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FXR Acetylation Is Normally Dynamically Regulated by p300 and SIRT1 but Constitutively Elevated in Metabolic Disease States
Open accessAbstract
The nuclear bile acid receptor FXR is critical for regulation of lipid and glucose metabolism. Here, we report that FXR is a target of SIRT1, a deacetylase that mediates nutritional and hormonal modulation of hepatic metabolism. Lysine 217 of FXR is the major acetylation site targeted by p300 and SIRT1. Acetylation of FXR increases its stability but inhibits heterodimerization with RXRalpha, DNA binding, and transactivation activity. Downregulation of hepatic SIRT1 increased FXR acetylation with deleterious metabolic outcomes. Surprisingly, in mouse models of metabolic disease, FXR interaction with SIRT1 and p300 was dramatically altered, FXR acetylation levels were elevated, and overexpression of SIRT1 or resveratrol treatment reduced acetylated FXR levels. Our data demonstrate that FXR acetylation is normally dynamically regulated by p300 and SIRT1 but is constitutively elevated in metabolic disease states. Small molecules that inhibit FXR acetylation by targeting SIRT1 or p300 may be promising therapeutic agents for metabolic disorders.
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“It has been demonstrated that the gene encoding FMO3 is a direct FXR target gene, and FXR has been found to be a target of sirtuin 1 (SIRT1) in metabolic regulation (23, 34, 35).”
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“Moreover, RSV increased the expression and activity of FMO3 in the liver, corresponding with previously published results (34).”
In the citing paper
“It has been demonstrated that the gene encoding FMO3 is a direct FXR target gene, and FXR has been found to be a target of sirtuin 1 (SIRT1) in metabolic regulation (23, 34, 35).”
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Self-citation
Metadata
- Authors
- Kemper, J. K., Xiao, Z., Ponugoti, B., Miao, J., Fang, S., Kanamaluru, D., Tsang, S., Wu, S.-Y., Chiang, C.-M., & Veenstra, T. D.
- Affiliations
- University of Illinois Urbana-Champaign (US)
- Frederick National Laboratory for Cancer Research (US)
- Harold C. Simmons Comprehensive Cancer Center (US)
- Corresponding author
- Kemper, Jongsook Kim
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2009-11
- Volume
- 10
- Issue
- 5
- Pages
- 392-404
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC2785075
- OpenAlex
- W1983620925
- Cited by
- 332
- References
- 39
- Citations by year
- 2026: 12 · 2025: 16 · 2024: 10 · 2023: 15 · 2022: 17 · 2021: 16 · 2020: 22 · 2019: 20 · 2018: 23 · 2017: 22 · 2016: 15 · 2015: 18 · 2014: 29 · 2013: 29 · 2012: 30
- FWCI
- 16.12
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- DigitalCommons-Cedarville (Cedarville University) (submittedVersion)
- Funders
- National Institutes of Health (n01co12400-79-0-22)
- National Cancer Institute (N01CO12400, N01-CO-012400, CA103867, R01CA103867, R01CA124760, CA124760)
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK062777, R01DK080032, DK062777, R56DK062777, DK80032)
- Topics
- Health Sciences › Medicine › Geriatrics and Gerontology › Sirtuins and Resveratrol in Medicine
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Cholesterol and Lipid Metabolism
- Health Sciences › Medicine › Oncology › Drug Transport and Resistance Mechanisms
- Keywords
- farnesoid X receptor, protein acetylation, P300, SIRT1, receptor stability, DNA binding, transcriptional activation, hepatic metabolism, metabolic disorders, resveratrol, small molecule drugs
- MeSH terms
- Resveratrol, Receptor, Farnesoid X-Activated, p300-CBP-Associated Factor, Acetylation, Animals, Disease Models, Animal, Histone Deacetylases, Liver, Liver Diseases, Male, Stilbenes, Transcription Factors, Transcriptional Activation, Down-Regulation, Mutagenesis, Site-Directed, Receptors, Cytoplasmic and Nuclear, Dimerization, RNA, Small Interfering, Retinoid X Receptor alpha, p300-CBP Transcription Factors, Mice, Protein Stability, Sirtuin 1, Hep G2 Cells
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