A mechanism of COOH-terminal binding protein-mediated repression.

Journal Article

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.

Full Text

Duke Authors

Cited Authors

  • Meloni, AR; Lai, C-H; Yao, T-P; Nevins, JR

Published Date

  • October 2005

Published In

Volume / Issue

  • 3 / 10

Start / End Page

  • 575 - 583

PubMed ID

  • 16254191

International Standard Serial Number (ISSN)

  • 1541-7786

Digital Object Identifier (DOI)

  • 10.1158/1541-7786.MCR-05-0088

Language

  • eng

Conference Location

  • United States