ArticleNucleic acids research1998
Multiple parameters determine the specificity of transcriptional response by nuclear receptors HNF-4, ARP-1, PPAR, RAR and RXR through common response elements.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 100 citations in OpenAlex.
- Review
- Gain-of-Function MN1 Truncation Variants Cause a Recognizable Syndrome with Craniofacial and Brain Abnormalities.American journal of human genetics · 2020Article
- Discovery of peroxisome proliferator-activated receptor α (PPARα) activators with a ligand-screening system using a human PPARα-expressing cell line.The Journal of biological chemistry · 2018Article
- Hnf4α is involved in the regulation of vertebrate LC-PUFA biosynthesis: insights into the regulatory role of Hnf4α on expression of liver fatty acyl desaturases in the marine teleost Siganus canaliculatus.Fish physiology and biochemistry · 2018Article
- On the Utility of ToxCast™ and ToxPi as Methods for Identifying New Obesogens.Environmental health perspectives · 2016Article
- Nuclear receptors and epigenetic regulation: opportunities for nutritional targeting and disease prevention.Advances in nutrition (Bethesda, Md.) · 2014Review
- Role of COUP-TFI during retinoic acid-induced differentiation of P19 cells to endodermal cells.Journal of cellular physiology · 2013Article
- HNF4α antagonists discovered by a high-throughput screen for modulators of the human insulin promoter.Chemistry & biology · 2012Article
- Identification of a binding motif specific to HNF4 by comparative analysis of multiple nuclear receptors.Nucleic acids research · 2012Article
- Evolution of gene regulation of pluripotency--the case for wiki tracks at genome browsers.Biology direct · 2010Article
- The Peroxisomal 3-keto-acyl-CoA thiolase B Gene Expression Is under the Dual Control of PPARα and HNF4α in the Liver.PPAR research · 2010Article
- Selenoprotein P regulation by the glucocorticoid receptor.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2009Article
- Cross-Talk between PPARs and the Partners of RXR: A Molecular Perspective.PPAR research · 2009Article
- The MODY1 gene for hepatocyte nuclear factor 4alpha and a feedback loop control COUP-TFII expression in pancreatic beta cells.Molecular and cellular biology · 2008Article
- The Role of PPARs in Cancer.PPAR research · 2008Article
- The MN1 oncoprotein synergizes with coactivators RAC3 and p300 in RAR-RXR-mediated transcription.Oncogene · 2003Article
- Co-operation of the transcription factor hepatocyte nuclear factor-4 with Sp1 or Sp3 leads to transcriptional activation of the human haem oxygenase-1 gene promoter in a hepatoma cell line.The Biochemical journal · 2002Article
- Regulation of aromatase promoter activity in human breast tissue by nuclear receptors.Oncogene · 2002Article
- Critical roles of nuclear receptor response elements in replication of hepatitis B virus.Journal of virology · 2001Article
- Transcriptional activation by hepatocyte nuclear factor-4 in a cell-free system derived from rat liver nuclei.Nucleic acids research · 2001Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
A number of nuclear receptors, including retinoic acid receptors (RARs), retinoid-X receptors (RXRs), hepatocyte nuclear factor 4 (HNF-4), chicken ovalbumin upstream promoter transcription factor I (COUP-TFI), apolipoprotein regulatory protein 1 (ARP-1) and peroxisome proliferator-activated receptor (PPAR), bind to response elements comprised of two core motifs, 5'-RG(G/T)TCA, or a closely related sequence separated by 1 nt (DR1 elements). The potential role of the precise sequence of the core motif as well as the spacer nucleotide in determining specificity and promiscuity of receptor-response element interactions was investigated. We show here that nucleotides at base positions 1, 2 and 4 of the core motif as well as the spacer nucleotide determine the binding preference of HNF-4 and ARP-1 homodimers and RAR:RXR and PPAR:RXR heterodimers. In transfection experiments transcriptional activation by HNF-4 and PPAR:RXR and repression by ARP-1 correlated with the relative in vitro binding affinity provided the element was located within the proper promoter context. Furthermore, promoter context also determined whether an element that binds to HNF-4 and PPAR:RXR with equal affinity functions as an HNF-4 response element or PPAR response element. Thus, apart from the element-specific differences in affinity for the receptors, additional promoter-specific transcription factors that interact with HNF-4 and PPAR:RXR determine the specificity of transcriptional response through DR1-type elements.
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