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The midbody interactome reveals unexpected roles for PP1 phosphatases in cytokinesis.

Accepted version
Peer-reviewed

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Authors

Capalbo, Luisa 
Geymonat, Marco 

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.

Description

Keywords

Aurora Kinase B, Binding Sites, Cytokinesis, HeLa Cells, Humans, Intravital Microscopy, Microtubule-Associated Proteins, Microtubules, Mitosis, Mutagenesis, Site-Directed, Myosin-Light-Chain Phosphatase, Phosphorylation, Protein Interaction Maps, Protein Phosphatase 1, RNA, Small Interfering, Spindle Apparatus, Time-Lapse Imaging

Journal Title

Nat Commun

Conference Name

Journal ISSN

2041-1723
2041-1723

Volume Title

10

Publisher

Springer Science and Business Media LLC

Rights

All rights reserved
Sponsorship
Biotechnology and Biological Sciences Research Council (BB/R001227/1)
Cancer Research UK (C19769/A11985)
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