ArticleMolecular and cellular biology1999
A novel role for helix 12 of retinoid X receptor in regulating repression.
Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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Who cites it
38 citing papers in PubMed, 112 citations in OpenAlex.
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- A ternary switch model governing ERα ligand binding domain conformation.Nature communications · 2025Article
- Thyroid Hormone Action by Genomic and Nongenomic Molecular Mechanisms.Methods in molecular biology (Clifton, N.J.) · 2025Article
- International Union of Basic and Clinical Pharmacology CXIII: Nuclear Receptor Superfamily-Update 2023.Pharmacological reviews · 2023Review
- Endogenous and combination retinoids are active in myelomonocytic leukemias.Haematologica · 2021Article
- Structural mechanism for signal transduction in RXR nuclear receptor heterodimers.Nature communications · 2015Article
- The optimal corepressor function of nuclear receptor corepressor (NCoR) for peroxisome proliferator-activated receptor γ requires G protein pathway suppressor 2.The Journal of biological chemistry · 2015Article
- Molecular adaptation and resilience of the insect's nuclear receptor USP.BMC evolutionary biology · 2012Article
- 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
- The androgen receptor and its use in biological assays: looking toward effect-based testing and its applications.Journal of analytical toxicology · 2011Review
- Structural basis for retinoic X receptor repression on the tetramer.The Journal of biological chemistry · 2011Article
- Aberrant corepressor interactions implicated in PML-RAR(alpha) and PLZF-RAR(alpha) leukemogenesis reflect an altered recruitment and release of specific NCoR and SMRT splice variants.The Journal of biological chemistry · 2011Article
- Analysis of agonist and antagonist effects on thyroid hormone receptor conformation by hydrogen/deuterium exchange.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Hydrogen/deuterium exchange reveals distinct agonist/partial agonist receptor dynamics within vitamin D receptor/retinoid X receptor heterodimer.Structure (London, England : 1993) · 2010Article
- A unique secondary-structure switch controls constitutive gene repression by retinoic acid receptor.Nature structural & molecular biology · 2010Article
- Nuclear receptor Rev-erbalpha: a heme receptor that coordinates circadian rhythm and metabolism.Nuclear receptor signaling · 2010Review
- Vitamin D-dependent recruitment of corepressors to vitamin D/retinoid X receptor heterodimers.Molecular and cellular biology · 2008Article
- Genetic and pharmacological evidence that a retinoic acid cannot be the RXR-activating ligand in mouse epidermis keratinocytes.Genes & development · 2006Article
- The tailless nuclear receptor acts as a dedicated repressor in the early Drosophila embryo.Molecular and cellular biology · 2006Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Nutrients, drugs, and hormones influence transcription during differentiation and metabolism by binding to high-affinity nuclear receptors. In the absence of ligand, some but not all nuclear receptors repress transcription as a heterodimer with retinoid X receptor (RXR). Here we define a novel role for helix 12 (H12) in sterically masking the corepressor (CoR) binding site in apo-RXR. Removing H12 converts RXR to a potent transcriptional repressor. The length but not the specific sequence of H12 is critical for masking RXR's intrinsic repression function. This contrasts with the amphipathic character required for mediating ligand-dependent activation and coactivator recruitment. Physiologically, we show that heterodimerization of RXR with apo-thyroid hormone receptor (TR) unmasks the CoR binding site in RXR and allows the TR-RXR heterodimer to repress. A molecular mechanism that involves sequence-specific interaction between RXR H12 and the coactivator-binding surface of the nuclear receptor is proposed for this heterodimerization-mediated unmasking. Peroxisome proliferator-activated receptor gamma does not interact as well with RXR H12, thus explaining its inability to repress transcription as an RXR heterodimer. The requirement to unmask RXR's latent repression function explains why only certain RXR partners repress transcription.
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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.