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The midbody interactome reveals unexpected roles for PP1 phosphatases in cytokinesis

Author

Listed:
  • Luisa Capalbo

    (University of Cambridge)

  • Zuni I. Bassi

    (University of Cambridge)

  • Marco Geymonat

    (University of Cambridge)

  • Sofia Todesca

    (University of Cambridge)

  • Liviu Copoiu

    (University of Cambridge
    University of Cambridge)

  • Anton J. Enright

    (University of Cambridge)

  • Giuliano Callaini

    (University of Siena)

  • Maria Giovanna Riparbelli

    (University of Siena)

  • Lu Yu

    (Wellcome Genome Campus
    The Institute of Cancer Research)

  • Jyoti S. Choudhary

    (Wellcome Genome Campus
    The Institute of Cancer Research)

  • Enrico Ferrero

    (University of Cambridge
    University of Cambridge
    Novartis Institutes for BioMedical Research)

  • Sally Wheatley

    (University of Nottingham)

  • Max E. Douglas

    (Wellcome Trust/Cancer Research UK Gurdon Institute
    The Francis Crick Institute)

  • Masanori Mishima

    (Wellcome Trust/Cancer Research UK Gurdon Institute
    Warwick Medical School, University of Warwick)

  • Pier Paolo D’Avino

    (University of Cambridge)

Abstract

The midbody is an organelle assembled at the intercellular bridge between the two daughter cells at the end of mitosis. It controls the final separation of the daughter cells and has been involved in cell fate, polarity, tissue organization, and cilium and lumen formation. Here, we report the characterization of the intricate midbody protein-protein interaction network (interactome), which identifies many previously unknown interactions and provides an extremely valuable resource for dissecting the multiple roles of the midbody. Initial analysis of this interactome revealed that PP1β-MYPT1 phosphatase regulates microtubule dynamics in late cytokinesis and de-phosphorylates the kinesin component MKLP1/KIF23 of the centralspindlin complex. This de-phosphorylation antagonizes Aurora B kinase to modify the functions and interactions of centralspindlin in late cytokinesis. Our findings expand the repertoire of PP1 functions during mitosis and indicate that spatiotemporal changes in the distribution of kinases and counteracting phosphatases finely tune the activity of cytokinesis proteins.

Suggested Citation

  • Luisa Capalbo & Zuni I. Bassi & Marco Geymonat & Sofia Todesca & Liviu Copoiu & Anton J. Enright & Giuliano Callaini & Maria Giovanna Riparbelli & Lu Yu & Jyoti S. Choudhary & Enrico Ferrero & Sally W, 2019. "The midbody interactome reveals unexpected roles for PP1 phosphatases in cytokinesis," Nature Communications, Nature, vol. 10(1), pages 1-17, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-019-12507-9
    DOI: 10.1038/s41467-019-12507-9
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    Cited by:

    1. Tamara Advedissian & Stéphane Frémont & Arnaud Echard, 2024. "Cytokinetic abscission requires actin-dependent microtubule severing," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    2. Gyu Ik Jung & Daniela Londoño-Vásquez & Sungjin Park & Ahna R. Skop & Ahmed Z. Balboula & Karen Schindler, 2023. "An oocyte meiotic midbody cap is required for developmental competence in mice," Nature Communications, Nature, vol. 14(1), pages 1-13, December.

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