The midbody interactome reveals unexpected roles for PP1 phosphatases in cytokinesis.
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Date
2019-10-04Author
Capalbo, L
Bassi, ZI
Geymonat, M
Todesca, S
Copoiu, L
Enright, AJ
Callaini, G
Riparbelli, MG
Yu, L
Choudhary, JS
Ferrero, E
Wheatley, S
Douglas, ME
Mishima, M
D'Avino, PP
Type
Journal Article
Metadata
Show full item recordAbstract
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.
Collections
Subject
Hela Cells
Microtubules
Humans
Myosin-Light-Chain Phosphatase
Microtubule-Associated Proteins
RNA, Small Interfering
Mutagenesis, Site-Directed
Cytokinesis
Mitosis
Binding Sites
Phosphorylation
Protein Phosphatase 1
Time-Lapse Imaging
Protein Interaction Maps
Spindle Apparatus
Aurora Kinase B
Intravital Microscopy
Research team
Telomere Biology
Language
eng
Date accepted
2019-09-13
License start date
2019-10-04
Citation
Nature communications, 2019, 10 (1), pp. 4513 - ?
Publisher
NATURE PUBLISHING GROUP