ArticleNucleic acids research2004
Functional role of G9a-induced histone methylation in small heterodimer partner-mediated transcriptional repression.
Article in Nucleic acids research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
32 citing papers in PubMed, 66 citations in OpenAlex.
- Review
- Article
- Nuclear receptors and transcriptional regulation in non-alcoholic fatty liver disease.Molecular metabolism · 2021Review
- The polycomb group protein PCGF6 mediates germline gene silencing by recruiting histone-modifying proteins to target gene promoters.The Journal of biological chemistry · 2020Article
- Up to date on cholesterol 7 alpha-hydroxylase (CYP7A1) in bile acid synthesis.Liver research (Beijing, China) · 2020Article
- Epigenetic regulation of drug metabolism and transport.Acta pharmaceutica Sinica. B · 2015Review
- Structural basis for corepressor assembly by the orphan nuclear receptor TLX.Genes & development · 2015Article
- Role of Nuclear Receptors in Central Nervous System Development and Associated Diseases.Journal of experimental neuroscience · 2015Review
- Structural insights into gene repression by the orphan nuclear receptor SHP.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Bile acid signal-induced phosphorylation of small heterodimer partner by protein kinase Cζ is critical for epigenomic regulation of liver metabolic genes.The Journal of biological chemistry · 2013Article
- Epigenomic regulation of bile acid metabolism: emerging role of transcriptional cofactors.Molecular and cellular endocrinology · 2013Review
- Prox1 directly interacts with LSD1 and recruits the LSD1/NuRD complex to epigenetically co-repress CYP7A1 transcription.PloS one · 2013Article
- Chromatin-targeting small molecules cause class-specific transcriptional changes in pancreatic endocrine cells.Proceedings of the National Academy of Sciences of the United States of America · 2012Article
- Involvement of liver X receptor alpha in histone modifications across the target fatty acid synthase gene.Lipids · 2012Article
- A pleiotropic role for the orphan nuclear receptor small heterodimer partner in lipid homeostasis and metabolic pathways.Journal of lipids · 2012Article
- Role of nuclear receptor SHP in metabolism and cancer.Biochimica et biophysica acta · 2011Review
- Regulation of FXR transcriptional activity in health and disease: Emerging roles of FXR cofactors and post-translational modifications.Biochimica et biophysica acta · 2011Review
- Ligand-dependent regulation of the activity of the orphan nuclear receptor, small heterodimer partner (SHP), in the repression of bile acid biosynthetic CYP7A1 and CYP8B1 genes.Molecular endocrinology (Baltimore, Md.) · 2011Article
- Insights into the binding mode and mechanism of action of some atypical retinoids as ligands of the small heterodimer partner (SHP).Journal of computer-aided molecular design · 2010Article
- Novel polymorphisms of nuclear receptor SHP associated with functional and structural changes.The Journal of biological chemistry · 2010Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Site-specific modification of nucleosomal histones plays a central role in the formation of transcriptionally active and inactive chromatin structures. These modifications may serve as specific recognition motifs for chromatin proteins, which act as a signal for the adoption of the appropriate regulatory responses. Here, we show that the orphan nuclear receptor SHP (small heterodimer partner), a coregulator that inhibits the activity of several nuclear receptors, can associate with unmodified and lysine 9-methylated histone-3, but not with the acetylated protein. The naturally occurring SHP mutant (R213C), which exhibits decreased transrepression potential, interacts less avidly with K9-methylated histone 3. We demonstrate that SHP can functionally interact with histone deacetylase-1 and the G9a methyltransferase and that it is localized exclusively in nuclease-sensitive euchromatin. The results point to the involvement of a multistep mechanism in SHP-dependent transcriptional repression, which includes histone deacetylation, followed by H3-K9 methylation and stable association of SHP itself with chromatin.
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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.