ArticleJournal of cell science2013
The phosphorylation of ARPP19 by Greatwall renders the auto-amplification of MPF independently of PKA in Xenopus oocytes.
Article in Journal of cell science, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 19 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
19 citing papers in PubMed, 29 citations in OpenAlex.
- Regulation of Translation by PKA Signaling Pathway.International journal of molecular sciences · 2026Review
- Egg Overactivation-An Overlooked Phenomenon of Gamete Physiology.International journal of molecular sciences · 2025Review
- Structural, enzymatic and spatiotemporal regulation of PP2A-B55 phosphatase in the control of mitosis.Frontiers in cell and developmental biology · 2022Review
- Selective dephosphorylation by PP2A-B55 directs the meiosis I-meiosis II transition in oocytes.eLife · 2021Article
- The study of the determinants controlling Arpp19 phosphatase-inhibitory activity reveals an Arpp19/PP2A-B55 feedback loop.Nature communications · 2021Article
- The M-phase regulatory phosphatase PP2A-B55δ opposes protein kinase A on Arpp19 to initiate meiotic division.Nature communications · 2021Article
- Translational Control ofCells · 2020Review
- Review
- Understanding MAPK Signaling Pathways in Apoptosis.International journal of molecular sciences · 2020Review
- Dissection of the Ovulatory Process UsingFrontiers in cell and developmental biology · 2020Review
- The G2-to-M transition from a phosphatase perspective: a new vision of the meiotic division.Cell division · 2020Review
- Induction of a Spindle-Assembly-Competent M Phase in Xenopus Egg Extracts.Current biology : CB · 2019Article
- The greatwall kinase is dominant over PKA in controlling the antagonistic function of ARPP19 in Xenopus oocytes.Cell cycle (Georgetown, Tex.) · 2017Article
- Article
- Increased ARPP-19 expression is associated with hepatocellular carcinoma.International journal of molecular sciences · 2014Article
- Calcium signaling and meiotic exit at fertilization in Xenopus egg.International journal of molecular sciences · 2014Review
- Mastl is required for timely activation of APC/C in meiosis I and Cdk1 reactivation in meiosis II.The Journal of cell biology · 2014Article
- Phosphorylation of ARPP19 by protein kinase A prevents meiosis resumption in Xenopus oocytes.Nature communications · 2014Article
- α-endosulfine (ENSA) regulates exit from prophase I arrest in mouse oocytes.Cell cycle (Georgetown, Tex.) · 2014Article
Corrections and comments
- Correction · 2018-07-30Falsification/Fabrication of Image · Investigation by Company/Institution · Manipulation of Images · Objections by Third Party ·
- Erratum issued
Authors and funding
6 authors at 4 institutions in 2 countries.
Funding
Abstract
Entry into mitosis or meiosis relies on the coordinated action of kinases and phosphatases that ultimately leads to the activation of Cyclin-B-Cdk1, also known as MPF for M-phase promoting factor. Vertebrate oocytes are blocked in prophase of the first meiotic division, an arrest that is tightly controlled by high PKA activity. Re-entry into meiosis depends on activation of Cdk1, which obeys a two-step mechanism: a catalytic amount of Cdk1 is generated in a PKA and protein-synthesis-dependent manner; then a regulatory network known as the MPF auto-amplification loop is initiated. This second step is independent of PKA and protein synthesis. However, none of the molecular components of the auto-amplification loop identified so far act independently of PKA. Therefore, the protein rendering this process independent of PKA in oocytes remains unknown. Using a physiologically intact cell system, the Xenopus oocyte, we show that the phosphorylation of ARPP19 at S67 by the Greatwall kinase promotes its binding to the PP2A-B55δ phosphatase, thus inhibiting its activity. This process is controlled by Cdk1 and has an essential role within the Cdk1 auto-amplification loop for entry into the first meiotic division. Moreover, once phosphorylated by Greatwall, ARPP19 escapes the negative regulation exerted by PKA. It also promotes activation of MPF independently of protein synthesis, provided that a small amount of Mos is present. Taken together, these findings reveal that PP2A-B55δ, Greatwall and ARPP19 are not only required for entry into meiotic divisions, but are also pivotal effectors within the Cdk1 auto-regulatory loop responsible for its independence with respect to the PKA-negative control.
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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.