ArticleProceedings of the National Academy of Sciences of the United States of America1995
Recruitment of hepatocyte nuclear factor 4 into specific intranuclear compartments depends on tyrosine phosphorylation that affects its DNA-binding and transactivation potential.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 88 citations in OpenAlex.
- Multiomics Analyses of HNF4α Protein Domain Function during Human Pluripotent Stem Cell Differentiation.iScience · 2019Article
- ROCK inhibition enhances microRNA function by promoting deadenylation of targeted mRNAs via increasing PAIP2 expression.Nucleic acids research · 2015Article
- The hepatitis B virus (HBV) HBx protein activates AKT to simultaneously regulate HBV replication and hepatocyte survival.Journal of virology · 2015Article
- Role of hepatocyte nuclear factor 4α (HNF4α) in cell proliferation and cancer.Gene expression · 2015Review
- Hepatocyte nuclear factor 4-alpha involvement in liver and intestinal inflammatory networks.World journal of gastroenterology · 2014Review
- Quantitative analysis of cytokine-induced hepatocyte nuclear factor-4α phosphorylation by mass spectrometry.Biochemistry · 2011Article
- Proteomic analysis of native hepatocyte nuclear factor-4α (HNF4α) isoforms, phosphorylation status, and interactive cofactors.The Journal of biological chemistry · 2011Article
- Hepatocyte nuclear factor 4alpha regulation of bile acid and drug metabolism.Expert opinion on drug metabolism & toxicology · 2009Review
- Nuclear receptors: mediators and modifiers of inflammation-induced cholestasis.Frontiers in bioscience (Landmark edition) · 2009Review
- Activation of bile acid biosynthesis by the p38 mitogen-activated protein kinase (MAPK): hepatocyte nuclear factor-4alpha phosphorylation by the p38 MAPK is required for cholesterol 7alpha-hydroxylase expression.The Journal of biological chemistry · 2007Article
- Mitogen-activated protein kinase-mediated disruption of enhancer-promoter communication inhibits hepatocyte nuclear factor 4alpha expression.Molecular and cellular biology · 2006Article
- Bile acids and cytokines inhibit the human cholesterol 7 alpha-hydroxylase gene via the JNK/c-jun pathway in human liver cells.Hepatology (Baltimore, Md.) · 2006Article
- Phosphorylation of Ser158 regulates inflammatory redox-dependent hepatocyte nuclear factor-4alpha transcriptional activity.The Biochemical journal · 2006Article
- Role of HNF4alpha in the superinduction of the IL-1beta-activated iNOS gene by oxidative stress.The Biochemical journal · 2006Article
- The G115S mutation associated with maturity-onset diabetes of the young impairs hepatocyte nuclear factor 4alpha activities and introduces a PKA phosphorylation site in its DNA-binding domain.The Biochemical journal · 2004Article
- Expression and localization of P1 promoter-driven hepatocyte nuclear factor-4α (HNF4α) isoforms in human and rats.Nuclear receptor · 2003Article
- Hepatocyte nuclear factor 4 response to injury involves a rapid decrease in DNA binding and transactivation via a JAK2 signal transduction pathway.The Biochemical journal · 2002Article
- Regulatory mechanisms controlling human hepatocyte nuclear factor 4alpha gene expression.Molecular and cellular biology · 2001Article
- Activity-dependent nuclear translocation and intranuclear distribution of NFATc in adult skeletal muscle fibers.The Journal of cell biology · 2001Article
- Identification and characterization of cis-acting elements conferring insulin responsiveness on hamster cholesterol 7alpha-hydroxylase gene promoter.The Biochemical journal · 2000Article
Corrections and comments
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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) is a prominent member of the family of liver-enriched transcription factors, playing a role in the expression of a large number of liver-specific genes. We report here that HNF-4 is a phosphoprotein and that phosphorylation at tyrosine residue(s) is important for its DNA-binding activity and, consequently, for its transactivation potential both in cell-free systems and in cultured cells. Tyrosine phosphorylation did not affect the transport of HNF-4 from the cytoplasm to the nucleus but had a dramatic effect on its subnuclear localization. HNF-4 was concentrated in distinct nuclear compartments, as evidenced by in situ immunofluorescence and electron microscopy. This compartmentalization disappeared when tyrosine phosphorylation was inhibited by genistein. The correlation between the intranuclear distribution of HNF-4 and its ability to activate endogenous target genes demonstrates a phosphorylation signal-dependent pathway in the regulation of transcription factor activity.
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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.