Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset

59 páginas 5 figuras, 1 tabla

Detalles Bibliográficos
Autores: Játiva, Soraya, Calabria, Ines, Moyano-Rodríguez, Yolanda, García, Patricia, Queralt, Ethel
Tipo de recurso: artículo
Estado:Versión aceptada para publicación
Fecha de publicación:2019
País:España
Institución:Consejo Superior de Investigaciones Científicas (CSIC)
Repositorio:DIGITAL.CSIC. Repositorio Institucional del CSIC
OAI Identifier:oai:digital.csic.es:10261/272414
Acceso en línea:http://hdl.handle.net/10261/272414
Access Level:acceso abierto
Palabra clave:Cell cycle
FEAR
Mitosis
Mitotic exit
PP2A–Cdc55
Phosphatases
Separase
Zds1
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network_acronym_str ES
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repository_id_str
spelling Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onsetJátiva, SorayaCalabria, InesMoyano-Rodríguez, YolandaGarcía, PatriciaQueralt, EthelCell cycleFEARMitosisMitotic exitPP2A–Cdc55PhosphatasesSeparaseZds159 páginas 5 figuras, 1 tablaExit from mitosis and completion of cytokinesis require the inactivation of mitotic cyclin-dependent kinase (Cdk) activity. In budding yeast, Cdc14 phosphatase is a key mitotic regulator that is activated in anaphase to counteract Cdk activity. In metaphase, Cdc14 is kept inactive in the nucleolus, where it is sequestered by its inhibitor, Net1. At anaphase onset, downregulation of PP2ACdc55 phosphatase by separase and Zds1 protein promotes Net1 phosphorylation and, consequently, Cdc14 release from the nucleolus. The mechanism by which PP2ACdc55 activity is downregulated during anaphase remains to be elucidated. Here, we demonstrate that Cdc55 regulatory subunit is phosphorylated in anaphase in a Cdk1-Clb2-dependent manner. Interestingly, cdc55-ED phosphomimetic mutant inactivates PP2ACdc55 phosphatase activity towards Net1 and promotes Cdc14 activation. Separase and Zds1 facilitate Cdk-dependent Net1 phosphorylation and Cdc14 release from the nucleolus by modulating PP2ACdc55 activity via Cdc55 phosphorylation. In addition, human Cdk1-CyclinB1 phosphorylates human B55, indicating that the mechanism is conserved in higher eukaryotes.We thank CERCA Program/Generalitat de Catalunya for institutional support. Our laboratory is funded by the Spanish Ministry of Economy, Industry and Competitiveness (MINECO), which is part of the State Agency, through the projects BFU2013-43132-P and BFU2016-77975-R, (co-funded by the European Regional Development Fund, ERDF, a way to build Europe). The proteomics analyses were performed in the IDIBELL Clinical Proteomics Unit which is part of Proteored, PRB3 and is supported by Grant PT17/0019, of the PE I+D+i 2013-2016, funded by ISCIII and ERDFPeer reviewedSpringer NatureMinisterio de Economía, Industria y Competitividad (España)European CommissionInstituto de Salud Carlos IIIQueralt, Ethel [0000-0003-0045-0039]202220222019info:eu-repo/semantics/articlehttp://purl.org/coar/resource_type/c_6501Postprintinfo:eu-repo/semantics/acceptedVersionhttp://hdl.handle.net/10261/272414reponame:DIGITAL.CSIC. Repositorio Institucional del CSICinstname:Consejo Superior de Investigaciones Científicas (CSIC)Inglés#PLACEHOLDER_PARENT_METADATA_VALUE##PLACEHOLDER_PARENT_METADATA_VALUE#info:eu-repo/grantAgreement/MINECO//BFU2013-43132-Pinfo:eu-repo/grantAgreement/MINECO//BFU2016-77975-Rhttps://dx.doi.org/10.1007/s00018-019-03086-5Noinfo:eu-repo/semantics/openAccessoai:digital.csic.es:10261/2724142026-05-22T06:33:51Z
dc.title.none.fl_str_mv Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
title Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
spellingShingle Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
Játiva, Soraya
Cell cycle
FEAR
Mitosis
Mitotic exit
PP2A–Cdc55
Phosphatases
Separase
Zds1
title_short Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
title_full Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
title_fullStr Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
title_full_unstemmed Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
title_sort Cdc14 activation requires coordinated Cdk1-dependent phosphorylation of Net1 and PP2A-Cdc55 at anaphase onset
dc.creator.none.fl_str_mv Játiva, Soraya
Calabria, Ines
Moyano-Rodríguez, Yolanda
García, Patricia
Queralt, Ethel
author Játiva, Soraya
author_facet Játiva, Soraya
Calabria, Ines
Moyano-Rodríguez, Yolanda
García, Patricia
Queralt, Ethel
author_role author
author2 Calabria, Ines
Moyano-Rodríguez, Yolanda
García, Patricia
Queralt, Ethel
author2_role author
author
author
author
dc.contributor.none.fl_str_mv Ministerio de Economía, Industria y Competitividad (España)
European Commission
Instituto de Salud Carlos III
Queralt, Ethel [0000-0003-0045-0039]
dc.subject.none.fl_str_mv Cell cycle
FEAR
Mitosis
Mitotic exit
PP2A–Cdc55
Phosphatases
Separase
Zds1
topic Cell cycle
FEAR
Mitosis
Mitotic exit
PP2A–Cdc55
Phosphatases
Separase
Zds1
description 59 páginas 5 figuras, 1 tabla
publishDate 2019
dc.date.none.fl_str_mv 2019
2022
2022
dc.type.none.fl_str_mv info:eu-repo/semantics/article
http://purl.org/coar/resource_type/c_6501
Postprint
info:eu-repo/semantics/acceptedVersion
format article
status_str acceptedVersion
dc.identifier.none.fl_str_mv http://hdl.handle.net/10261/272414
url http://hdl.handle.net/10261/272414
dc.language.none.fl_str_mv Inglés
language_invalid_str_mv Inglés
dc.relation.none.fl_str_mv #PLACEHOLDER_PARENT_METADATA_VALUE#
#PLACEHOLDER_PARENT_METADATA_VALUE#
info:eu-repo/grantAgreement/MINECO//BFU2013-43132-P
info:eu-repo/grantAgreement/MINECO//BFU2016-77975-R
https://dx.doi.org/10.1007/s00018-019-03086-5
No
dc.rights.none.fl_str_mv info:eu-repo/semantics/openAccess
eu_rights_str_mv openAccess
dc.publisher.none.fl_str_mv Springer Nature
publisher.none.fl_str_mv Springer Nature
dc.source.none.fl_str_mv reponame:DIGITAL.CSIC. Repositorio Institucional del CSIC
instname:Consejo Superior de Investigaciones Científicas (CSIC)
instname_str Consejo Superior de Investigaciones Científicas (CSIC)
reponame_str DIGITAL.CSIC. Repositorio Institucional del CSIC
collection DIGITAL.CSIC. Repositorio Institucional del CSIC
repository.name.fl_str_mv
repository.mail.fl_str_mv
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score 15,811543

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