The APC/C and CBP/p300 cooperate to regulate transcription and cell-cycle progression

Andrew S. Turnell (), Grant S. Stewart, Roger J. A. Grand, Susan M. Rookes, Ashley Martin, Hiroyuki Yamano, Stephen J. Elledge and Phillip H. Gallimore
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Andrew S. Turnell: The Medical School, The University of Birmingham
Grant S. Stewart: The Medical School, The University of Birmingham
Roger J. A. Grand: The Medical School, The University of Birmingham
Susan M. Rookes: The Medical School, The University of Birmingham
Ashley Martin: The Medical School, The University of Birmingham
Hiroyuki Yamano: The Chart
Stephen J. Elledge: Baylor College of Medicine
Phillip H. Gallimore: The Medical School, The University of Birmingham

Nature, 2005, vol. 438, issue 7068, 690-695

Abstract: Abstract The anaphase-promoting complex/cyclosome (APC/C) is a multicomponent E3 ubiquitin ligase that, by targeting protein substrates for 26S proteasome-mediated degradation through ubiquitination, coordinates the temporal progression of eukaryotic cells through mitosis and the subsequent G1 phase of the cell cycle1,2,3,4. Other functions of the APC/C are, however, less well defined. Here we show that two APC/C components, APC5 and APC7, interact directly with the coactivators CBP and p300 through protein–protein interaction domains that are evolutionarily conserved in adenovirus E1A5,6,7,8. This interaction stimulates intrinsic CBP/p300 acetyltransferase activity and potentiates CBP/p300-dependent transcription. We also show that APC5 and APC7 suppress E1A-mediated transformation in a CBP/p300-dependent manner, indicating that these components of the APC/C may be targeted during cellular transformation. Furthermore, we establish that CBP is required in APC/C function; specifically, gene ablation of CBP by RNA-mediated interference markedly reduces the E3 ubiquitin ligase activity of the APC/C and the progression of cells through mitosis. Taken together, our results define discrete roles for the APC/C–CBP/p300 complexes in growth regulation.

Date: 2005
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DOI: 10.1038/nature04151

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