Open AccessHeterodimerization of thyroid hormone (TH) receptor with H-2RIIBP (RXR beta) enhances DNA binding and TH-dependent transcriptional activation.
Author(s) -
Paul L. Hallenbeck,
Michael S. Marks,
Roland E. Lippoldt,
Keiko Ozato,
Vera M. Nikodem
Publication year - 1992
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.89.12.5572
Subject(s) - thyroid hormone receptor , hormone response element , nuclear receptor , receptor , thyroid hormone receptor beta , retinoid x receptor , biology , promoter , hormone receptor , retinoic acid receptor , thyroid hormone receptor alpha , steroid hormone receptor , retinoic acid , steroid hormone , hormone , transcriptional regulation , retinoid x receptor gamma , microbiology and biotechnology , transcription factor , gene , biochemistry , genetics , gene expression , cancer , estrogen receptor , breast cancer
Steroid/TH receptors mediate transcriptional induction of promoters containing hormone response elements (HREs) through an unclear mechanism that involves receptor binding to both hormone and a HRE. Here we demonstrate that both HRE binding and the transcriptional inducing activities of one member of this family, TH receptor, were markedly enhanced by heterodimerization with H-2RIIBP, a non-TH-binding member of the steroid hormone receptor superfamily. H-2RIIBP, the mouse homologue of human retinoic acid-related receptor, was shown to form stable heterodimers with the TH receptor either in solution or when bound to a TH response element. The results presented indicate that it might be necessary for the TH receptor or other members of this superfamily to have specific partners for heterodimer formation to elicit maximal hormone-specific gene regulation from particular HREs.