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Acetylation of yeast AMPK controls intrinsic aging independently of caloric restriction.

Cell | Sep 16, 2011

http://www.ncbi.nlm.nih.gov/pubmed/21906795

Acetylation of histone and nonhistone proteins is an important posttranslational modification affecting many cellular processes. Here, we report that NuA4 acetylation of Sip2, a regulatory β subunit of the Snf1 complex (yeast AMP-activated protein kinase), decreases as cells age. Sip2 acetylation, controlled by antagonizing NuA4 acetyltransferase and Rpd3 deacetylase, enhances interaction with Snf1, the catalytic subunit of Snf1 complex. Sip2-Snf1 interaction inhibits Snf1 activity, thus decreasing phosphorylation of a downstream target, Sch9 (homolog of Akt/S6K), and ultimately leading to slower growth but extended replicative life span. Sip2 acetylation mimetics are more resistant to oxidative stress. We further demonstrate that the anti-aging effect of Sip2 acetylation is independent of extrinsic nutrient availability and TORC1 activity. We propose a protein acetylation-phosphorylation cascade that regulates Sch9 activity, controls intrinsic aging, and extends replicative life span in yeast.

Pubmed ID: 21906795 RIS Download

Mesh terms: AMP-Activated Protein Kinases | Acetylation | Caloric Restriction | Cell Division | Histone Acetyltransferases | Histone Deacetylases | Protein Kinases | Protein-Serine-Threonine Kinases | Saccharomyces cerevisiae | Saccharomyces cerevisiae Proteins | Trans-Activators | Transcription Factors

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Associated grants

  • Agency: NCRR NIH HHS, Id: U54 RR020839
  • Agency: NCRR NIH HHS, Id: U54 RR020839-07
  • Agency: NCRR NIH HHS, Id: U54 RR020839-08
  • Agency: NCRR NIH HHS, Id: U54 RR020839-09
  • Agency: NCRR NIH HHS, Id: U54-RR020839

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