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Regulation of CBP and Tip60 coordinates histone acetylation at local and global levels during Ras-induced transformation.

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dc.contributor.authorSánchez-Molina, Sara
dc.contributor.authorEstarás, Conchi
dc.contributor.authorOliva-Martinez, Jose Luis
dc.contributor.authorAkizu, Naiara
dc.contributor.authorAsensio-Juan, Elena
dc.contributor.authorRojas-Cabañeros, Jose Maria
dc.contributor.authorMartínez-Balbás, Marian A
dc.contributor.funderMinisterio de Educación y Ciencia (España)
dc.contributor.funderFundación La Marató TV3
dc.contributor.funderInstituto de Salud Carlos III
dc.contributor.funderRed Temática de Investigación Cooperativa en Cáncer (RTICC) (España)
dc.contributor.funderGovernment of Catalonia (España)
dc.contributor.funderInnovate UK
dc.contributor.funderFondation Jérôme-Lejeune
dc.date.accessioned2025-01-23T10:03:50Z
dc.date.available2025-01-23T10:03:50Z
dc.date.issued2014-10
dc.description.abstractCell transformation is clearly linked to epigenetic changes. However, the role of the histone-modifying enzymes in this process is still poorly understood. In this study, we investigated the contribution of the histone acetyltransferase (HAT) enzymes to Ras-mediated transformation. Our results demonstrated that lysine acetyltransferase 5, also known as Tip60, facilitates histone acetylation of bulk chromatin in Ras-transformed cells. As a consequence, global H4 acetylation (H4K8ac and H4K12ac) increases in Ras-transformed cells, rendering a more decompacted chromatin than in parental cells. Furthermore, low levels of CREB-binding protein (CBP) lead to hypoacetylation of retinoblastoma 1 (Rb1) and cyclin-dependent kinase inhibitor 1B (Cdkn1b or p27Kip1) tumour suppressor gene promoters to facilitate Ras-mediated transformation. In agreement with these data, overexpression of Cbp counteracts Ras transforming capability in a HAT-dependent manner. Altogether our results indicate that CBP and Tip60 coordinate histone acetylation at both local and global levels to facilitate Ras-induced transformation.
dc.description.peerreviewedSí
dc.description.sponsorshipThe Spanish Ministry of Education and Science (BFU2006-01493, BFU2009-11527, CSD2006-00049, BFU-2012–34261); Fundació La Marató de TV3 (090210); Fondation Jérôme Lejeune to MAMB; the Spanish Ministry of Education and Science, Fondo de Investigaciones Sanitarias-Intrasalud PI09/0562 (SAF2006-04247); Red Temática de Investigación Cooperativa en Cáncer from the Instituto de Salud Carlos III (RD06/0020/0003 and RD12/0036/0021 to J.M.R.); I3P fellowship (I3P-BPD2005) to N.A.; a FPU fellow ship to C.E.; and a Generalitat de Catalunya predoctoral fellowship to S.S.-M.
dc.format.number10
dc.format.page2194-2202
dc.format.volume35
dc.identifier.citationSánchez-Molina S, Estarás C, Oliva JL, Akizu N, Asensio-Juan E, Rojas JM, Martínez-Balbás MA. Regulation of CBP and Tip60 coordinates histone acetylation at local and global levels during Ras-induced transformation. Carcinogenesis. 2014 Oct;35(10):2194-202.
dc.identifier.doi10.1093/carcin/bgu111
dc.identifier.e-issn1460-2180
dc.identifier.issn0143-3334
dc.identifier.journalCarcinogenesis
dc.identifier.pubmedID24853677
dc.identifier.urihttps://hdl.handle.net/20.500.12105/26107
dc.language.isoeng
dc.publisherOxford University Press
dc.relation.projectIDinfo:eu-repo/grantAgreement/MEC//BFU2006-01493/ES/MECANISMOS EPIGENETICOS IMPLICADOS EN LA PROLIFERACION Y DIFERENCION CELULARES: PAPEL DE LAS MODIFICACIONES DE LAS HISTONAS/
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/CSD2006-00049
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/BFU-2012-34261
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/PI09/0562
dc.relation.projectIDinfo:eu-repo/grantAgreement/MEC//SAF2006-04247/ES/ANALISIS DE LOS MECANISMOS DE REGULACION DE LAS VIAS DE TRANSMISION DE SEÑALES DEPENDIENTES DE LAS PROTEINAS RAS: EFECTOS DIFERENCIALES, SISTEMAS DOCKING%2FSCAFFOLD Y NUEVOS ESTIMULOS/
dc.relation.projectIDinfo:eu-repo/grantAgreement/MSC//RD06%2F0020%2F0003/ES/RED TEMÁTICA DE INVESTIGACIÓN COOPERATIVA DEL CANCER/
dc.relation.projectIDinfo:eu-repo/grantAgreement/ES/RD12/0036/0021
dc.relation.publisherversionhttps://doi.org/10.1093/carcin/bgu111
dc.repisalud.centroISCIII::Unidad Funcional de Investigación de Enfermedades Crónicas (UFIEC)
dc.repisalud.institucionISCIII
dc.rights.accessRightsopen access
dc.rights.licenseAttribution-NonCommercial-NoDerivatives 4.0 International
dc.rights.urihttp://creativecommons.org/licenses/by-nc-nd/4.0/
dc.subjectHistone acetylation
dc.subjectRas transformation
dc.subjectGene expression
dc.subjectChromatin modification
dc.subject.meshAcetylation
dc.subject.meshAnimals
dc.subject.meshCREB-Binding Protein
dc.subject.meshCell Transformation, Neoplastic
dc.subject.meshChromatin
dc.subject.meshCyclin-Dependent Kinase Inhibitor p27
dc.subject.meshGenes, ras
dc.subject.meshHistone Acetyltransferases
dc.subject.meshHistones
dc.subject.meshLysine Acetyltransferase 5
dc.subject.meshMice
dc.subject.meshNIH 3T3 Cells
dc.subject.meshPhosphatidylinositol 3-Kinases
dc.subject.meshPromoter Regions, Genetic
dc.subject.meshSignal Transduction
dc.subject.meshTrans-Activators
dc.titleRegulation of CBP and Tip60 coordinates histone acetylation at local and global levels during Ras-induced transformation.
dc.typeresearch article
dc.type.hasVersionSMUR
dspace.entity.typePublication
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