Evidence map›Paper›PMID 28100664›Full record

ArticleOpen biology2017

Rab1 interacts with GOLPH3 and controls Golgi structure and contractile ring constriction during cytokinesis in Drosophila melanogaster.

Stefano Sechi, Anna Frappaolo, Roberta Fraschini, Luisa Capalbo, Marco Gottardo, Giorgio Belloni, David M Glover, Alan Wainman, Maria Grazia Giansanti

Open access · goldAbstract read
In one paragraph

Article in Open biology, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
2.3field-weighted citation impact, top 13% 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

28 citing papers in PubMed, 41 citations in OpenAlex.

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  14. Endosomal Rab GTPases regulate secretory granule maturation inCommunicative & integrative biology · 2021
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  20. Development (Cambridge, England) · 2019
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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

9 authors at 5 institutions in 2 countries.

Stefano SechiIstituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Biologia e Biotecnologie, Università Sapienza di Roma, Piazzale A. Moro 5, 00185 Roma, Italy.
Anna FrappaoloIstituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Biologia e Biotecnologie, Università Sapienza di Roma, Piazzale A. Moro 5, 00185 Roma, Italy.
Roberta FraschiniDipartimento di Biotecnologie e Bioscienze, Università degli studi di Milano Bicocca, Piazza della Scienza 2, 20126 Milan, Italy.
Luisa CapalboDepartment of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, UK.
Marco GottardoDipartimento di Scienze della Vita, Università di Siena, Via A. Moro 2, 53100 Siena, Italy.
Giorgio BelloniIstituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Biologia e Biotecnologie, Università Sapienza di Roma, Piazzale A. Moro 5, 00185 Roma, Italy.
David M GloverDepartment of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, UK.
Alan WainmanSir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK alan.wainman@path.ox.ac.uk.ORCID 0000-0002-6292-4183
Maria Grazia GiansantiIstituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Biologia e Biotecnologie, Università Sapienza di Roma, Piazzale A. Moro 5, 00185 Roma, Italy mariagrazia.giansanti@uniroma1.it.ORCID 0000-0002-6753-7262
Institute of Molecular Biology and Pathology · ITUniversity of Cambridge · GBUniversity of Milano-Bicocca · ITUniversity of Oxford · GBUniversity of Siena · IT

Funding

Cancer Research UK RG78567Wellcome TrustWellcome Trust 107457
6 · The paper itself

Abstract

Cytokinesis requires a tight coordination between actomyosin ring constriction and new membrane addition along the ingressing cleavage furrow. However, the molecular mechanisms underlying vesicle trafficking to the equatorial site and how this process is coupled with the dynamics of the contractile apparatus are poorly defined. Here we provide evidence for the requirement of Rab1 during cleavage furrow ingression in cytokinesis. We demonstrate that the gene omelette (omt) encodes the Drosophila orthologue of human Rab1 and is required for successful cytokinesis in both mitotic and meiotic dividing cells of Drosophila melanogaster We show that Rab1 protein colocalizes with the conserved oligomeric Golgi (COG) complex Cog7 subunit and the phosphatidylinositol 4-phosphate effector GOLPH3 at the Golgi stacks. Analysis by transmission electron microscopy and 3D-SIM super-resolution microscopy reveals loss of normal Golgi architecture in omt mutant spermatocytes indicating a role for Rab1 in Golgi formation. In dividing cells, Rab1 enables stabilization and contraction of actomyosin rings. We further demonstrate that GTP-bound Rab1 directly interacts with GOLPH3 and controls its localization at the Golgi and at the cleavage site. We propose that Rab1, by associating with GOLPH3, controls membrane trafficking and contractile ring constriction during cytokinesis.

Indexed as

AnimalsCell MembraneCytokinesisDrosophila melanogasterDrosophila ProteinsGolgi ApparatusMaleMembrane ProteinsOncogene ProteinsProtein Transportrab1 GTP-Binding Proteinsrab GTP-Binding ProteinsSpermatocytesDrosophila ProteinsMembrane ProteinsOncogene Proteinsrab1 GTP-Binding ProteinsRab1 protein, Drosophilarab GTP-Binding Proteinssau protein, DrosophilacytokinesisDrosophilaGolgiRab1

Identifiers

PMID28100664
PMCPMC5303273
OpenAlexW2578667190

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.