ArticleeLife2016
An oxygen-insensitive Hif-3α isoform inhibits Wnt signaling by destabilizing the nuclear β-catenin complex.
Article in eLife, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- HIF-mediated hierarchical hypoxic adaptation, a novel paradigm in heart failure pathogenesis: is there a role for targeted therapies?Frontiers in pharmacology · 2026Review
- Genome-wide DNA methylation changes after 24 hours at high altitude.Environmental epigenetics · 2026Article
- HIF-3α/PPAR-γ Regulates Hypoxia Tolerance by Altering Glycolysis and Lipid Synthesis in Blunt Snout Bream (International journal of molecular sciences · 2025Article
- Hypoxia inducible factor 3-alpha promotes a malignant phenotype in colorectal cancer cells.IUBMB life · 2025Article
- Expression of HIF‑α and their association with clinicopathological parameters in clinical renal cell carcinoma.Upsala journal of medical sciences · 2024Article
- Hypoxia Pathway Proteins are Master Regulators of Erythropoiesis.International journal of molecular sciences · 2020Review
- A long hypoxia-inducible factor 3 isoform 2 is a transcription activator that regulates erythropoietin.Cellular and molecular life sciences : CMLS · 2020Article
- Wnt5b integrates Fak1a to mediate gastrulation cell movements via Rac1 and Cdc42.Open biology · 2020Article
- Pro-inflammatory cytokines activate hypoxia-inducible factor 3α via epigenetic changes in mesenchymal stromal/stem cells.Scientific reports · 2018Article
Corrections and comments
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Authors and funding
5 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Hypoxia-inducible factors (HIFs), while best known for their roles in the hypoxic response, have oxygen-independent roles in early development with poorly defined mechanisms. Here, we report a novel Hif-3α variant, Hif-3α2, in zebrafish. Hif-3α2 lacks the bHLH, PAS, PAC, and ODD domains, and is expressed in embryonic and adult tissues independently of oxygen availability. Hif-3α2 is a nuclear protein with significant hypoxia response element (HRE)-dependent transcriptional activity. Hif-3α2 overexpression not only decreases embryonic growth and developmental timing but also causes left-right asymmetry defects. Genetic deletion of Hif-3α2 by CRISPR/Cas9 genome editing increases, while Hif-3α2 overexpression decreases, Wnt/β-catenin signaling. This action is independent of its HRE-dependent transcriptional activity. Mechanistically, Hif-3α2 binds to β-catenin and destabilizes the nuclear β-catenin complex. This mechanism is distinct from GSK3β-mediated β-catenin degradation and is conserved in humans. These findings provide new insights into the oxygen-independent actions of HIFs and uncover a novel mechanism regulating Wnt/β-catenin signaling.
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Registered trials
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