ArticleMolecular and cellular biology1995
The tau 4 activation domain of the thyroid hormone receptor is required for release of a putative corepressor(s) necessary for transcriptional silencing.
Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 76 papers.
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Who cites it
76 citing papers in PubMed, 247 citations in OpenAlex.
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- Overcoming oncogene addiction in breast and prostate cancers: a comparative mechanistic overview.Endocrine-related cancer · 2021Review
- Origins of the Field of Molecular Endocrinology: A Personal Perspective.Molecular endocrinology (Baltimore, Md.) · 2016Article
- Transcriptional coregulators: emerging roles of SRC family of coactivators in disease pathology.Journal of molecular endocrinology · 2014Review
- Steroid receptor coactivators: servants and masters for control of systems metabolism.Trends in endocrinology and metabolism: TEM · 2014Review
- Ectopically tethered CP190 induces large-scale chromatin decondensation.Scientific reports · 2014Article
- An evolving understanding of nuclear receptor coregulator proteins.Journal of molecular endocrinology · 2013Review
- Nuclear receptors and their selective pharmacologic modulators.Pharmacological reviews · 2013Review
- Minireview: nuclear receptor and coregulator proteomics--2012 and beyond.Molecular endocrinology (Baltimore, Md.) · 2012Review
- Multiple novel signals mediate thyroid hormone receptor nuclear import and export.The Journal of biological chemistry · 2012Article
- Steroid receptor coactivators 1, 2, and 3: critical regulators of nuclear receptor activity and steroid receptor modulator (SRM)-based cancer therapy.Molecular and cellular endocrinology · 2012Review
- Disruption of thyroid hormone receptor-mediated transcription and thyroid hormone-induced Purkinje cell dendrite arborization by polybrominated diphenyl ethers.Environmental health perspectives · 2011Article
- Steroid receptor coactivator (SRC) family: masters of systems biology.The Journal of biological chemistry · 2010Review
- Multi-modulation of nuclear receptor coactivators through posttranslational modifications.Trends in endocrinology and metabolism: TEM · 2009Review
- p66alpha and p66beta of the Mi-2/NuRD complex mediate MBD2 and histone interaction.Nucleic acids research · 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
- The highly conserved region of the co-repressor Sin3A functionally interacts with the co-repressor Alien.Nucleic acids research · 2004Article
- Nuclear receptor corepressors.Nuclear receptor signaling · 2003Article
- The LIM-only protein FHL2 interacts with beta-catenin and promotes differentiation of mouse myoblasts.The Journal of cell biology · 2002Article
- Peroxisome-proliferator-activated receptor delta mediates the effects of long-chain fatty acids on post-confluent cell proliferation.The Biochemical journal · 2000Article
16 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
Abstract
The C terminus of nuclear hormone receptors is a complex structure that contains multiple functions. We are interested in the mechanism by which thyroid hormone converts its receptor from a transcriptional silencer to an activator of transcription. Both regulatory functions are localized in the ligand binding domain of this receptor superfamily member. In this study, we have identified and characterized several functional domains within the ligand binding domain of the human thyroid hormone receptor (TR beta) conferring transactivation. Interestingly, these domains are localized adjacent to hormone binding sites. One activation domain, designated tau 4, is only 17 amino acids in length and is localized at the extreme C terminus of TR. Deletion of six amino acids of tau 4 resulted in a receptor that could still bind hormone but acted as a constitutive silencer, indicating that tau 4 is required for both transactivation and relief of the silencing functions. In addition, we performed in vivo competition experiments, the results of which suggest that in the absence of tau 4 or hormone, TR is bound by a corepressor protein(s) and that one role of hormone is to release corepressor from the receptor. We propose a general model in which the role of hormone is to induce a conformational change in the receptor that subsequently affects the action of tau 4, leading to both relief of silencing and transcriptional activation.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the Socratic graph.