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J Biol Chem, Vol. 273, Issue 6, 3375-3380, February 6, 1998
From the Division of Endocrinology and Metabolism, University of
Michigan Medical Center, Ann Arbor, Michigan 48109-0678
Thyroid hormone receptors are ligand-modulated
transcription factors that can repress or activate transcription
depending upon the absence or presence of thyroid hormone and the
nature of the hormone response element to which the receptors are
bound. The ability of thyroid hormone receptors to repress
transcription in the absence of ligand is thought to be due to
associations with nuclear hormone receptor corepressors. Ligand binding
by the thyroid hormone receptor is believed to dissociate these
corepressors and recruit coactivators to promote transcription from
target promoters. We hypothesize that variations in response element architecture may influence both the association and dissociation of
corepressors from DNA-bound thyroid hormone receptors. Using a chimeric
corepressor, we find that ligand alone does not fully relieve
corepressor-mediated repression, particularly in the presence of
thyroid hormone receptor and its heterodimerization partner, the
retinoid X receptor. Interestingly, the steroid receptor coactivator 1 together with ligand is able to mediate full release of corepression, but this relief is dependent upon the architecture of the response element to which the nuclear receptor dimer-corepressor complex is
bound. These studies suggest that other cellular factors in addition to
ligand may be required for the release of corepressors from thyroid
hormone receptor dimers.
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