells.
Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 53 citations in OpenAlex.
- The MASTL/YBX1/PAK4 axis regulated by stress-activated STK24 triggers lenvatinib resistance and tumor progression in HCC.Hepatology (Baltimore, Md.) · 2026Article
- Phosphatase specificity influences phosphorylation timing of CDK substrates during the cell cycle.Nature communications · 2025Article
- Oscillations in PP1 activity are essential for accurate progression through mammalian oocyte meiosis.Cell cycle (Georgetown, Tex.) · 2023Article
- Article
- SILAC kinase screen identifies potential MASTL substrates.Scientific reports · 2022Article
- Dephosphorylation in nuclear reassembly after mitosis.Frontiers in cell and developmental biology · 2022Review
- Structural, enzymatic and spatiotemporal regulation of PP2A-B55 phosphatase in the control of mitosis.Frontiers in cell and developmental biology · 2022Review
- Analysis of Host Jejunum Transcriptome and Associated Microbial Community Structure Variation in Young Calves with Feed-Induced Acidosis.Metabolites · 2021Article
- Coupling of Cdc20 inhibition and activation by BubR1.The Journal of cell biology · 2021Article
- Towards Dissecting the Mechanism of Protein Phosphatase-1 Inhibition by Its C-Terminal Phosphorylation.Chembiochem : a European journal of chemical biology · 2021Article
- Bistable, Biphasic Regulation of PP2A-B55 Accounts for the Dynamics of Mitotic Substrate Phosphorylation.Current biology : CB · 2021Article
- Knockdown of Microtubule Associated Serine/threonine Kinase Like Expression Inhibits Gastric Cancer Cell Growth and Induces Apoptosis by Activation of ERK1/2 and Inactivation of NF-κB Signaling.Current medical science · 2021Article
- PP1 promotes cyclin B destruction and the metaphase-anaphase transition by dephosphorylating CDC20.Molecular biology of the cell · 2020Article
- The Greatwall kinase safeguards the genome integrity by affecting the kinome activity in mitosis.Oncogene · 2020Article
- Ordered dephosphorylation initiated by the selective proteolysis of cyclin B drives mitotic exit.eLife · 2020Article
- AKT Regulates Mitotic Progression of Mammalian Cells by Phosphorylating MASTL, Leading to Protein Phosphatase 2A Inactivation.Molecular and cellular biology · 2020Article
- Greatwall-Endosulfine: A Molecular Switch that Regulates PP2A/B55 Protein Phosphatase Activity in Dividing and Quiescent Cells.International journal of molecular sciences · 2019Review
- Review
- Phosphatases in Mitosis: Roles and Regulation.Biomolecules · 2019Review
- Protein phosphatases in the regulation of mitosis.The Journal of cell biology · 2019Review
Corrections and comments
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Authors and funding
12 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Entry into mitosis is driven by the phosphorylation of thousands of substrates, under the master control of Cdk1. During entry into mitosis, Cdk1, in collaboration with MASTL kinase, represses the activity of the major mitotic protein phosphatases, PP1 and PP2A, thereby ensuring mitotic substrates remain phosphorylated. For cells to complete and exit mitosis, these phosphorylation events must be removed, and hence, phosphatase activity must be reactivated. This reactivation of phosphatase activity presumably requires the inhibition of MASTL; however, it is not currently understood what deactivates MASTL and how this is achieved. In this study, we identified that PP1 is associated with, and capable of partially dephosphorylating and deactivating, MASTL during mitotic exit. Using mathematical modelling, we were able to confirm that deactivation of MASTL is essential for mitotic exit. Furthermore, small decreases in Cdk1 activity during metaphase are sufficient to initiate the reactivation of PP1, which in turn partially deactivates MASTL to release inhibition of PP2A and, hence, create a feedback loop. This feedback loop drives complete deactivation of MASTL, ensuring a strong switch-like activation of phosphatase activity during mitotic exit.
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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.