ArticleMolecular and cellular biology1997
Novel receptor interaction and repression domains in the orphan receptor SHP.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 132 citations in OpenAlex.
- Small heterodimer partner as a predictor of neoadjuvant radiochemotherapy response and survival in patients with rectal cancer: A preliminary study.Oncology letters · 2021Article
- Plasma Cell-Free DNA Methylomics of Bipolar Disorder With and Without Rapid Cycling.Frontiers in neuroscience · 2021Article
- Small Heterodimer Partner and Innate Immune Regulation.Endocrinology and metabolism (Seoul, Korea) · 2016Review
- The orphan nuclear receptor small heterodimer partner is required for thiazolidinedione effects in leptin-deficient mice.Journal of biomedical science · 2015Article
- Role of Nuclear Receptors in Central Nervous System Development and Associated Diseases.Journal of experimental neuroscience · 2015Review
- Liver receptor homolog-1 (LRH-1): a potential therapeutic target for cancer.Cancer biology & therapy · 2015Review
- TLR4 signaling and the inhibition of liver hepcidin expression by alcohol.World journal of gastroenterology · 2014Article
- 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
- A pleiotropic role for the orphan nuclear receptor small heterodimer partner in lipid homeostasis and metabolic pathways.Journal of lipids · 2012Article
- Regulation of human apolipoprotein m gene expression by orphan and ligand-dependent nuclear receptors.The Journal of biological chemistry · 2010Article
- Novel polymorphisms of nuclear receptor SHP associated with functional and structural changes.The Journal of biological chemistry · 2010Article
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- Differential inhibition of nuclear hormone receptor-dependent hepatitis B virus replication by the small heterodimer partner.Journal of virology · 2008Article
- A protein interaction atlas for the nuclear receptors: properties and quality of a hub-based dimerisation network.BMC systems biology · 2007Article
- An adamantyl-substituted retinoid-derived molecule that inhibits cancer cell growth and angiogenesis by inducing apoptosis and binds to small heterodimer partner nuclear receptor: effects of modifying its carboxylate group on apoptosis, proliferation, and protein-tyrosine phosphatase activity.Journal of medicinal chemistry · 2007Article
- Transcriptional repression of the gluconeogenic gene PEPCK by the orphan nuclear receptor SHP through inhibitory interaction with C/EBPalpha.The Biochemical journal · 2007Article
- Adamantyl-substituted retinoid-related molecules bind small heterodimer partner and modulate the Sin3A repressor.Cancer research · 2007Article
- Regulation of hepatic metabolic pathways by the orphan nuclear receptor SHP.The EMBO journal · 2005Article
- Role of an mSin3A-Swi/Snf chromatin remodeling complex in the feedback repression of bile acid biosynthesis by SHP.Molecular and cellular biology · 2004Article
- Functional role of G9a-induced histone methylation in small heterodimer partner-mediated transcriptional repression.Nucleic acids research · 2004Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
SHP (short heterodimer partner) is a novel orphan receptor that lacks a conventional DNA binding domain and interacts with other members of the nuclear hormone receptor superfamily. We have characterized the SHP sequences required for interaction with other superfamily members, and have defined an SHP repressor domain. In the mammalian two-hybrid system, a fusion of full-length SHP to the GAL4 DNA binding domain shows 9-cis-retinoic acid-dependent interaction with a VP16-retinoid X receptor alpha (RXR alpha) fusion. By deletion analysis, sequences required for this RXR interaction map to the central portion of SHP (amino acids 92 to 148). The same region is required for interaction with RXR in vitro and in the yeast two-hybrid system, and results from the yeast system suggest that the same SHP sequences are required for interaction with other members of the nuclear hormone receptor superfamily such as thyroid hormone receptor and retinoic acid receptor. In mammalian cells, a GAL4-SHP fusion protein shows about 10-fold-decreased transcriptional activation relative to GAL4 alone, and fusion of SHP to the C terminus of a GAL4-VP16 fusion to generate a triple chimera also results in a strong decrease in transactivation activity. Sequences required for this repressor function were mapped to the C terminus of SHP. This region is distinct from that required for corepressor interaction by other members of the nuclear hormone receptor superfamily, and SHP did not interact with N-CoR in either the yeast or mammalian two-hybrid system. Together, these results identify novel receptor interaction and repressor domains in SHP and suggest two distinct mechanisms for inhibition of receptor signaling pathways by SHP.
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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.