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Cytoplasmic cleavage of DPPA3 is required for intracellular trafficking and cleavage-stage development in mice

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  • Seung-Wook Shin

    (NIDDK, National Institutes of Health)

  • Edgar John Vogt

    (NIDDK, National Institutes of Health)

  • Maria Jimenez-Movilla

    (Medical School, University of Murcia, IMIB)

  • Boris Baibakov

    (NIDDK, National Institutes of Health)

  • Jurrien Dean

    (NIDDK, National Institutes of Health)

Abstract

Degradation of maternal proteins by the ubiquitin-proteasome system (UPS) accompanies the maternal-to-zygotic transition. DPPA3/Stella/PGC7, encoded by a maternal effect gene, is present in the nucleus and cytoplasm of zygotes and has been associated with protecting the female pronucleus from TET3-mediated demethylation. We now report that cytoplasmic DPPA3 is partially cleaved by the ubiquitin-proteasome system and an N-terminus fragment remains in the cytoplasm where it associates with early and re-cycling endosomes. If DPPA3 is absent or if cleavage is prevented, multiple vesicles coalesce/aggregate and markers of lysosomes are decreased. Fertilized eggs develop poorly into blastocysts, which results in significantly decreased fecundity of Dppa3 R60A transgenic mice. This phenocopies aspects of Lamp1/2 knockdowns and Dppa3 KO embryos can be partially rescued in vitro by DPPA31–60 and to a lesser extent by LAMP1/2. Thus, the N-terminus of DPPA3 has a significant role in cytoplasmic vesicular trafficking in addition to its previously reported nuclear function.

Suggested Citation

  • Seung-Wook Shin & Edgar John Vogt & Maria Jimenez-Movilla & Boris Baibakov & Jurrien Dean, 2017. "Cytoplasmic cleavage of DPPA3 is required for intracellular trafficking and cleavage-stage development in mice," Nature Communications, Nature, vol. 8(1), pages 1-12, December.
    • Handle: RePEc:nat:natcom:v:8:y:2017:i:1:d:10.1038_s41467-017-01387-6
    DOI: 10.1038/s41467-017-01387-6
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