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

AuthorsSánchez-Molina, Sara; Estarás, Conchi ; Oliva, José Luis; Akizu, Naiara; Asensio-Juan, Elena ; Rojas, José María; Martínez-Balbás, Marian
Issue Date22-May-2014
PublisherOxford University Press
CitationCarcinogenesis 35(10): 2194-2202 (2014)
Abstract© The Author 2014. Published by Oxford University Press. All rights reserved. For Permissions, please email: journals.permissions@oup.com. Cell 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.
Publisher version (URL)http://dx.doi.org/10.1093/carcin/bgu111
Identifiersdoi: 10.1093/carcin/bgu111
issn: 1460-2180
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