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dc.contributor.authorMateo, Francesca-
dc.contributor.authorVidal-Laliena, Miriam-
dc.contributor.authorCanela, Núria-
dc.contributor.authorBusino, Luca-
dc.contributor.authorMartínez-Balbás, Marian-
dc.contributor.authorPagano, Michele-
dc.contributor.authorAgell, Neus-
dc.contributor.authorBachs, Oriol-
dc.date.accessioned2015-09-08T09:35:14Z-
dc.date.available2015-09-08T09:35:14Z-
dc.date.issued2009-06-01-
dc.identifierdoi: 10.1038/onc.2009.127-
dc.identifierissn: 0950-9232-
dc.identifier.citationOncogene 28(29): 2654-2666 (2009)-
dc.identifier.urihttp://hdl.handle.net/10261/121770-
dc.description.abstractCyclin A accumulates at the onset of S phase, remains high during G 2 and early mitosis and is degraded at prometaphase. Here, we report that the acetyltransferase P/CAF directly interacts with cyclin A that as a consequence becomes acetylated at lysines 54, 68, 95 and 112. Maximal acetylation occurs simultaneously to ubiquitylation at mitosis, indicating importance of acetylation on cyclin A stability. This was further confirmed by the observation that the pseudoacetylated cyclin A mutant can be ubiquitylated whereas the nonacetylatable mutant cannot. The nonacetylatable mutant is more stable than cyclin A WT (cycA WT) and arrests cell cycle at mitosis. Moreover, in cells treated with histone deacetylase inhibitors cyclin A acetylation increases and its stability decreases, thus supporting the function of acetylation on cyclin A degradation. Although the nonacetylatable mutant cannot be ubiquitylated, it interacts with the proteins needed for its degradation (cdks, Cks, Cdc20, Cdh1 and APC/C). In fact, its association with cdks is increased and its complexes with these kinases display higher activity than control cycA WT-cdk complexes. All these results indicate that cyclin A acetylation at specific lysines is crucial for cyclin A stability and also has a function in the regulation of cycA-cdk activity. © 2009 Macmillan Publishers Limited All rights reserved.-
dc.description.sponsorshipThis research was supported by grants SAF2006-05212 and SAF2007-60491 from the Ministerio de Educación y Ciencia of Spain and RETICS RD06/0020/0010 from the Instituto de Salud Carlos III. It was also supported by grants from the National Institutes of Health (R01-GM57587, R37-CA76584, and R21-CA125173) and the Multiple Myeloma Research foundation to Michele Pagano-
dc.publisherNature Publishing Group-
dc.relation.isversionofPostprint-
dc.rightsopenAccess-
dc.titleDegradation of cyclin A is regulated by acetylation-
dc.typeartículo-
dc.identifier.doi10.1038/onc.2009.127-
dc.relation.publisherversionhttp://dx.doi.org/10.1038/onc.2009.127-
dc.date.updated2015-09-08T09:35:14Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.contributor.funderMinisterio de Educación y Ciencia (España)-
dc.contributor.funderInstituto de Salud Carlos III-
dc.contributor.funderMultiple Myeloma Research Foundation-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100004587es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/100001253es_ES
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