ArticleMolecular and cellular biology1995
Exclusive homodimerization of the orphan receptor hepatocyte nuclear factor 4 defines a new subclass of nuclear receptors.
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 67 papers.
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Who cites it
67 citing papers in PubMed, 185 citations in OpenAlex.
- The role of HNF4α in adenocarcinoma.Biochemical Society transactions · 2026Review
- HNF4α isoforms regulate the circadian balance between carbohydrate and lipid metabolism in the liver.Frontiers in endocrinology · 2023Article
- HNF4α isoforms: the fraternal twin master regulators of liver function.Frontiers in endocrinology · 2023Review
- Long-Term Dietary Taurine Lowers Plasma Levels of Cholesterol and Bile Acids.International journal of molecular sciences · 2022Article
- Retinoic acid signaling drives differentiation toward the absorptive lineage in colorectal cancer.iScience · 2021Article
- Review
- Human Hepatocyte Nuclear Factor 4-α Encodes Isoforms with Distinct Transcriptional Functions.Molecular & cellular proteomics : MCP · 2020Article
- Article
- Conservation of DNA and ligand binding properties of retinoid X receptor from the placozoan Trichoplax adhaerens to human.The Journal of steroid biochemistry and molecular biology · 2018Review
- HNF-4 participates in the hibernation-associated transcriptional regulation of the chipmunk hibernation-related protein gene.Scientific reports · 2017Article
- Peak-valley-peak pattern of histone modifications delineates active regulatory elements and their directionality.Nucleic acids research · 2016Article
- Exploring the emerging complexity in transcriptional regulation of energy homeostasis.Nature reviews. Genetics · 2015Review
- Differential Effects of Hepatocyte Nuclear Factor 4α Isoforms on Tumor Growth and T-Cell Factor 4/AP-1 Interactions in Human Colorectal Cancer Cells.Molecular and cellular biology · 2015Article
- Transcriptional Factors Mediating Retinoic Acid Signals in the Control of Energy Metabolism.International journal of molecular sciences · 2015Review
- Recent advances in 2D and 3D in vitro systems using primary hepatocytes, alternative hepatocyte sources and non-parenchymal liver cells and their use in investigating mechanisms of hepatotoxicity, cell signaling and ADME.Archives of toxicology · 2013Review
- Multiple roles of COUP-TFII in cancer initiation and progression.Journal of molecular endocrinology · 2012Review
- Localization of hepatocyte nuclear factor-4α in the nucleolus and nucleus is regulated by its C-terminus.Journal of diabetes investigation · 2012Article
- Identification of a binding motif specific to HNF4 by comparative analysis of multiple nuclear receptors.Nucleic acids research · 2012Article
- Coordinate regulation of lipid metabolism by novel nuclear receptor partnerships.PLoS genetics · 2012Article
- Nuclear receptor HNF4α binding sequences are widespread in Alu repeats.BMC genomics · 2011Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hepatocyte nuclear factor 4 (HNF-4), a highly conserved member of the steroid hormone receptor superfamily critical for development and liver-specific gene expression, is very similar to another superfamily member, retinoid X receptor alpha (RXR alpha), in overall amino acid sequence and DNA binding specificity. Since RXR alpha is known to heterodimerize with many other nuclear receptors, the formation of heterodimers between HNF-4 and RXR alpha was examined. With the electrophoretic mobility shift assay, coimmunoprecipitation, and transient transfection assays, it is shown that, unlike other nuclear receptors, HNF-4 does not form heterodimers with RXR alpha either in the presence or in the absence of DNA. We also show that in vitro-translated HNF-4 does not form heterodimeric complexes on DNA with a number of other receptors, including RXR beta, RXR gamma, retinoic acid receptor alpha, or thyroid hormone receptor alpha. To investigate the hypothesis that the lack of heterodimerization between HNF-4 and RXR alpha is due to a strong homodimerization activity of HNF-4, glycerol gradient sedimentation and kinetic analysis were used to show that HNF-4 is in fact a stable homodimer in solution. Finally, immunohistochemistry is used to show that the HNF-4 protein is found exclusively in the nuclei in both HepG2 cells, which express endogenous HNF-4, and transfected COS cells, which overexpress HNF-4. These findings lead us to propose that HNF-4 defines a new subclass of nuclear receptors which reside primarily in the nucleus and which bind DNA and regulate transcription as homodimers.
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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.