ArticleCell communication and signaling : CCS2024
PGC7 regulates maternal mRNA translation via AKT1-YBX1 interactions in mouse oocytes.
Article in Cell communication and signaling : CCS, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed.
- Emerging roles of RNA N5-methylcytosine modification in reproductive physiology and gynecological diseases.Epigenetics · 2026Review
- Phosphorylation of YBX1 in the Kidneys is Altered in Legumain Knockout-Mice.Journal of proteome research · 2026Article
- 5-Methylcytidine RNA Epitranscriptomics in Women's Health and Disease: Mechanisms and Clinical Implications.Cells · 2026Review
- Translational Fidelity Decline in the Aging Oocyte and Embryo Development.International journal of molecular sciences · 2026Review
- Harnessing cuproptosis: a new avenue for targeted cancer therapies.Apoptosis : an international journal on programmed cell death · 2025Review
- Ybx1 deficiency impairs spermatid development and male fertility without affecting meiosis in mice: insights into spermatogenesis.The Journal of reproduction and development · 2025Article
- PGC7 maintains the pluripotency of F9 embryonic carcinoma cells by promoting Nanog translation.Acta biochimica et biophysica Sinica · 2025Article
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Authors and funding
8 authors.
Funding
Abstract
Timely and accurate translation of maternal mRNA is essential for oocyte maturation and early embryonic development. Previous studies have highlighted the importance of Primordial Germ cell 7 (PGC7) as a maternal factor in maintaining DNA methylation of maternally imprinted loci in zygotes. However, it is still unknown whether PGC7 is involved in the regulation of Maternal mRNA Translation. In this study, we have identified that PGC7-AKT1-YBX1 axis is involved in promoting the translation of maternal mRNAs. PGC7 not only sustains AKT1 activity by counteracting PP2A dephosphorylation and facilitating PDK1-AKT1 binding but also assists AKT1 in phosphorylating the translation inhibitor YBX1. In the absence of PGC7, despite increased PIK3CA expression and AKT1 phosphorylation, AKT1 is unable to phosphorylate YBX1. PGC7 facilitates the interaction between AKT1 and YBX1, enhancing YBX1-Serine 100 phosphorylation, which leads to YBX1 dissociation from eIF4E, thereby activating the translation of maternal Cyclin B1 and YAP1. The findings demonstrate the indispensability of PGC7 for translation activation in mammalian oocytes and provide a potential network regulated by PGC7 in early oogenesis.
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