Evidence map›Paper›PMID 31586073›Full record

ArticleNature communications2019

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 and 5 more

Open access · goldAbstract readVideo-Audio Media
In one paragraph

Article in Nature communications, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.

0numbers the graph read from it
0cells of the map it votes in
65citing papers in PubMed
7.4field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

65 citing papers in PubMed, 124 citations in OpenAlex.

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5 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

15 authors at 7 institutions in 3 countries.

Luisa CapalboDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.
Zuni I BassiDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.ORCID http://orcid.org/0000-0003-4309-9656
Marco GeymonatDepartment of Genetics, University of Cambridge, Downing Street, Cambridge, CB2 3EH, UK.
Sofia TodescaDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.ORCID http://orcid.org/0000-0002-8841-7008
Liviu CopoiuDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.ORCID http://orcid.org/0000-0001-9329-114X
Anton J EnrightDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK.
Giuliano CallainiDepartment of Medical Biotechnologies, University of Siena, Via A. Moro 4, 53100, Siena, Italy.
Maria Giovanna RiparbelliDepartment of Life Sciences, University of Siena, Via A. Moro 4, 53100, Siena, Italy.
Lu YuThe Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, CB10 1SA, UK.
Jyoti S ChoudharyThe Wellcome Trust Sanger Institute, Wellcome Genome Campus, Hinxton, CB10 1SA, UK.ORCID http://orcid.org/0000-0003-0881-5477
Enrico FerreroDepartment of Genetics, University of Cambridge, Downing Street, Cambridge, CB2 3EH, UK.ORCID http://orcid.org/0000-0002-8362-100X
Sally WheatleySchool of Life Sciences, University of Nottingham, Nottingham, NG7 2UH, UK.ORCID http://orcid.org/0000-0002-9550-8979
Max E DouglasWellcome Trust/Cancer Research UK Gurdon Institute, Cambridge, CB2 1QN, UK.
Masanori MishimaWellcome Trust/Cancer Research UK Gurdon Institute, Cambridge, CB2 1QN, UK.
Pier Paolo D'AvinoDepartment of Pathology, University of Cambridge, Tennis Court Road, Cambridge, CB2 1QP, UK. ppd21@cam.ac.uk.
University of Cambridge · GBInstitute of Cancer Research · GBUniversity of Siena · ITNovartis (Switzerland) · CHThe Francis Crick Institute · GBThe Gurdon Institute · GBUniversity of Nottingham · GB

Funding

Biotechnology and Biological Sciences Research Council BB/R001227/1Cancer Research UK 11985Cancer Research UK C309/A25144
6 · The paper itself

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.

Indexed as

Aurora Kinase BBinding SitesCytokinesisHeLa CellsHumansIntravital MicroscopyMicrotubule-Associated ProteinsMicrotubulesMitosisMutagenesis, Site-DirectedMyosin-Light-Chain PhosphatasePhosphorylationProtein Interaction MapsProtein Phosphatase 1RNA, Small InterferingSpindle ApparatusAURKB protein, humanAurora Kinase BKIF23 protein, humanMicrotubule-Associated ProteinsMyosin-Light-Chain PhosphatasePPP1R12A protein, humanProtein Phosphatase 1RNA, Small Interfering

Identifiers

PMID31586073
PMCPMC6778137
OpenAlexW2979077645

What OpenQuestion holds

Textmetadata
LicenceCC BY
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.