ArticleProteins2026
Interplay of Ser273 Phosphorylation and K268 and K293 Acetylation in PPARγ: Implications for PPARγ Activation.
Article in Proteins, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
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Authors and funding
7 authors.
Funding
Abstract
Post-translational modifications (PTMs) play a critical role in regulating the transcriptional activity of PPARγ, a nuclear receptor central to glucose and lipid homeostasis. Among these, lysine acetylation at K268 and K293 and phosphorylation at S273 are particularly relevant to insulin sensitivity. These residues form a regulatory binding interface for protein partners such as SIRT1 and CDK5, which exert opposing effects on PPARγ activity-SIRT1 promoting deacetylation and insulin sensitization, and CDK5 driving phosphorylation linked to insulin resistance. Here we show that modifications at this interface influence PPARγ's interaction with its regulators and its transcriptional activity. Acetyl-mimetic mutations at K268 and K293 reduce CDK5 binding and phosphorylation, while enhancing transcriptional activity. Phosphorylation at S273 weakens SIRT1 binding and limits its repressive function, even under overexpression. These effects likely reflect both direct interference with protein docking and changes in the global acetylation or phosphorylation landscape. Our findings reveal that this PTM-rich interface functions as a regulatory hub, integrating signals from multiple protein partners to fine-tune PPARγ activity. Unlike full receptor activation by agonists, which often triggers adverse effects, modulating this interface represents a refined therapeutic avenue for enhancing insulin sensitivity in metabolic diseases like obesity and type 2 diabetes, with improved specificity and reduced side effects.
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