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dc.contributor.author | Ovejero, Sara | |
dc.contributor.author | Ayala, Patricia | |
dc.contributor.author | Malumbres Martinez, Marcos | |
dc.contributor.author | Pimentel-Muiños, Felipe X | |
dc.contributor.author | Bueno, Avelino | |
dc.contributor.author | Sacristán, María P | |
dc.date.accessioned | 2018-11-16T11:21:41Z | |
dc.date.available | 2018-11-16T11:21:41Z | |
dc.date.issued | 2018-08-08 | |
dc.identifier.citation | Sci Rep. 2018; 8(1):11871. | es_ES |
dc.identifier.issn | 2045-2322 | es_ES |
dc.identifier.uri | http://hdl.handle.net/20.500.12105/6615 | |
dc.description.abstract | Cdc14 enzymes compose a family of highly conserved phosphatases that are present in a wide range of organisms, including yeast and humans, and that preferentially reverse the phosphorylation of Cyclin-Dependent Kinase (Cdk) substrates. The budding yeast Cdc14 orthologue has essential functions in the control of late mitosis and cytokinesis. In mammals, however, the two Cdc14 homologues, Cdc14A and Cdc14B, do not play a prominent role in controlling late mitotic events, suggesting that some Cdc14 functions are not conserved across species. Moreover, in yeast, Cdc14 is regulated by changes in its subcellular location and by phosphorylation events. In contrast, little is known about the regulation of human Cdc14 phosphatases. Here, we have studied how the human Cdc14A orthologue is regulated during the cell cycle. We found that Cdc14A is phosphorylated on Ser411, Ser453 and Ser549 by Cdk1 early in mitosis and becomes dephosphorylated during late mitotic stages. Interestingly, in vivo and in vitro experiments revealed that, unlike in yeast, Cdk1-mediated phosphorylation of human Cdc14A did not control its catalytic activity but likely modulated its interaction with other proteins in early mitosis. These findings point to differences in Cdk1-mediated mechanisms of regulation between human and yeast Cdc14 orthologues. | es_ES |
dc.description.sponsorship | We thank S. Andrés for technical assistance and other members of laboratory for helpful discussions. We are grateful to Dr. I. García-Higuera and S. Moreno (IBFG, Salamanca) for Cdh1 plasmids and anti-Plk1 antibodies, Dr. J. Dong (Univ. Nebraska Medical Center, Nebraska) for the KIBRA plasmids, Dr. C. Guerrero (IBMCC, Salamanca) for the anti-PP2A antibody and Dr. Jallepalli (Memorial Sloan Kettering Cancer Center, New York) for the RPE Cdc14A − / − cells. We are grateful to the proteomics facility of Centro de Investigación del Cáncer, Salamanca, Spain, where the proteomic analysis was performed, Grant PRB2 (IPT13/0001 - ISCIII-SGEFI / FEDER). This work was funded by grants from the Spanish Ministry of Economy, Industry and Competitiveness (MINECO; BFU2015-69709-P and SAF2015-69920-R). S.O. was supported by a FPU fellowship from the Spanish Ministry of Education and P.A. was supported by a JAE-Predoctoral fellowship from the Spanish National research Council (CSIC). | es_ES |
dc.language.iso | eng | es_ES |
dc.publisher | Nature Publishing Group | es_ES |
dc.type.hasVersion | VoR | es_ES |
dc.rights.uri | http://creativecommons.org/licenses/by/4.0/ | * |
dc.subject | MITOTIC EXIT | es_ES |
dc.subject | FISSION YEAST | es_ES |
dc.subject | CHROMOSOME SEGREGATION | es_ES |
dc.subject | QUANTITATIVE MODEL | es_ES |
dc.subject | G(2)/M TRANSITION | es_ES |
dc.subject | CYTOKINESIS | es_ES |
dc.subject | CDK1 | es_ES |
dc.subject | CENTROSOME | es_ES |
dc.subject | PROGRESSION | es_ES |
dc.subject | CHECKPOINT | es_ES |
dc.title | Biochemical analyses reveal amino acid residues critical for cell cycle-dependent phosphorylation of human Cdc14A phosphatase by cyclin-dependent kinase 1 | es_ES |
dc.type | journal article | es_ES |
dc.rights.license | Atribución 4.0 Internacional | * |
dc.identifier.pubmedID | 30089874 | es_ES |
dc.format.volume | 8 | es_ES |
dc.format.number | 1 | es_ES |
dc.format.page | 11871 | es_ES |
dc.identifier.doi | 10.1038/s41598-018-30253-8 | es_ES |
dc.contributor.funder | Centro de Investigación en Cáncer - CIC | |
dc.contributor.funder | Ministerio de Ciencia e Innovación (España) | |
dc.description.peerreviewed | Sí | |
dc.identifier.e-issn | 2045-2322 | es_ES |
dc.relation.publisherversion | https://doi.org/10.1038/s41598-018-30253-8. | es_ES |
dc.identifier.journal | Scientific reports | es_ES |
dc.repisalud.institucion | CNIO | es_ES |
dc.repisalud.orgCNIO | CNIO::Grupos de investigación::Grupo de División Celular y Cáncer | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/ES/PRB2IPT13/0001 | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/ES/SAF2015-69920-R | es_ES |
dc.relation.projectID | info:eu-repo/grantAgreement/ES/BFU2015-69709-P | es_ES |
dc.rights.accessRights | open access | es_ES |