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J. Biol. Chem., Vol. 276, Issue 30, 28402-28412, July 27, 2001
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From the Institute of Molecular and Cell Biology, 30 Medical Drive,
Singapore 117609, Republic of Singapore
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, 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 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.
To whom correspondence should be addressed: Institute of Molecular
and Cell Biology, 30 Medical Dr., Singapore 117609, Republic of
Singapore. Tel.: 65-7786827; Fax: 65-7791117; E-mail:
mcbhwj@imcb.nus.edu.sg.
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