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Proc Natl Acad Sci U S A. 1995 Aug 29;92(18):8288-92.

Interactions between the retinoid X receptor and a conserved region of the TATA-binding protein mediate hormone-dependent transactivation.

Author information

1
Salk Institute for Biological Studies, La Jolla, CA 92037, USA.

Abstract

The retinoid X receptor (RXR) participates in a wide array of hormonal signaling pathways, either as a homodimer or as a heterodimer, with other members of the steroid and thyroid hormone receptor superfamily. In this report the ligand-dependent transactivation function of RXR has been characterized, and the ability of RXR to interact with components of the basal transcription machinery has been examined. In vivo and in vitro experiments indicate the RXR ligand-binding domain makes a direct, specific, and ligand-dependent contact with a highly conserved region of the TATA-binding protein. The ability of mutations that reduce ligand-dependent transcription by RXR to disrupt the RXR-TATA-binding protein interaction in vivo and in vitro suggests that RXR makes direct contact with the basal transcription machinery to achieve activation.

PMID:
7667283
PMCID:
PMC41142
DOI:
10.1073/pnas.92.18.8288
[Indexed for MEDLINE]
Free PMC Article

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