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Papers In Press, published online ahead of print May 17, 2001
Membrane Biology Laboratory, Institute of Molecular and Cell Biology, Singapore 117609
Corresponding Author: mcbhwj{at}imcb.nus.edu.sg
Retinoblastoma binding protein 2 (Rbp2) was originally identified as a retinoblastoma protein (RB)-pocket domain binding protein. Although Rbp2 has been shown to interact with RB, p107, TATA-binding protein (TBP) and T-cell oncogene rhombotin-2, the physiological function of Rbp2 remains unclear. Here we demonstrate that Rbp2 not only binds to nuclear receptors (NRs), but also enhances the transcription mediated by them. Rbp2 interacts with the DNA-binding domains (DBD) of NRs and potentiates NR-mediated transcription in an AF-2-dependent manner. Both the N-terminal and C-terminal domains of Rbp2 are critical for the transactivation activity of Rbp2 on NRs. The C-terminus is the NR-interacting region. In addition, RB functions in maximizing the effect of Rbp2 on the transcription by NRs. These results suggest that Rbp2 is a coregulator of NRs and define a potential role for Rbp2 in NR-mediated transcription.
J. Biol. Chem, 10.1074/jbc.M100313200
Submitted on January 12, 2001
Revised on May 17, 2001
Accepted on May 17, 2001
Retinoblastoma binding protein 2 (Rbp2) potentiates nuclear hormone receptor-mediated transcription
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