Histone acetyltransferase activity of CBP is controlled by cyclin-dependent kinases and oncoprotein E1A

Transforming viral proteins such as E1A force cells through the restriction point of the cell cycle into S phase by forming complexes with two cellular proteins: the retinoblastoma protein (Rb), a transcriptional co-repressor, and CBP/p300, a transcriptional co-activator. These two proteins locally...

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Bibliographic Details
Published in:Nature (London) 1998-11, Vol.396 (6707), p.184-186
Main Authors: Ait-Si-Ali, S, Ramirez, S, Barre, F-X, Dkhissi, F, Magnaghi-Jaulin, L, Girault, JA, Robin, P, Knibiehler, M, Pritchard, L L, Docommun, B, Trouche, D, Harel-Bellan, A
Format: Article
Language:English
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Summary:Transforming viral proteins such as E1A force cells through the restriction point of the cell cycle into S phase by forming complexes with two cellular proteins: the retinoblastoma protein (Rb), a transcriptional co-repressor, and CBP/p300, a transcriptional co-activator. These two proteins locally influence chromatin structure: Rb recruits a histone deacetylase, whereas CBP is a histone acetyltransferase. Progression through the restriction point is triggered by phosphorylation of Rb, leading to disruption of Rb-associated repressive complexes and allowing the activation of S-phase genes. Here we show that CBP, like Rb, is controlled by phosphorylation at the G1/S boundary, increasing its histone acetyltransferase activity. This enzymatic activation is mimicked by E1A.
ISSN:0028-0836