Heterodimerization of Thyroid Hormone (TH) Receptor with H-2RIIBP (RXBβ) Enhances DNA Binding and TH-Dependent Transcriptional Activation

• Published in: Proceedings of the National Academy of Sciences - PNAS Vol. 89; no. 12; pp. 5572 - 5576
• Main Authors: Hallenbeck, Paul L., Marks, Michael S., Lippoldt, Roland E., Ozato, Keiko, Nikodem, Vera M.
• Format: Journal Article
• Language: English
• Published: Washington, DC National Academy of Sciences of the United States of America 15-06-1992; National Acad Sciences; National Academy of Sciences
• Subjects: 3T3 cells; Animals; Antibodies; Baculoviridae - genetics; Biochemistry; Biological and medical sciences; Cell Line; Cell nucleus; Cell Nucleus - metabolism; Cell receptors; Cell structures and functions; Chloramphenicol O-Acetyltransferase - genetics; Chloramphenicol O-Acetyltransferase - metabolism; DNA; DNA - genetics; DNA - metabolism; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; Electrophoresis, Polyacrylamide Gel; Fundamental and applied biological sciences. Psychology; Gels; Hormone receptors. Growth factor receptors. Cytokine receptors. Prostaglandin receptors; Hormones; Insecta; Kinetics; Macromolecular Substances; Methionine - metabolism; Molecular and cellular biology; Molecular Weight; NIH 3T3 cells; Nuclear proteins; Plasmids; Rats; Receptors; Receptors, Thyroid Hormone - isolation & purification; Receptors, Thyroid Hormone - metabolism; Recombinant Proteins - metabolism; Transcription, Genetic; Transcriptional activation; Transfection; Transcription; Rodentia; Activation; Response element; Binding protein; Vertebrata; Mammalia; Binding capacity; Mouse; Thyroid hormone; Mechanism of action; Dimerization; Biological receptor; Hormonal receptor
• ISSN: 0027-8424; 1091-6490
• DOI: 10.1073/pnas.89.12.5572

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.