Author
Listed:
- Elisa Vitiello
(Domaine universitaire)
- Philippe Moreau
(Domaine universitaire)
- Vanessa Nunes
(Universidade do Porto
Universidade do Porto)
- Amel Mettouchi
(Institut Pasteur, Département de Microbiologie, Unité des Toxines Bactériennes, Université Paris Descartes)
- Helder Maiato
(Universidade do Porto
Universidade do Porto
Universidade do Porto, Alameda Prof. Hernâni Monteiro)
- Jorge G. Ferreira
(Universidade do Porto
Universidade do Porto
Universidade do Porto, Alameda Prof. Hernâni Monteiro)
- Irène Wang
(Domaine universitaire)
- Martial Balland
(Domaine universitaire)
Abstract
The presence of aberrant number of centrioles is a recognized cause of aneuploidy and hallmark of cancer. Hence, centriole duplication needs to be tightly regulated. It has been proposed that centriole separation limits centrosome duplication. The mechanism driving centriole separation is poorly understood and little is known on how this is linked to centriole duplication. Here, we propose that actin-generated forces regulate centriole separation. By imposing geometric constraints via micropatterns, we were able to prove that precise acto-myosin force arrangements control direction, distance and time of centriole separation. Accordingly, inhibition of acto-myosin contractility impairs centriole separation. Alongside, we observed that organization of acto-myosin force modulates specifically the length of S-G2 phases of the cell cycle, PLK4 recruitment at the centrosome and centriole fidelity. These discoveries led us to suggest that acto-myosin forces might act in fundamental mechanisms of aneuploidy prevention.
Suggested Citation
Elisa Vitiello & Philippe Moreau & Vanessa Nunes & Amel Mettouchi & Helder Maiato & Jorge G. Ferreira & Irène Wang & Martial Balland, 2019.
"Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity,"
Nature Communications, Nature, vol. 10(1), pages 1-12, December.
Handle:
RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-07965-6
DOI: 10.1038/s41467-018-07965-6
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