ArticleScientific reports2017
Conjunction of potential G-quadruplex and adjacent cis-elements in the 5' UTR of hepatocyte nuclear factor 4-alpha strongly inhibit protein expression.
Article in Scientific reports, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 15 citations in OpenAlex.
- RNA G-quadruplex structure targeting and imaging: recent advances and future directions.RNA (New York, N.Y.) · 2025Review
- Overexpression of DTX1 inhibits D-GalN/TNF-α-induced pyroptosis and inflammation in hepatocytes by regulating NLRP3 ubiquitination.Toxicology research · 2024Article
- The Functional Meaning of 5'UTR in Protein-Coding Genes.International journal of molecular sciences · 2023Review
- Reversal of G-Quadruplexes' Role in Translation Control When Present in the Context of an IRES.Biomolecules · 2022Review
- Quadruplex Ligands in Cancer Therapy.Cancers · 2021Review
- Article
- An Updated Focus on Quadruplex Structures as Potential Therapeutic Targets in Cancer.International journal of molecular sciences · 2020Review
- Translational Inhibition of α-Neurexin 2.Scientific reports · 2020Article
- Role of hepatocyte nuclear factor 4-alpha in gastrointestinal and liver diseases.World journal of gastroenterology · 2019Review
- Colocalization of mACS central science · 2019Review
- Novel mechanisms of regulation of the expression and transcriptional activity of hepatocyte nuclear factor 4α.Journal of cellular biochemistry · 2019Article
- Conjunction of G-quadruplex and stem-loop in the 5' untranslated region of mouse hepatocyte nuclear factor 4-alpha1 mediates strong inhibition of protein expression.Molecular and cellular biochemistry · 2018Article
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2 authors at 1 institution in 1 country.
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Abstract
Hepatocyte nuclear factor 4-alpha (HNF4α) is a well established master regulator of liver development and function. We identified the in vitro presence of a stable secondary structure, G-quadruplex (G4) in the 5' UTR of P1-HNF4A, the predominant HNF4α isoform(s) in adult liver. Our data suggest that the cooperation of G4 and the adjacent putative protein-binding sites within the 5' UTR was necessary and sufficient to mediate a strong translational repression. This was supported by analysis of deleted/mutated 5'UTRs and two native regulatory single-nucleotide polymorphisms in the 5'UTR. Additional results indicated that G4 motifs in the 5' UTRs of other liver-enriched transcription factors also inhibited protein expression. Moreover, pyridostatin, a G4 ligand, specifically potentiated the translational suppressing effect of P1-HNF4A-5' UTR. In summary, the present study provides the first evidence of the presence of G4 in human P1-HNF4A-5' UTR in vitro, and establishes a novel working model of strong inhibition of protein translation via interactions of G4 with potential RNA-binding proteins (RBPs). The protein expression of the tumor suppressor HNF4α may be inhibited by interactions of RBPs with the G4 motif in the 5' UTR to promote cell proliferation during liver development and carcinogenesis.
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