ArticleCell proliferation2016
Protein phosphatase 4 plays dual roles during cell proliferation.
Article in Cell proliferation, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 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.
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Who cites it
7 citing papers in PubMed.
- The regulation of protein phosphatase 4 by FBXO42 is required for cancer cell survival.EMBO reports · 2026Article
- Heterogeneous nuclear ribonucleoprotein U (HNRNPU) safeguards the developing mouse cortex.Nature communications · 2022Article
- Protein Phosphatase 4 Promotes Hepatocyte Lipoapoptosis by Regulating RAC1/MLK3/JNK Pathway.Oxidative medicine and cellular longevity · 2021Article
- Functional roles of protein phosphatase 4 in multiple aspects of cellular physiology: a friend and a foe.BMB reports · 2020Review
- PP4 deficiency leads to DNA replication stress that impairs immunoglobulin class switch efficiency.Cell death and differentiation · 2019Article
- Phosphatase-regulated recruitment of the spindle- and kinetochore-associated (Ska) complex to kinetochores.Biology open · 2017Article
- The protein phosphatase 4 complex promotes the Notch pathway andBiology open · 2017Article
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
objectivesProtein phosphatase 4 (PP4) has been reported to be indispensable for cell proliferation and survival. Deletion of PP4 has been shown to induce abnormal and even lethal events in growth and development both in lower eukaryotes and in mammals. However, until now, effects of PP4 up-regulation have remained unclear. MATERIALS AND
methodsTo test effects of PP4 on cell proliferation, cell cycle and morphology in HepG2 cells, it was down-regulated using PP4 siRNA or its activity was inhibited using PP4RL (a PP4 phosphatase-dead mutant) adenoviruses. Alternatively, PP4 was up-regulated using PP4 adenoviruses. Next, we used a functional proteomic approach to identify proteins that may interact with PP4. Furthermore, we performed rescue experiments to verify the possible mechanisms.
resultsTo our surprise, we found that both up-regulation and inhibition of PP4 inhibited cell proliferation. Unlike PP4 inhibition, PP4 up-regulation induced prominent arrest at the prometaphase/metaphase transition by causing defects in chromosome alignment and spindle assembly. Moreover, we identified scaffold attachment factor A (SAF-A) (an important protein required for kinetochore-microtubule attachment that participates in the prometaphase/metaphase transition), to be a novel protein that interacts with PP4, using a proteomic approach. Thus, mutual regulatory mechanisms exist between PP4 and SAF-A. Interactions between PP4 and SAF-A played a role in prometaphase/metaphase transition.
conclusionsOur data demonstrate a novel regulatory mechanism involving PP4 in cell proliferation.
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