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

S. Ait-Si-Ali, S. Ramirez, F.-X. Barre, F. Dkhissi, L. Magnaghi-Jaulin, J. A. Girault, P. Robin, M. Knibiehler, L. L. Pritchard, B. Ducommun, D. Trouche and A. Harel-Bellan ()
Additional contact information
S. Ait-Si-Ali: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
S. Ramirez: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
F.-X. Barre: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
F. Dkhissi: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
L. Magnaghi-Jaulin: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
J. A. Girault: INSERM U114, Collège de France
P. Robin: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
M. Knibiehler: IPBS, CNRS UPR 9062, Université Paul Sabatier
L. L. Pritchard: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
B. Ducommun: INSERM U114, Collège de France
D. Trouche: Laboratoire Oncogénèse, Différenciation et Transduction du Signal
A. Harel-Bellan: Laboratoire Oncogénèse, Différenciation et Transduction du Signal

Nature, 1998, vol. 396, issue 6707, 184-186

Abstract: Abstract 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 proteins1,2,3: the retinoblastoma protein (Rb)4, a transcriptional co-repressor5, and CBP/p300 (ref. 6), a transcriptional co-activator7,8,9. These two proteins locally influence chromatin structure: Rb recruits a histone deacetylase10,11,12, whereas CBP is a histone acetyltransferase13,14. 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 genes15. 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.

Date: 1998
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DOI: 10.1038/24190

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