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Two mechanisms repress cyclin B1 translation to maintain prophase arrest in mouse oocytes

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  • Shiya Cheng

    (Max Planck Institute for Multidisciplinary Sciences
    Wuhan University)

  • Melina Schuh

    (Max Planck Institute for Multidisciplinary Sciences
    University of Göttingen)

Abstract

In mammals, oocytes are arrested in prophase of meiosis I for long periods of time. Prophase arrest is critical for reproduction because it allows oocytes to grow to their full size to support meiotic maturation and embryonic development. Prophase arrest requires the inhibitory phosphorylation of the mitotic kinase CDK1. Whether prophase arrest is also regulated at the translational level is unknown. Here, we show that prophase arrest is regulated by translational control of dormant cyclin B1 mRNAs. Using Trim-Away, we identify two mechanisms that maintain cyclin B1 dormancy and thus prophase arrest. First, a complex of the RNA-binding proteins DDX6, LSM14B and CPEB1 directly represses cyclin B1 translation through interacting with its 3’UTR. Second, cytoplasmic poly(A)-binding proteins (PABPCs) indirectly repress the translation of cyclin B1 and other poly(A)-tail-less or short-tailed mRNAs by sequestering the translation machinery on long-tailed mRNAs. Together, we demonstrate how RNA-binding proteins coordinately regulate prophase arrest, and reveal an unexpected role for PABPCs in controlling mRNA dormancy.

Suggested Citation

  • Shiya Cheng & Melina Schuh, 2024. "Two mechanisms repress cyclin B1 translation to maintain prophase arrest in mouse oocytes," Nature Communications, Nature, vol. 15(1), pages 1-18, December.
    • Handle: RePEc:nat:natcom:v:15:y:2024:i:1:d:10.1038_s41467-024-54161-w
    DOI: 10.1038/s41467-024-54161-w
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    References listed on IDEAS

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    1. Sybille Pfender & Vitaliy Kuznetsov & Michał Pasternak & Thomas Tischer & Balaji Santhanam & Melina Schuh, 2015. "Live imaging RNAi screen reveals genes essential for meiosis in mammalian oocytes," Nature, Nature, vol. 524(7564), pages 239-242, August.
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