Identification of oleoylethanolamide as an endogenous ligand for HIF-3α
Open accessAbstract
Hypoxia-inducible factors (HIFs) are α/β heterodimeric transcription factors modulating cellular responses to the low oxygen condition. Among three HIF-α isoforms, HIF-3α is the least studied to date. Here we show that oleoylethanolamide (OEA), a physiological lipid known to regulate food intake and metabolism, binds selectively to HIF-3α. Through crystallographic analysis of HIF-3 α/β heterodimer in both apo and OEA-bound forms, hydrogen-deuterium exchange mass spectrometry (HDX-MS), molecular dynamics (MD) simulations, and biochemical and cell-based assays, we unveil the molecular mechanism of OEA entry and binding to the PAS-B pocket of HIF-3α, and show that it leads to enhanced heterodimer stability and functional modulation of HIF-3. The identification of HIF-3α as a selective lipid sensor is consistent with recent human genetic findings linking HIF-3α with obesity, and demonstrates that endogenous metabolites can directly interact with HIF-α proteins to modulate their activities, potentially as a regulatory mechanism supplementary to the well-known oxygen-dependent HIF-α hydroxylation.
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The PAS domains across the bHLH-PAS family are likely to act as ligand-sensing sites, as evidenced by AHR endogenous ligands such as FICZ and a recently identified metabolite ligand for HIF-3α, oleoylethanolamide.
“The PAS domains across this family are likely to act as ligand-sensing sites, as best evidenced by previously established AHR endogenous ligands such as FICZ, and a recently identified metabolite ligand for HIF-3α, oleoylethanolamide34.”
From Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex (2025) · cites this paper as [34]
Site-directed mutagenesis was confirmed by DNA sequencing.
“Site-directed mutagenesis was performed as previously34, and confirmed by DNA sequencing.”
From Structural basis for the ligand-dependent activation of heterodimeric AHR-ARNT complex (2025) · cites this paper as [34]
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Targeting hypoxia-inducible factors: therapeutic opportunities and challenges
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- Authors
- Diao, X., Ye, F., Zhang, M., Ren, X., Tian, X., Lu, J., Sun, X., Hou, Z., Chen, X., Li, F., Zhuang, J., Ding, H., Peng, C., Rastinejad, F., Luo, C., & Wu, D.
- Affiliations
- Shandong University (CN)
- Zhejiang Chinese Medical University (CN)
- Chinese Academy of Sciences (CN)
- University of Oxford (GB)
- Corresponding author
- Rastinejad, Fraydoon
- Luo, Cheng
- Wu, Dalei
- ORCID
- Venue
- Nature Communications
- Published
- 2022-05-09
- Volume
- 13
- Issue
- 1
- Pages
- 2529-2529
- ISSN
- 2041-1723 (ISSN-L)
- PMC
- PMC9085743
- OpenAlex
- W4229372258
- Cited by
- 51
- References
- 72
- Citations by year
- 2026: 10 · 2025: 15 · 2024: 9 · 2023: 12 · 2022: 5
- FWCI
- 4.32
- Type
- journal article
- Language
- en
- Open access
- gold
- doi.org
- Locations
- Nature Communications (publishedVersion, cc-by)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- RePEc: Research Papers in Economics (submittedVersion)
- DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
- Funders
- National Natural Science Foundation of China (22177063)
- Natural Science Foundation of Shandong Province (ZR2021JQ30)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Lipids, and Metabolism
- Physical Sciences › Materials Science › Materials Chemistry › Enzyme Structure and Function
- Keywords
- oleoylethanolamide, HIF-3α, hypoxia-inducible factor, lipid binding, heterodimer stability, endogenous ligands, lipid sensing, obesity, crystal structure, hydrogen-deuterium exchange mass spectrometry
- MeSH terms
- Humans, Ligands, Oleic Acids, Oxygen, Repressor Proteins, Apoptosis Regulatory Proteins, Basic Helix-Loop-Helix Proteins, Basic Helix-Loop-Helix Transcription Factors, Hypoxia-Inducible Factor 1, alpha Subunit, Endocannabinoids
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