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Open Biol. 2017 Jan;7(1). pii: 160257. doi: 10.1098/rsob.160257.

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

Author information

1
Istituto di Biologia e Patologia Molecolari del CNR, Dipartimento di Biologia e Biotecnologie, Università Sapienza di Roma, Piazzale A. Moro 5, 00185 Roma, Italy.
2
Dipartimento di Biotecnologie e Bioscienze, Università degli studi di Milano Bicocca, Piazza della Scienza 2, 20126 Milan, Italy.
3
Department of Genetics, University of Cambridge, Downing Street, Cambridge CB2 3EH, UK.
4
Dipartimento di Scienze della Vita, Università di Siena, Via A. Moro 2, 53100 Siena, Italy.
5
Sir William Dunn School of Pathology, University of Oxford, South Parks Road, Oxford OX1 3RE, UK alan.wainman@path.ox.ac.uk.
6
Istituto 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.

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.

KEYWORDS:

Drosophila; Golgi; Rab1; cytokinesis

PMID:
28100664
PMCID:
PMC5303273
DOI:
10.1098/rsob.160257
[Indexed for MEDLINE]
Free PMC Article

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