Pericentrin-mediated SAS-6 recruitment promotes centriole assembly
Autor(a) principal: | |
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Data de Publicação: | 2019 |
Outros Autores: | , , , , , , , |
Tipo de documento: | Artigo |
Idioma: | eng |
Título da fonte: | Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
Texto Completo: | http://hdl.handle.net/10400.7/899 |
Resumo: | The centrosome is composed of two centrioles surrounded by a microtubule-nucleating pericentriolar material (PCM). Although centrioles are known to regulate PCM assembly, it is less known whether and how the PCM contributes to centriole assembly. Here we investigate the interaction between centriole components and the PCM by taking advantage of fission yeast, which has a centriole-free, PCM-containing centrosome, the SPB. Surprisingly, we observed that several ectopically-expressed animal centriole components such as SAS-6 are recruited to the SPB. We revealed that a conserved PCM component, Pcp1/pericentrin, interacts with and recruits SAS-6. This interaction is conserved and important for centriole assembly, particularly its elongation. We further explored how yeasts kept this interaction even after centriole loss and showed that the conserved calmodulin-binding region of Pcp1/pericentrin is critical for SAS-6 interaction. Our work suggests that the PCM not only recruits and concentrates microtubule-nucleators, but also the centriole assembly machinery, promoting biogenesis close by. |
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Repositório Científico de Acesso Aberto de Portugal (Repositórios Cientìficos) |
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spelling |
Pericentrin-mediated SAS-6 recruitment promotes centriole assemblyThe centrosome is composed of two centrioles surrounded by a microtubule-nucleating pericentriolar material (PCM). Although centrioles are known to regulate PCM assembly, it is less known whether and how the PCM contributes to centriole assembly. Here we investigate the interaction between centriole components and the PCM by taking advantage of fission yeast, which has a centriole-free, PCM-containing centrosome, the SPB. Surprisingly, we observed that several ectopically-expressed animal centriole components such as SAS-6 are recruited to the SPB. We revealed that a conserved PCM component, Pcp1/pericentrin, interacts with and recruits SAS-6. This interaction is conserved and important for centriole assembly, particularly its elongation. We further explored how yeasts kept this interaction even after centriole loss and showed that the conserved calmodulin-binding region of Pcp1/pericentrin is critical for SAS-6 interaction. Our work suggests that the PCM not only recruits and concentrates microtubule-nucleators, but also the centriole assembly machinery, promoting biogenesis close by.ARCAIto, DaisukeZitouni, SihemJana, Swadhin ChandraDuarte, PauloSurkont, JaroslawCarvalho-Santos, ZitaPereira-Leal, José BFerreira, Miguel GodinhoBettencourt-Dias, Mónica2019-07-25T13:51:06Z20192019-01-01T00:00:00Zinfo:eu-repo/semantics/publishedVersioninfo:eu-repo/semantics/articleapplication/pdfhttp://hdl.handle.net/10400.7/899eng10.7554/eLife.41418info: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:RCAAP2022-11-29T14:35:18ZPortal AgregadorONG |
dc.title.none.fl_str_mv |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly |
title |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly |
spellingShingle |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly Ito, Daisuke |
title_short |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly |
title_full |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly |
title_fullStr |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly |
title_full_unstemmed |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly |
title_sort |
Pericentrin-mediated SAS-6 recruitment promotes centriole assembly |
author |
Ito, Daisuke |
author_facet |
Ito, Daisuke Zitouni, Sihem Jana, Swadhin Chandra Duarte, Paulo Surkont, Jaroslaw Carvalho-Santos, Zita Pereira-Leal, José B Ferreira, Miguel Godinho Bettencourt-Dias, Mónica |
author_role |
author |
author2 |
Zitouni, Sihem Jana, Swadhin Chandra Duarte, Paulo Surkont, Jaroslaw Carvalho-Santos, Zita Pereira-Leal, José B Ferreira, Miguel Godinho Bettencourt-Dias, Mónica |
author2_role |
author author author author author author author author |
dc.contributor.none.fl_str_mv |
ARCA |
dc.contributor.author.fl_str_mv |
Ito, Daisuke Zitouni, Sihem Jana, Swadhin Chandra Duarte, Paulo Surkont, Jaroslaw Carvalho-Santos, Zita Pereira-Leal, José B Ferreira, Miguel Godinho Bettencourt-Dias, Mónica |
description |
The centrosome is composed of two centrioles surrounded by a microtubule-nucleating pericentriolar material (PCM). Although centrioles are known to regulate PCM assembly, it is less known whether and how the PCM contributes to centriole assembly. Here we investigate the interaction between centriole components and the PCM by taking advantage of fission yeast, which has a centriole-free, PCM-containing centrosome, the SPB. Surprisingly, we observed that several ectopically-expressed animal centriole components such as SAS-6 are recruited to the SPB. We revealed that a conserved PCM component, Pcp1/pericentrin, interacts with and recruits SAS-6. This interaction is conserved and important for centriole assembly, particularly its elongation. We further explored how yeasts kept this interaction even after centriole loss and showed that the conserved calmodulin-binding region of Pcp1/pericentrin is critical for SAS-6 interaction. Our work suggests that the PCM not only recruits and concentrates microtubule-nucleators, but also the centriole assembly machinery, promoting biogenesis close by. |
publishDate |
2019 |
dc.date.none.fl_str_mv |
2019-07-25T13:51:06Z 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 |
http://hdl.handle.net/10400.7/899 |
url |
http://hdl.handle.net/10400.7/899 |
dc.language.iso.fl_str_mv |
eng |
language |
eng |
dc.relation.none.fl_str_mv |
10.7554/eLife.41418 |
dc.rights.driver.fl_str_mv |
info:eu-repo/semantics/openAccess |
eu_rights_str_mv |
openAccess |
dc.format.none.fl_str_mv |
application/pdf |
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 |
institution |
RCAAP |
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 |
|
repository.mail.fl_str_mv |
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_version_ |
1777301595145371648 |