RBP1 Recruits Both Histone Deacetylase-Dependent and -Independent Repression Activities to Retinoblastoma Family Proteins

Author:

Lai Albert1,Lee Joseph M.1,Yang Wen-Ming2,DeCaprio James A.3,Kaelin William G.34,Seto Edward2,Branton Philip E.15

Affiliation:

1. Departments of Biochemistry 1 and

2. H. Lee Moffitt Cancer Center and Research Institute, Molecular Oncology Program, University of South Florida, Tampa, Florida 33612 2 ; and

3. Dana-Farber Cancer Institute and Harvard Medical School 3 and

4. Howard Hughes Medical Institute, 4 Boston, Massachusetts 02115

5. Oncology, 5 McGill University, Montreal, Quebec, Canada H3G 1Y6;

Abstract

ABSTRACT Retinoblastoma (RB) tumor suppressor family proteins block cell proliferation in part by repressing certain E2F-specific promoters. Both histone deacetylase (HDAC)-dependent and -independent repression activities are associated with the RB “pocket.” The mechanism by which these two repression functions occupy the pocket is unknown. A known RB-binding protein, RBP1, was previously found by our group to be an active corepressor which, if overexpressed, represses E2F-mediated transcription via its association with the pocket. We show here that RBP1 contains two repression domains, one of which binds all three known HDACs and represses them in an HDAC-dependent manner while the other domain functions independently of the HDACs. Thus, RB family members repress transcription by recruiting RBP1 to the pocket. RBP1, in turn, serves as a bridging molecule to recruit HDACs and, in addition, provides a second HDAC-independent repression function.

Publisher

American Society for Microbiology

Subject

Cell Biology,Molecular Biology

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