Abstract
Hypoxia-inducible transcription factors (HIF) form heterodimeric complexes that mediate cell responses to hypoxia. The oxygen-dependent stability and activity of the HIF-α subunits is traditionally associated to post-translational modifications such as hydroxylation, acetylation, ubiquitination, and phosphorylation. Here we report novel evidence showing that unsaturated fatty acids are naturally occurring, non-covalent structural ligands of HIF-3α, thus providing the initial framework for exploring its exceptional role as a lipid sensor under hypoxia.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Apoptosis Regulatory Proteins
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Basic Helix-Loop-Helix Transcription Factors / chemistry
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Basic Helix-Loop-Helix Transcription Factors / genetics
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Basic Helix-Loop-Helix Transcription Factors / metabolism*
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Cloning, Molecular
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Crystallography, X-Ray
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Escherichia coli / genetics
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Escherichia coli / metabolism
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Gene Expression
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Humans
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Ligands
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Linoleic Acid / chemistry
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Linoleic Acid / metabolism*
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Models, Molecular
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Monoglycerides / chemistry
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Monoglycerides / metabolism
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Neoplasms / genetics
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Neoplasms / metabolism*
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Neoplasms / pathology
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Oleic Acid / chemistry
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Oleic Acid / metabolism*
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Protein Binding
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Protein Structure, Secondary
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Protein Structure, Tertiary
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Recombinant Proteins / chemistry
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Recombinant Proteins / genetics
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Recombinant Proteins / metabolism
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Repressor Proteins
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Signal Transduction
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Stearic Acids / chemistry
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Stearic Acids / metabolism
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Tissue Array Analysis
Substances
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Apoptosis Regulatory Proteins
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Basic Helix-Loop-Helix Transcription Factors
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HIF3A protein, human
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Ligands
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Monoglycerides
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Recombinant Proteins
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Repressor Proteins
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Stearic Acids
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Oleic Acid
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stearic acid
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Linoleic Acid