Sirtuin 1 Modulates Cellular Responses to Hypoxia by Deacetylating Hypoxia-Inducible Factor 1α
Open accessAbstract
To survive in hypoxic environments, organisms must be able to cope with redox imbalance and oxygen deficiency. The SIRT1 deacetylase and the HIF-1alpha transcription factor act as redox and oxygen sensors, respectively. Here, we found that SIRT1 binds to HIF-1alpha and deacetylates it at Lys674, which is acetylated by PCAF. By doing so, SIRT1 inactivated HIF-1alpha by blocking p300 recruitment and consequently repressed HIF-1 target genes. During hypoxia, SIRT1 was downregulated due to decreased NAD(+) levels, which allowed the acetylation and activation of HIF-1alpha. Conversely, when the redox change was attenuated by blocking glycolysis, SIRT1 was upregulated, leading to the deacetylation and inactivation of HIF-1alpha even in hypoxia. In addition, we confirmed the SIRT1-HIF-1alpha interaction in hypoxic mouse tissues and observed in vivo that SIRT1 has negative effects on tumor growth and angiogenesis. Our results suggest that crosstalk between oxygen- and redox-responsive signal transducers occurs through the SIRT1-HIF-1alpha interaction.
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When hypoxia is induced, NAD+/NADH levels increase due to glycolysis down-regulating SIRT-1, favoring HIF-1α activation.
“However, when hypoxia is induced, the NAD+/NADH levels increase due to glycolysis down-regulating SIRT-1 favoring HIF-1α activation69.”
From HIF-1α pathway: role, regulation and intervention for cancer therapy (2015) · cites this paper as [69]
The Results (‘Regulation of corepressor function by nuclear NADH’) report that the NAD+/NADH ratio significantly decreased during hypoxia, contrary to the claimed increase. The Results (‘SIRT1 Links Glycolysis with HIF-1 Signaling’) do support the downstream link: the shift leads to SIRT1 suppression and HIF-1α activation. (LLM, conf=0.91)
Checked by a reasoning model — may be wrong.
Experimental — accuracy not yet measuredHIF-1α acetylation by PCAF at K674 in low NAD+ is critical for promoting p300 recruitment and expression of HIF-1α target genes.
“Recent evidence indicates that HIF-1α acetylation by p300/CBP associated factor (PCAF) at K674 in an environment of low NAD+ is critical for promoting p300 recruitment and subsequent expression of HIF-1α target genes.”
From HIF-1α pathway: role, regulation and intervention for cancer therapy (2015) · cites this paper as [69]
SIRT1 opposes this reaction by catalyzing HIF-1α deacetylation at high NAD+ levels.
“Sirtuin 1 (SIRT 1), a redox-sensing deacetylase considered as class III histone deacetylase (HDAC), opposes this reaction by catalyzing HIF-1α deacetylation at high NAD+ levels.”
From HIF-1α pathway: role, regulation and intervention for cancer therapy (2015) · cites this paper as [69]
SirT1 negatively regulates HIF-1α activity in hypoxia by direct deacetylation.
“SirT1 was recently demonstrated to negatively regulate HIF-1α activity in hypoxia by direct deacetylation (Lim et al., 2010).”
From SirT3 suppresses hypoxia inducible factor 1α and tumor growth by inhibiting mitochondrial ROS production (2011) · cites this paper as Lim et al., 2010
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1 retracted
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“Accordingly, HIF-driven transcriptional reprogramming reflects a combination of HRE sequence preference, isoform-specific DNA binding, tissue-restricted cofactors [71,83,84], and epigenetic features such as enhancer – promoter interactions and chromatin accessibility [80,81, 85 – 87].”
- Authors
- Lim, J.-H., Lee, Y.-M., Chun, Y.-S., Chen, J., Kim, J.-E., & Park, J.-W.
- Affiliations
- Seoul National University (KR)
- The University of Texas MD Anderson Cancer Center (US)
- Kyung Hee University (KR)
- Corresponding author
- Kim, Ja-Eun
- Park, Jong-Wan
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2010-06
- Volume
- 38
- Issue
- 6
- Pages
- 864-878
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2011376105
- Cited by
- 758
- References
- 45
- Citations by year
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- FWCI
- 18.49
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer, Hypoxia, and Metabolism
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Histone Deacetylase Inhibitors Research
- Keywords
- SIRT1, HIF-1α, hypoxia, protein deacetylation, PCAF, P300, NAD+, glycolysis, redox signaling, oxygen sensing, HIF-1 target genes, tumor growth, angiogenesis, lysine acetylation
- MeSH terms
- Acetylation, Animals, Cell Line, Humans, Male, Mice, Nude, Neoplasm Transplantation, Neoplasms, Experimental, Neovascularization, Pathologic, Oxidation-Reduction, Transplantation, Heterologous, Cell Hypoxia, Protein Transport, Cell Line, Tumor, p300-CBP Transcription Factors, Mice, Hypoxia-Inducible Factor 1, alpha Subunit, Sirtuin 1
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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