ArticleThe EMBO journal1994
Characterization of the ligand-dependent transactivation domain of thyroid hormone receptor.
Article in The EMBO journal, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 79 papers.
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Who cites it
79 citing papers in PubMed.
- Nuclear receptor corepressor 1 levels differentially impact the intracellular dynamics of mutant thyroid hormone receptors associated with resistance to thyroid hormone syndrome.Molecular and cellular endocrinology · 2024Article
- Thyroid hormone-regulated chromatin landscape and transcriptional sensitivity of the pituitary gland.Communications biology · 2023Article
- Thyroid hormone receptor α mutation causes a severe and thyroxine-resistant skeletal dysplasia in female mice.Endocrinology · 2014Article
- Multiple novel signals mediate thyroid hormone receptor nuclear import and export.The Journal of biological chemistry · 2012Article
- The role of nuclear receptor NHR-64 in fat storage regulation in Caenorhabditis elegans.PloS one · 2010Article
- Complex actions of thyroid hormone receptor antagonist NH-3 on gene promoters in different cell lines.Molecular and cellular endocrinology · 2008Article
- Non-DNA binding, dominant-negative, human PPARgamma mutations cause lipodystrophic insulin resistance.Cell metabolism · 2006Article
- A novel 1297-1304delGCCTGCCA mutation in the exon 10 of the thyroid hormone receptor β gene causes resistance to thyroid hormone.Molecular diagnosis : a journal devoted to the understanding of human disease through the clinical application of molecular biology · 2004Article
- A permissive retinoid X receptor/thyroid hormone receptor heterodimer allows stimulation of prolactin gene transcription by thyroid hormone and 9-cis-retinoic acid.Molecular and cellular biology · 2004Article
- Two domains of the progesterone receptor interact with the estrogen receptor and are required for progesterone activation of the c-Src/Erk pathway in mammalian cells.Molecular and cellular biology · 2003Article
- Article
- Domain structure of the NRIF3 family of coregulators suggests potential dual roles in transcriptional regulation.Molecular and cellular biology · 2001Article
- The hairless gene mutated in congenital hair loss disorders encodes a novel nuclear receptor corepressor.Genes & development · 2001Article
- Article
- Specific structural motifs determine TRAP220 interactions with nuclear hormone receptors.Molecular and cellular biology · 2000Article
- Peroxisome proliferator-activated receptor gamma-dependent repression of the inducible nitric oxide synthase gene.Molecular and cellular biology · 2000Article
- The DRIP complex and SRC-1/p160 coactivators share similar nuclear receptor binding determinants but constitute functionally distinct complexes.Molecular and cellular biology · 2000Article
- Molecular determinants of nuclear receptor-corepressor interaction.Genes & development · 1999Article
- The AF1 and AF2 domains of the androgen receptor interact with distinct regions of SRC1.Molecular and cellular biology · 1999Article
- NRIF3 is a novel coactivator mediating functional specificity of nuclear hormone receptors.Molecular and cellular biology · 1999Article
19 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Transcriptional activation by nuclear receptors is achieved through autonomous activation functions (AFs), a constitutive N-terminal AF-1 and a C-terminal, ligand-dependent AF-2 that comprises a motif conserved between nuclear receptors. We have performed an extensive mutational analysis of the putative AF-2 domain of chicken thyroid hormone receptor alpha (cT3R alpha). We show that the AF-2 region mediates transactivation as well as transcriptional interference (squelching), not only between the thyroid hormone and vitamin (type II) receptors, but also between type II and steroid hormone (type I) receptors. Transcriptional activation and interference require equivalent doses of the cognate ligand, and mutations in the conserved motif that reduce ligand-induced transactivation also impair transcriptional interference. When fused to the Gal4 DNA binding domain, a 35 amino acid long fragment containing the conserved motif is able to transactivate and squelch, albeit in a ligand-independent manner. Our results define the AF-2 of cT3R alpha as an autonomous transactivation domain that, in its natural context, is governed by ligand. We propose that AF-2 is probably part of a surface for interaction with either a general transcription factor or a putative bridging factor, that might be utilized by type I and II receptors.
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