Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity

Detalhes bibliográficos
Autor(a) principal: Vitiello, E
Data de Publicação: 2019
Outros Autores: Moreau, P, Nunes, V, Mettouchi, A, Maiato, H, Ferreira, JG, Wang, I, Balland, M
Tipo de documento: Artigo
Idioma: eng
Título da fonte: Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
Texto Completo: https://hdl.handle.net/10216/136235
Resumo: 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.
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spelling Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelityThe 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.Nature Publishing Group20192019-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttps://hdl.handle.net/10216/136235eng2041-172310.1038/s41467-018-07965-6Vitiello, EMoreau, PNunes, VMettouchi, AMaiato, HFerreira, JGWang, IBalland, Minfo:eu-repo/semantics/openAccessreponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãoinstacron:RCAAP2023-11-29T12:56:26Zoai:repositorio-aberto.up.pt:10216/136235Portal AgregadorONGhttps://www.rcaap.pt/oai/openaireopendoar:71602024-03-19T23:30:00.733599Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informaçãofalse
dc.title.none.fl_str_mv Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
title Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
spellingShingle Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
Vitiello, E
title_short Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
title_full Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
title_fullStr Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
title_full_unstemmed Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
title_sort Acto-myosin force organization modulates centriole separation and PLK4 recruitment to ensure centriole fidelity
author Vitiello, E
author_facet Vitiello, E
Moreau, P
Nunes, V
Mettouchi, A
Maiato, H
Ferreira, JG
Wang, I
Balland, M
author_role author
author2 Moreau, P
Nunes, V
Mettouchi, A
Maiato, H
Ferreira, JG
Wang, I
Balland, M
author2_role author
author
author
author
author
author
author
dc.contributor.author.fl_str_mv Vitiello, E
Moreau, P
Nunes, V
Mettouchi, A
Maiato, H
Ferreira, JG
Wang, I
Balland, M
description 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.
publishDate 2019
dc.date.none.fl_str_mv 2019
2019-01-01T00:00:00Z
dc.type.status.fl_str_mv info:eu-repo/semantics/publishedVersion
dc.type.driver.fl_str_mv info:eu-repo/semantics/article
format article
status_str publishedVersion
dc.identifier.uri.fl_str_mv https://hdl.handle.net/10216/136235
url https://hdl.handle.net/10216/136235
dc.language.iso.fl_str_mv eng
language eng
dc.relation.none.fl_str_mv 2041-1723
10.1038/s41467-018-07965-6
dc.rights.driver.fl_str_mv info:eu-repo/semantics/openAccess
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dc.format.none.fl_str_mv application/pdf
dc.publisher.none.fl_str_mv Nature Publishing Group
publisher.none.fl_str_mv Nature Publishing Group
dc.source.none.fl_str_mv reponame:Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
instname:Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron:RCAAP
instname_str Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
instacron_str RCAAP
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reponame_str Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
collection Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos)
repository.name.fl_str_mv Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) - Agência para a Sociedade do Conhecimento (UMIC) - FCT - Sociedade da Informação
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