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, A. Harel-Bellan

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264 Scopus citations

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 proteins: the retinoblastoma protein (Rb), a transcriptional co- repressor, and CBP/p300 (ref. 6), 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.

Original languageEnglish (US)
Pages (from-to)184-186
Number of pages3
JournalNature
Volume396
Issue number6707
DOIs
StatePublished - Nov 12 1998
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • General

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