Author
Listed:
- 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)
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.
Suggested Citation
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, 1998.
"Histone acetyltransferase activity of CBP is controlled by cycle-dependent kinases and oncoprotein E1A,"
Nature, Nature, vol. 396(6707), pages 184-186, November.
Handle:
RePEc:nat:nature:v:396:y:1998:i:6707:d:10.1038_24190
DOI: 10.1038/24190
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