ArticleMolecular and cellular endocrinology2009
The thyroid hormone receptor recruits NCoR via widely spaced receptor-interacting domains.
Article in Molecular and cellular endocrinology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 14 citations in OpenAlex.
- Nuclear receptor coregulator interactions: beyond the switch.Genes & development · 2026Review
- 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
- NCOR1 Orchestrates Transcriptional Landscapes and Effector Functions of CD4Frontiers in immunology · 2020Article
- Genetic and Pharmacological Targeting of Transcriptional Repression in Resistance to Thyroid Hormone Alpha.Thyroid : official journal of the American Thyroid Association · 2019Article
- Thyroid Hormone Receptor β Suppression of RUNX2 Is Mediated by Brahma-Related Gene 1-Dependent Chromatin Remodeling.Endocrinology · 2018Article
- NCoR1-independent mechanism plays a role in the action of the unliganded thyroid hormone receptor.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Thyroid hormone signaling in vivo requires a balance between coactivators and corepressors.Molecular and cellular biology · 2014Article
- SMRTε, a corepressor variant, interacts with a restricted subset of nuclear receptors, including the retinoic acid receptors α and β.Molecular and cellular endocrinology · 2012Article
- Nuclear hormone receptor co-repressors: structure and function.Molecular and cellular endocrinology · 2012Review
- NCoR1 regulates thyroid hormone receptor isoform-dependent adipogenesis.Journal of molecular endocrinology · 2011Article
- Thyroid hormone receptor mutations in cancer and resistance to thyroid hormone: perspective and prognosis.Journal of thyroid research · 2011Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
The nuclear receptor corepressor (NCoR) interacts with the DNA-bound thyroid receptor (TR) homodimer through two of its three receptor-interacting domains (RIDs). One of these RIDs must be the most N-terminal, termed N3, which preferentially works with the next closest RID, N2. Interestingly, the spacing between the RIDs is conserved between species such that N3 and N2 are separated by approximately 120 aa, while the spacing between N2 and N1 is around 205 aa, suggesting that distance plays a role in the specificity of N3 and N2. Herein, we demonstrate that even when spaced by 122 aa N2 and N1 cannot mediate recruitment to the TR homodimer. Furthermore, N3 is able to function with either N2 or N1 at distances as small as 45 aa and as large as 240 aa. Thus, specificity of NCoR recruitment to the TR is dictated by the amino acid sequence of N3, and not by the distance separating it from other RIDs. Furthermore, the wide spacing of the NCoR RIDs likely allows for potential flexibility in the DNA-bound TR complex in its ability to recruit NCoR.
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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 OpenQuestion graph.