Region-specific anti-thyroid hormone receptor (TR) antibodies detect changes in TR structure due to ligand-binding and dimerization

Paul M. Yen, Akira Sugawara, Marc Forgione, Remco A. Spanjaard, Enrico Macchia, Sheue Yann Cheng, William W. Chin

Research output: Contribution to journalArticlepeer-review

10 Citations (Scopus)

Abstract

There are multiple factors that potentially can induce structural changes in DNA-bound thyroid hormone receptors (TRs) including protein-protein interactions, ligand-binding to TRs, and the thyroid hormone response element (TRE) sequence. We used a battery of anti-TR antibodies that recognize the amino-terminal, hinge, or carboxy-terminal regions of TRs to study changes in the epitope regions of in vitro translated TRs in electrophoretic mobility shift assays. We found that the carboxy-terminal and hinge region antibodies recognized TR homodimers but not TR/T3-receptor auxiliary protein or TR/retinoid X receptor heterodimers. The amino-terminal antibodies detected conformational changes due to ligand binding. In contrast, each antibody recognized TR complexes bound to TREs containing half-sites arranged in three different orientations. These results suggest that dimerization with nuclear proteins and ligand-binding, rather than the orientation of TRE half-sites, cause changes in several TR subregions.

Original languageEnglish
Pages (from-to)93-99
Number of pages7
JournalMolecular and Cellular Endocrinology
Volume97
Issue number1-2
DOIs
Publication statusPublished - 1993 Nov
Externally publishedYes

Keywords

  • Anti-TR antibody
  • Heterodimer
  • Homodimer
  • Monomer
  • Thyroid hormone receptor
  • Transcriptional regulation

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Endocrinology

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