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Acetylation of Yeast AMPK Controls Intrinsic Aging Independently of Caloric Restriction
- Source :
-
Cell . Sep2011, Vol. 146 Issue 6, p969-979. 11p. - Publication Year :
- 2011
-
Abstract
- Summary: 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. [Copyright &y& Elsevier]
Details
- Language :
- English
- ISSN :
- 00928674
- Volume :
- 146
- Issue :
- 6
- Database :
- Academic Search Index
- Journal :
- Cell
- Publication Type :
- Academic Journal
- Accession number :
- 65494928
- Full Text :
- https://doi.org/10.1016/j.cell.2011.07.044