ArticleThe EMBO journal2024
The global phosphorylation landscape of mouse oocytes during meiotic maturation.
Article in The EMBO journal, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Article
- Attribute Network-based Ranking (ANeR) identifies conserved translational fingerprints of M-phase.Nucleic acids research · 2026Article
- Proteomics-based insights into mammalian oocyte and early embryo development.Nature cell biology · 2026Review
- 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
- hnRNPU Safeguards Oocyte Development and Female Fertility via Regulation of Alternative Splicing.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- Stage-Resolved Phosphoproteomic Landscape of Mouse Spermiogenesis Reveals Key Kinase Signaling in Sperm Morphogenesis.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- RAS/ERK signaling and PLK1: Coordinating developmental regulation and disease mechanisms.Current opinion in cell biology · 2025Review
- Decoding protein phosphorylation during oocyte meiotic divisions using phosphoproteomics.eLife · 2025Article
- Protein-targeting reverse genetic approaches: the future of oocyte and preimplantation embryo research.Molecular human reproduction · 2025Review
- Absence of CDK12 in oocyte leads to female infertility.Cell death & disease · 2025Article
- No transcription, no problem: Protein phosphorylation changes and the transition from oocyte to embryo.Current topics in developmental biology · 2025Review
Corrections and comments
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Authors and funding
16 authors.
Funding
Abstract
Phosphorylation is a key post-translational modification regulating protein function and biological outcomes. However, the phosphorylation dynamics orchestrating mammalian oocyte development remains poorly understood. In the present study, we apply high-resolution mass spectrometry-based phosphoproteomics to obtain the first global in vivo quantification of mouse oocyte phosphorylation. Of more than 8000 phosphosites, 75% significantly oscillate and 64% exhibit marked upregulation during meiotic maturation, indicative of the dominant regulatory role. Moreover, we identify numerous novel phosphosites on oocyte proteins and a few highly conserved phosphosites in oocytes from different species. Through functional perturbations, we demonstrate that phosphorylation status of specific sites participates in modulating critical events including metabolism, translation, and RNA processing during meiosis. Finally, we combine inhibitor screening and enzyme-substrate network prediction to discover previously unexplored kinases and phosphatases that are essential for oocyte maturation. In sum, our data define landscape of the oocyte phosphoproteome, enabling in-depth mechanistic insights into developmental control of germ cells.
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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.