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The midbody interactome reveals unexpected roles for PP1 phosphatases in cytokinesis

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 Wheatley, Max E. Douglas, Masanori Mishima and Pier Paolo D’Avino ()
Additional contact information
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
Anton J. Enright: University of Cambridge
Giuliano Callaini: University of Siena
Maria Giovanna Riparbelli: University of Siena
Lu Yu: Wellcome Genome Campus
Jyoti S. Choudhary: Wellcome Genome Campus
Enrico Ferrero: University of Cambridge
Sally Wheatley: University of Nottingham
Max E. Douglas: Wellcome Trust/Cancer Research UK Gurdon Institute
Masanori Mishima: Wellcome Trust/Cancer Research UK Gurdon Institute
Pier Paolo D’Avino: University of Cambridge

Nature Communications, 2019, vol. 10, issue 1, 1-17

Abstract: 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.

Date: 2019
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DOI: 10.1038/s41467-019-12507-9

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