ArticlePloS one2013
SIRT1 is a direct coactivator of thyroid hormone receptor β1 with gene-specific actions.
Article in PloS one, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.
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Who cites it
39 citing papers in PubMed, 68 citations in OpenAlex.
- SIRT1 in Senescence: Mitochondria and Immune Crosstalk.Biology · 2026Review
- A Function-Centric Framework for Mitochondrial Quality Control.Biomolecules · 2026Review
- Resmetirom and thyroid hormone receptor-targeted treatment for metabolic dysfunction-associated steatotic liver disease (MASLD).Portal hypertension & cirrhosis · 2025Article
- Actions of thyroid hormones and thyromimetics on the liver.Nature reviews. Gastroenterology & hepatology · 2025Review
- Thyroid hormone receptor beta (THRβ1) is the major regulator of T3 action in human iPSC-derived hepatocytes.Molecular metabolism · 2024Article
- Metabolic Messengers: Thyroid Hormones.Nature metabolism · 2024Review
- Polyphenols alleviate metabolic disorders: the role of ubiquitin-proteasome system.Frontiers in nutrition · 2024Review
- Hepatic Energy Metabolism under the Local Control of the Thyroid Hormone System.International journal of molecular sciences · 2023Review
- The role of Sirtuin 1 in the pathophysiology of polycystic ovary syndrome.European journal of medical research · 2022Review
- Thyroid hormone signaling in the intestinal stem cells and their niche.Cellular and molecular life sciences : CMLS · 2022Review
- Elevated thyroid hormones caused by high concentrate diets participate in hepatic metabolic disorders in dairy cows.Animal bioscience · 2022Article
- Effects of Thyroid Hormones on Lipid Metabolism Pathologies in Non-Alcoholic Fatty Liver Disease.Biomedicines · 2022Review
- Development of Thyroid Hormones and Synthetic Thyromimetics in Non-Alcoholic Fatty Liver Disease.International journal of molecular sciences · 2022Review
- Thymoquinone protects the testes of hypothyroid rats by suppressing pro-inflammatory cytokines and oxidative stress and promoting SIRT1 testicular expression.Frontiers in pharmacology · 2022Article
- Hepatic PPARα Is Destabilized by SIRT1 Deacetylase in Undernourished Male Mice.Frontiers in nutrition · 2022Article
- Association of serum free thyroxine and glucose homeostasis: Korea National Health and Nutrition Examination Survey.The Korean journal of internal medicine · 2021Article
- Thyroid Hormone-Regulated Expression of Period2 Promotes Liver Urate Production.Frontiers in cell and developmental biology · 2021Article
- Moderate SIRT1 overexpression protects against brown adipose tissue inflammation.Molecular metabolism · 2020Article
- Metabolic Functions of G Protein-Coupled Receptors in Hepatocytes-Potential Applications for Diabetes and NAFLD.Biomolecules · 2020Review
- The long-term oral administration of thyroxine: effects on blood hematological and biochemical features in broiler breeder hens.Poultry science · 2019Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 1 country.
Funding
Abstract
Sirtuin 1 (SIRT1) NAD(+)-dependent deacetylase regulates energy metabolism by modulating expression of genes involved in gluconeogenesis and other liver fasting responses. While many effects of SIRT1 on gene expression are mediated by deacetylation and activation of peroxisome proliferator activated receptor coactivator α (PGC-1α), SIRT1 also binds directly to DNA bound transcription factors, including nuclear receptors (NRs), to modulate their activity. Since thyroid hormone receptor β1 (TRβ1) regulates several SIRT1 target genes in liver and interacts with PGC-1α, we hypothesized that SIRT1 may influence TRβ1. Here, we confirm that SIRT1 cooperates with PGC-1α to enhance response to triiodothyronine, T3. We also find, however, that SIRT1 stimulates TRβ1 activity in a manner that is independent of PGC-1α but requires SIRT1 deacetylase activity. SIRT1 interacts with TRβ1 in vitro, promotes TRβ1 deacetylation in the presence of T3 and enhances ubiquitin-dependent TRβ1 turnover; a common response of NRs to activating ligands. More surprisingly, SIRT1 knockdown only strongly inhibits T3 response of a subset of TRβ1 target genes, including glucose 6 phosphatase (G-6-Pc), and this is associated with blockade of TRβ1 binding to the G-6-Pc promoter. Drugs that target the SIRT1 pathway, resveratrol and nicotinamide, modulate T3 response at dual TRβ1/SIRT1 target genes. We propose that SIRT1 is a gene-specific TRβ1 co-regulator and TRβ1/SIRT1 interactions could play important roles in regulation of liver metabolic response. Our results open possibilities for modulation of subsets of TR target genes with drugs that influence the SIRT1 pathway.
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