Histone acetyltransferase activity of CBP is controlled by cycle-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 1 , 2 , 3 : the retinoblastoma protein (Rb) 4 , a transcriptional co-repressor 5 , and CBP/p300 ( ref. 6 ), a transcriptional co-activator...

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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, J. A., Robin, P., Knibiehler, M., Pritchard, L. L., Ducommun, B., Trouche, D., Harel-Bellan, A.
Format: Article
Language:English
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
Humanities and Social Sciences
letter
Life Sciences
Mice
Molecular and cellular biology
multidisciplinary
Nuclear Proteins - metabolism
Oncogene Proteins - metabolism
Phosphorylation
Protein-Serine-Threonine Kinases - metabolism
Proteins
S Phase
Saccharomyces cerevisiae Proteins
Science
Science (multidisciplinary)
Trans-Activators - metabolism
Transcriptional Activation
Transfection
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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 1 , 2 , 3 : the retinoblastoma protein (Rb) 4 , a transcriptional co-repressor 5 , and CBP/p300 ( ref. 6 ), a transcriptional co-activator 7 , 8 , 9 . These two proteins locally influence chromatin structure: Rb recruits a histone deacetylase 10 , 11 , 12 , whereas CBP is a histone acetyltransferase 13 , 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 genes 15 . 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
1476-4687
DOI:10.1038/24190