Cited by 332Sirtuins and Resveratrol in MedicineCholesterol and Lipid MetabolismDrug Transport and Resistance Mechanisms

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FXR Acetylation Is Normally Dynamically Regulated by p300 and SIRT1 but Constitutively Elevated in Metabolic Disease States

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Kemper, Jongsook Kim, Xiao, Zhen, Ponugoti, Bhaskar, Miao, Ji, Fang, Sungsoon, Kanamaluru, Deepthi, Tsang, Stephanie, Wu, Shwu-Yuan, Chiang, Cheng-Ming, Veenstra, Timothy D.·2009·Cell Metabolism

DOI 10.1016/j.cmet.2009.09.009PMC PMC2785075

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Abstract

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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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
ORCID: Kemper, Jongsook Kim
Xiao, Zhen
Miao, Ji
Fang, Sungsoon
Veenstra, Timothy D.
Venue: Cell Metabolism
Publisher: Elsevier BV
Published: 2009-11
Volume: 10
Issue: 5
Pages: 392-404
ISSN: 1550-4131 (ISSN-L)
DOI: 10.1016/j.cmet.2009.09.009
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: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
www.elsevier.com/legal/tdmrep-license (tdm)
www.elsevier.com/open-access/userlicense/1.0/ (vor, 1390 d)
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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FXR Acetylation Is Normally Dynamically Regulated by p300 and SIRT1 but Constitutively Elevated in Metabolic Disease States

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