Evidence map›Paper›PMID 21906795›Full record

ArticleCell2011

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

Jin-Ying Lu, Yu-Yi Lin, Jin-Chuan Sheu, June-Tai Wu, Fang-Jen Lee, Yue Chen, Min-I Lin, Fu-Tien Chiang, Tong-Yuan Tai, Shelley L Berger and 5 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 99 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
99citing papers in PubMed, 1 pooled it
7.6field-weighted citation impact, top 2% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

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.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

99 citing papers in PubMed, 1 synthesis or guideline pooled it, 151 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. Protein lysine acetylation regulates oral microorganisms.Frontiers in cellular and infection microbiology · 2025
    Review
  5. Article
  6. Review
  7. Advances inJournal of fungi (Basel, Switzerland) · 2023
    Review
  8. Article
  9. Review
  10. Article
  11. Article
  12. Review
  13. Review
  14. Article
  15. Article
  16. Review
  17. D-Xylose Sensing inInternational journal of molecular sciences · 2021
    Review
  18. Article
  19. Review
  20. A Molecular Perspective on Sirtuin Activity.International journal of molecular sciences · 2020
    Review

39 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

15 authors at 6 institutions in 2 countries.

Jin-Ying LuDepartment of Laboratory Medicine, National Taiwan University Hospital, National Taiwan University, Taipei 100, Taiwan.
Yu-Yi Lin
Jin-Chuan Sheu
June-Tai Wu
Fang-Jen Lee
Yue Chen
Min-I Lin
Fu-Tien Chiang
Tong-Yuan Tai
Shelley L Berger
Yingming Zhao
Keh-Sung Tsai
Heng Zhu
Lee-Ming Chuang
Jef D Boeke
National Taiwan University · TWNational Taiwan University Hospital · TWUniversity of Chicago · USHigh Throughput Biology (United States) · USJohns Hopkins Medicine · USThe Wistar Institute · US

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Networks, Pathways and Dynamics of Lysine ModificationU54GM103520 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI BADER, JOEL S. · 2012 to 2013
$7.0M
NCRR NIH HHS U54 RR020839NCRR NIH HHS U54-RR020839NIGMS NIH HHS U54 GM103520
6 · The paper itself

Abstract

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.

Indexed as

AcetylationAMP-Activated Protein KinasesCaloric RestrictionCell DivisionHistone AcetyltransferasesHistone DeacetylasesProtein KinasesProtein Serine-Threonine KinasesSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsTrans-ActivatorsTranscription FactorsAMP-Activated Protein KinasesHistone AcetyltransferasesHistone DeacetylasesNuA4 protein, S cerevisiaeProtein KinasesProtein Serine-Threonine KinasesRPD3 protein, S cerevisiaeSaccharomyces cerevisiae ProteinsSCH9 protein kinaseSIP2 protein, S cerevisiaeSNF1-related protein kinasesTORC1 protein complex, S cerevisiaeTrans-ActivatorsTranscription Factors

Identifiers

PMID21906795
PMCPMC3176974
OpenAlexW2063087406

What OpenQuestion holds

Textmetadata
LicenceTDM
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.