| Autor: |
Meloni AR; Department of Molecular Genetics and Microbiology, Duke University Medical Center, Box 3054, Durham, North Carolina 27710, USA., Lai CH, Yao TP, Nevins JR |
| Jazyk: |
angličtina |
| Zdroj: |
Molecular cancer research : MCR [Mol Cancer Res] 2005 Oct; Vol. 3 (10), pp. 575-83. |
| DOI: |
10.1158/1541-7786.MCR-05-0088 |
| Abstrakt: |
The E2F4 and E2F5 proteins specifically associate with the Rb-related p130 protein in quiescent cells to repress transcription of various genes encoding proteins important for cell growth. A series of reports has provided evidence that Rb-mediated repression involves both histone deacetylase (HDAC)-dependent and HDAC-independent events. Our previous results suggest that one such mechanism for Rb-mediated repression, independent of recruitment of HDAC, involves the recruitment of the COOH-terminal binding protein (CtBP) corepressor, a protein now recognized to play a widespread role in transcriptional repression. We now find that CtBP can interact with the histone acetyltransferase, cyclic AMP--responsive element--binding protein (CREB) binding protein, and inhibit its ability to acetylate histone. This inhibition is dependent on a NH2-terminal region of CtBP that is also required for transcription repression. These results thus suggest two complementary mechanisms for E2F/p130-mediated repression that have in common the control of histone acetylation at target promoters. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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