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Signaling and Regulation

A Mechanism of COOH–Terminal Binding Protein–Mediated Repression

Departments of ¹ Molecular Genetics and Microbiology and ² Pharmacology and Cancer Biology and ³ Duke Institute for Genome Sciences and Policy, Duke University Medical Center, Durham, North Carolina

Requests for reprints: Joseph R. Nevins, Department of Genetics, Howard Hughes Medical Institute, Duke University Medical Center, Box 3054, Durham, NC 27710. Phone: 919-684-2746; Fax: 919-681-8973. E-mail: nevin001{at}mc.duke.edu

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.

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