ArticleeLife2025
SIRT2-mediated ACSS2 K271 deacetylation suppresses lipogenesis under nutrient stress.
Article in eLife, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed.
- Sirtuin 2 inhibits global protein synthesis via Rheb-GTPase degradation.EMBO reports · 2026Article
- SIRT2 mediates integrated stress response by deacetylating and stabilizing 4E-BP1 to suppress translation.EMBO reports · 2026Article
- AcuB senses cellular energy charge to coordinate acetyl-CoA synthesis in bacteria.Nature communications · 2026Article
- Article
- SMAD2 S-palmitoylation promotes its linker region phosphorylation and TScience signaling · 2025Article
- Deacetylation of HSC70 by SIRT2 promotes chaperone mediated autophagy.Autophagy reports · 2025Article
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
De novo lipogenesis is associated with the development of human diseases such as cancer, diabetes, and obesity. At the core of lipogenesis lies acetyl coenzyme A (CoA), a metabolite that plays a crucial role in fatty acid synthesis. One of the pathways contributing to the production of cytosolic acetyl-CoA is mediated by acetyl-CoA synthetase 2 (ACSS2). Here, we reveal that when cells encounter nutrient stress, particularly a deficiency in amino acids, Sirtuin 2 (SIRT2) catalyzes the deacetylation of ACSS2 at the lysine residue K271. This results in K271 ubiquitination and subsequently proteasomal degradation of ACSS2. Substitution of K271 leads to decreased ubiquitination of ACSS2, increased ACSS2 protein level, and thus increased lipogenesis. Our study uncovers a mechanism that cells employ to efficiently manage lipogenesis during periods of nutrient stress.
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Registered trials
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