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Kinase-controlled phase transition of membraneless organelles in mitosis

Author

Listed:
  • Arpan Kumar Rai

    (University of Zurich)

  • Jia-Xuan Chen

    (Max Delbrück Center for Molecular Medicine
    University of Cambridge)

  • Matthias Selbach

    (Max Delbrück Center for Molecular Medicine
    Charité-Universitätsmedizin Berlin)

  • Lucas Pelkmans

    (University of Zurich)

Abstract

Liquid–liquid phase separation has been shown to underlie the formation and disassembly of membraneless organelles in cells, but the cellular mechanisms that control this phenomenon are poorly understood. A prominent example of regulated and reversible segregation of liquid phases may occur during mitosis, when membraneless organelles disappear upon nuclear-envelope breakdown and reappear as mitosis is completed. Here we show that the dual-specificity kinase DYRK3 acts as a central dissolvase of several types of membraneless organelle during mitosis. DYRK3 kinase activity is essential to prevent the unmixing of the mitotic cytoplasm into aberrant liquid-like hybrid organelles and the over-nucleation of spindle bodies. Our work supports a mechanism in which the dilution of phase-separating proteins during nuclear-envelope breakdown and the DYRK3-dependent degree of their solubility combine to allow cells to dissolve and condense several membraneless organelles during mitosis.

Suggested Citation

  • Arpan Kumar Rai & Jia-Xuan Chen & Matthias Selbach & Lucas Pelkmans, 2018. "Kinase-controlled phase transition of membraneless organelles in mitosis," Nature, Nature, vol. 559(7713), pages 211-216, July.
    • Handle: RePEc:nat:nature:v:559:y:2018:i:7713:d:10.1038_s41586-018-0279-8
    DOI: 10.1038/s41586-018-0279-8
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    Cited by:

    1. Juan Manuel Valverde & Geronimo Dubra & Michael Phillips & Austin Haider & Carlos Elena-Real & Aurélie Fournet & Emile Alghoul & Dhanvantri Chahar & Nuria Andrés-Sanchez & Matteo Paloni & Pau Bernadó , 2023. "A cyclin-dependent kinase-mediated phosphorylation switch of disordered protein condensation," Nature Communications, Nature, vol. 14(1), pages 1-23, December.
    2. Lennart Enders & Marton Siklos & Jan Borggräfe & Stefan Gaussmann & Anna Koren & Monika Malik & Tatjana Tomek & Michael Schuster & Jiří Reiniš & Elisa Hahn & Andrea Rukavina & Andreas Reicher & Tamara, 2023. "Pharmacological perturbation of the phase-separating protein SMNDC1," Nature Communications, Nature, vol. 14(1), pages 1-19, December.
    3. Mathieu Cayla & Christos Spanos & Kirsty McWilliam & Eliza Waskett & Juri Rappsilber & Keith R. Matthews, 2024. "Differentiation granules, a dynamic regulator of T. brucei development," Nature Communications, Nature, vol. 15(1), pages 1-16, December.
    4. Halima H. Schede & Pradeep Natarajan & Arup K. Chakraborty & Krishna Shrinivas, 2023. "A model for organization and regulation of nuclear condensates by gene activity," Nature Communications, Nature, vol. 14(1), pages 1-15, December.
    5. Santiago Martínez-Lumbreras & Lena K. Träger & Miriam M. Mulorz & Marco Payr & Varvara Dikaya & Clara Hipp & Julian König & Michael Sattler, 2024. "Intramolecular autoinhibition regulates the selectivity of PRPF40A tandem WW domains for proline-rich motifs," Nature Communications, Nature, vol. 15(1), pages 1-17, December.
    6. Min Lee & Hyungseok C. Moon & Hyeonjeong Jeong & Dong Wook Kim & Hye Yoon Park & Yongdae Shin, 2024. "Optogenetic control of mRNA condensation reveals an intimate link between condensate material properties and functions," Nature Communications, Nature, vol. 15(1), pages 1-14, December.
    7. Jorine M. Eeftens & Manya Kapoor & Davide Michieletto & Clifford P. Brangwynne, 2021. "Polycomb condensates can promote epigenetic marks but are not required for sustained chromatin compaction," Nature Communications, Nature, vol. 12(1), pages 1-12, December.

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