ArticleMolecular and cellular biology1995
Determinants of target gene specificity for ROR alpha 1: monomeric DNA binding by an orphan nuclear receptor.
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 40 papers.
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Who cites it
40 citing papers in PubMed, 123 citations in OpenAlex.
- Retinoic acid-related orphan receptor alpha (RORα) as a candidate multi-pathway target in Alzheimer's disease: mechanisms and therapeutic prospects.Frontiers in neuroscience · 2026Review
- Autism spectrum disorder and the role of nuclear hormone receptors: insights and therapeutic implications.Frontiers in neuroscience · 2025Review
- The Circadian Clock Component RORA Increases Immunosurveillance in Melanoma by Inhibiting PD-L1 Expression.Cancer research · 2024Article
- Induction of hepatic fibrosis in mice with schistosomiasis by extracellular microRNA-30 derived fromFrontiers in immunology · 2024Article
- The REV-ERB Nuclear Receptors: Timekeepers for the Core Clock Period and Metabolism.Endocrinology · 2023Review
- Unraveling the physiological roles of retinoic acid receptor-related orphan receptor α.Experimental & molecular medicine · 2021Review
- Sex-specific expression mechanism of hepatic estrogen inactivating enzyme and transporters in diabetic women.Biochemical pharmacology · 2021Article
- RORα Regulates Odontoblastic Differentiation and Mediates the Pro-Odontogenic Effect of Melatonin on Dental Papilla Cells.Molecules (Basel, Switzerland) · 2021Article
- Transcriptional Control of Circadian Rhythms and Metabolism: A Matter of Time and Space.Endocrine reviews · 2020Review
- Ser100-Phosphorylated RORMolecular pharmacology · 2020Article
- The Pleiotropic Role of Retinoic Acid/Retinoic Acid Receptors Signaling: From Vitamin A Metabolism to Gene Rearrangements in Acute Promyelocytic Leukemia.International journal of molecular sciences · 2019Review
- Retinoic acid-related Orphan Receptor γ (RORγ): connecting sterol metabolism to regulation of the immune system and autoimmune disease.Current opinion in toxicology · 2018Article
- Melatonin and Hippo Pathway: Is There Existing Cross-Talk?International journal of molecular sciences · 2017Article
- A fourth subtype of retinoic acid receptor-related orphan receptors is activated by oxidized all-Zoological letters · 2017Article
- Genetic and epigenomic mechanisms of mammalian circadian transcription.Nature structural & molecular biology · 2016Review
- Novel Function of Rev-erbα in Promoting Brown Adipogenesis.Scientific reports · 2015Article
- Role of Nuclear Receptors in Central Nervous System Development and Associated Diseases.Journal of experimental neuroscience · 2015Review
- Retinoid receptors in bone and their role in bone remodeling.Frontiers in endocrinology · 2015Review
- Targeting nuclear receptors with marine natural products.Marine drugs · 2014Review
- Retinoic acid actions through mammalian nuclear receptors.Chemical reviews · 2014Review
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The ROR alpha isoforms are orphan members of the steroid/thyroid/retinoid receptor superfamily. Previous DNA-binding studies indicated that ROR alpha isoforms bind to response elements consisting of a single copy of the core recognition sequence AGGTCA preceded by a 6-bp A/T-rich sequence and that the distinct amino-terminal domains of each isoform influence DNA-binding specificity. In this report, we have investigated in detail the protein determinants of target gene specificity for the ROR alpha 1 isoform and have now identified the minimal sequence both in its amino- and carboxy-terminal domains required for high-affinity DNA binding. High-resolution methylation and ethylation interference analyses and mixing of truncated proteins in a DNA-binding assay show that ROR alpha 1 presumably binds along one face of the DNA helix as a monomer. By analogy to previous studies of the orphan receptors NGFI-B and FTZ-F1, extensive mutational analysis of the ROR alpha 1 protein shows that a domain extending from the carboxy-terminal end of the second conserved zinc-binding motif is required for specific DNA recognition. However, point mutations and domain swap experiments between ROR alpha 1 and NGFI-B demonstrated that sequence-specific recognition dictated by the carboxy-terminal extension is determined by distinct subdomains in the two receptors. These results demonstrate that monomeric nuclear receptors utilize diverse mechanisms to achieve high-affinity and specific DNA binding and that ROR alpha 1 represents the prototype for a distinct subfamily of monomeric orphan nuclear receptors.
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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.