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- Title
The APC/C and CBP/p300 cooperate to regulate transcription and cell-cycle progression.
- Authors
Turnell, Andrew S.; Stewart, Grant S.; Grand, Roger J. A.; Rookes, Susan M.; Martin, Ashley; Yamano, Hiroyuki; Elledge, Stephen J.; Gallimore, Phillip H.
- 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 cycle. 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 E1A. 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.
- Subjects
EUKARYOTIC cells; MITOSIS; UBIQUITIN; LIGASES; CELL cycle; PROTEIN-protein interactions; ACETYLTRANSFERASES
- Publication
Nature, 2005, Vol 438, Issue 7068, p690
- ISSN
0028-0836
- Publication type
Article
- DOI
10.1038/nature04151