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

• Published in: Nature (London) Vol. 396; no. 6707; pp. 184 - 186
• Main Authors: Harel-Bellan, A, Ait-Si-Ali, S, Ramirez, S, Barre, F.-X, Dkhissi, F, Magnaghi-Jaulin, L, Girault, J. A, Robin, P, Knibiehler, M, Pritchard, L. L, Ducommun, B, Trouche, D
• Format: Journal Article
• Language: English
• Published: London Nature Publishing 12.11.1998; Nature Publishing Group
• Subjects: 3T3 Cells; Acetyltransferases - metabolism; Adenovirus E1A Proteins - metabolism; Animals; Biological and medical sciences; CDC2-CDC28 Kinases; Cell Cycle; Cell cycle, cell proliferation; Cell physiology; Cells; CREB-Binding Protein; Cyclin E - metabolism; Cyclin-Dependent Kinase 2; Cyclin-Dependent Kinases - metabolism; Enzyme Activation; Enzymes; Fundamental and applied biological sciences. Psychology; G1 Phase; Genes; Histone Acetyltransferases; Life Sciences; Mice; Molecular and cellular biology; Nuclear Proteins - metabolism; Oncogene Proteins - metabolism; Phosphorylation; Protein-Serine-Threonine Kinases - metabolism; Proteins; S Phase; Saccharomyces cerevisiae Proteins; Trans-Activators - metabolism; Transcriptional Activation; Transfection; Acyltransferases; Phosphorylation; Enzyme; Transferases; Rodentia; 3T3-Cell line; Histone acetyltransferase; In vitro; Vertebrata; Regulation(control); Mammalia; Mouse; Enzymatic activity; Cell cycle; Fibroblast
• ISSN: 0028-0836; 1476-4687
• DOI: 10.1038/24190

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.