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A nuclear hormone receptor-associated protein that inhibits transactivation by the thyroid hormone and retinoic acid receptors

Burris, T.P.; Nawaz, Z.; Tsai, M.J.; O'Malley, B.W.

Proceedings of the National Academy of Sciences of the United States of America 92(21): 9525-9529

1995


ISSN/ISBN: 0027-8424
PMID: 7568167
DOI: 10.2307/2368508
Accession: 008061965

Nuclear hormone receptors are transcription factors that require multiple protein-protein interactions to regulate the expression of their target genes. Using the yeast two-hybrid system, we identified a protein, thyroid hormone receptor uncoupling protein (TRUP), that specifically interacts with a region of the human thyroid hormone receptor (TR) consisting of the hinge region and the N-terminal portion of the ligand binding domain in a hormone-independent manner. Interestingly, TRUP inhibits transactivation by TR and the retinoic acid receptor but has no effect on the estrogen receptor or the retinoid X receptor in mammalian cells. We also demonstrate that TRUP exerts its action on TR and retinoic acid receptor by interfering with their abilities to interact with their DNA. TRUP represents a type of regulatory protein that modulates the transcriptional activity of a subclass of the nuclear hormone receptor superfamily by preventing interaction with their genomic response elements.

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