ArticleMolecular biology of the cell2001
Cyclin B/cdc2 induces c-Mos stability by direct phosphorylation in Xenopus oocytes.
Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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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
32 citing papers in PubMed, 69 citations in OpenAlex.
- Greatwall depletion from Xenopus oocytes reveals a key role of the cyclin B/CDK1-PP2A-B55 balance in the coordination of meiotic events.Nature communications · 2026Article
- Translational repression by 4E-T is crucial to maintain the prophase-I arrest in vertebrate oocytes.Nature communications · 2025Article
- Egg Overactivation-An Overlooked Phenomenon of Gamete Physiology.International journal of molecular sciences · 2025Review
- Multiple intersecting pathways are involved in CPEB1 phosphorylation and regulation of translation during mouse oocyte meiosis.Development (Cambridge, England) · 2024Article
- Multiple intersecting pathways are involved in the phosphorylation of CPEB1 to activate translation during mouse oocyte meiosis.bioRxiv : the preprint server for biology · 2024Article
- Egg Development AfterThe journal of poultry science · 2023Article
- Regulation of oocyte maturation: Role of conserved ERK signaling.Molecular reproduction and development · 2022Review
- Translational Control ofCells · 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
- In Vitro Reconstruction ofInternational journal of molecular sciences · 2019Article
- Effect of Kisspeptin on the Developmental Competence and Early Transcript Expression in Porcine Oocytes Parthenogenetically Activated with Different Methods.BioMed research international · 2018Article
- Positive mRNA Translational Control in Germ Cells by Initiation Factor Selectivity.BioMed research international · 2015Review
- Transmembrane signal transduction in oocyte maturation and fertilization: focusing on Xenopus laevis as a model animal.International journal of molecular sciences · 2014Review
- Calcium signaling and meiotic exit at fertilization in Xenopus egg.International journal of molecular sciences · 2014Review
- Paxillin and steroid signaling: from frog to human.Methods in molecular biology (Clifton, N.J.) · 2014Article
- Release from meiotic arrest in ascidian eggs requires the activity of two phosphatases but not CaMKII.Development (Cambridge, England) · 2013Article
- Autoregulation of Musashi1 mRNA translation during Xenopus oocyte maturation.Molecular reproduction and development · 2012Article
- Nitric oxide-donor SNAP induces Xenopus eggs activation.PloS one · 2012Article
- Characterization of the mechanisms controlling Greatwall activity.Molecular and cellular biology · 2011Article
Corrections and comments
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The c-Mos proto-oncogene product plays an essential role during meiotic divisions in vertebrate eggs. In Xenopus, it is required for progression of oocyte maturation and meiotic arrest of unfertilized eggs. Its degradation after fertilization is essential to early embryogenesis. In this study we investigated the mechanisms involved in c-Mos degradation. We present in vivo evidence for ubiquitin-dependent degradation of c-Mos in activated eggs. We found that c-Mos degradation is not directly dependent on the anaphase-promoting factor activator Fizzy/cdc20 but requires cyclin degradation. We demonstrate that cyclin B/cdc2 controls in vivo c-Mos phosphorylation and stabilization. Moreover, we show that cyclin B/cdc2 is capable of directly phosphorylating c-Mos in vitro, inducing a similar mobility shift to the one observed in vivo. Tryptic phosphopeptide analysis revealed a practically identical in vivo and in vitro phosphopeptide map and allowed identification of serine-3 as the largely preferential phosphorylation site as previously described (Freeman et al., 1992). Altogether, these results demonstrate that, in vivo, stability of c-Mos is directly regulated by cyclin B/cdc2 kinase activity.
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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.