ArticleOncotarget2014
Acetylation-defective mutant of Pparγ is associated with decreased lipid synthesis in breast cancer cells.
Article in Oncotarget, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
26 citing papers in PubMed, 38 citations in OpenAlex.
- Crosstalk between cysteine and lysine modifications: Integrating redox and metabolic regulation.Redox biology · 2026Review
- Article
- PPARγ acetylation governs mammary adenocarcinoma tumor growth via acetylated residues that determine DNA sequence-specific binding.Oncogene · 2025Article
- PPAR-γ in Melanoma and Immune Cells: Insights into Disease Pathogenesis and Therapeutic Implications.Cells · 2025Review
- ACSS2 controls PPARγ activity homeostasis to potentiate adipose-tissue plasticity.Cell death and differentiation · 2024Article
- Sirtuin Inhibitor Cambinol Induces Cell Differentiation and Differently Interferes with SIRT1 and 2 at the Substrate Binding Site.Biomedicines · 2023Article
- Comparison of protective effects of hesperetin and pectolinarigenin on high-fat diet-induced hyperlipidemia and hepatic steatosis in Golden Syrian hamsters.Experimental animals · 2023Article
- Acetylated-PPARγ expression is regulated by differentCancer biology & medicine · 2023Article
- The Role of Peroxisome Proliferator-Activated Receptor Gamma and Atherosclerosis: Post-translational Modification and Selective Modulators.Frontiers in physiology · 2022Review
- Hepatic PPARα Is Destabilized by SIRT1 Deacetylase in Undernourished Male Mice.Frontiers in nutrition · 2022Article
- RORγt protein modifications and IL-17-mediated inflammation.Trends in immunology · 2021Review
- Article
- The PPARPPAR research · 2020Review
- Aryl hydrocarbon receptor (AhR) regulates adipocyte differentiation by assembling CRL4B ubiquitin ligase to target PPARγ for proteasomal degradation.The Journal of biological chemistry · 2019Article
- Troglitazone activates TRPV1 and causes deacetylation of PPARγ in 3T3-L1 cells.Biochimica et biophysica acta. Molecular basis of disease · 2019Article
- Functional Regulation of PPARs through Post-Translational Modifications.International journal of molecular sciences · 2018Review
- Ginkgolic acid, a sumoylation inhibitor, promotes adipocyte commitment but suppresses adipocyte terminal differentiation of mouse bone marrow stromal cells.Scientific reports · 2018Article
- Implication of atypical supraclavicular F18-fluorodeoxyglucose uptake in patients with breast cancer: Association between brown adipose tissue and breast cancer.Oncology letters · 2017Article
- PPARs: regulators of metabolism and as therapeutic targets in cardiovascular disease. Part II: PPAR-β/δ and PPAR-γ.Future cardiology · 2017Review
- Metabolism and acetylation in innate immune cell function and fate.Seminars in immunology · 2016Review
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 1 country.
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Abstract
In our prior publications we characterized a conserved acetylation motif (K(R)xxKK) of evolutionarily related nuclear receptors. Recent reports showed that peroxisome proliferator activated receptor gamma (PPARγ) deacetylation by SIRT1 is involved in delaying cellular senescence and maintaining the brown remodeling of white adipose tissue. However, it still remains unknown whether lysyl residues 154 and 155 (K154/155) of the conserved acetylation motif (RIHKK) in Pparγ1 are acetylated. Herein, we demonstrate that Pparγ1 is acetylated and regulated by both endogenous TSA-sensitive and NAD-dependent deacetylases. Acetylation of lysine 154 was identified by mass spectrometry (MS) while deacetylation of lysine 155 by SIRT1 was confirmed by in vitro deacetylation assay. An in vivo labeling assay revealed K154/K155 as bona fide acetylation sites. The conserved acetylation sites of Pparγ1 and the catalytic domain of SIRT1 are both required for the interaction between Pparγ1 and SIRT1. Sirt1 and Pparγ1 converge to govern lipid metabolism in vivo. Acetylation-defective mutants of Pparγ1 were associated with reduced lipid synthesis in ErbB2 overexpressing breast cancer cells. Together, these results suggest that the conserved lysyl residues K154/K155 of Pparγ1 are acetylated and play an important role in lipid synthesis in ErbB2-positive breast cancer cells.
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Registered trials
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