Evidence map›Paper›PMID 19303850›Full record

ArticleCell2009

Protein acetylation microarray reveals that NuA4 controls key metabolic target regulating gluconeogenesis.

Yu-yi Lin, Jin-ying Lu, Junmei Zhang, Wendy Walter, Weiwei Dang, Jun Wan, Sheng-Ce Tao, Jiang Qian, Yingming Zhao, Jef D Boeke and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 182 papers.

0numbers the graph read from it
0cells of the map it votes in
182citing papers in PubMed
14.1field-weighted citation impact, top 1% 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

182 citing papers in PubMed, 304 citations in OpenAlex.

  1. Article
  2. Article
  3. Glucosinolates from Seed-Press Cake ofAntioxidants (Basel, Switzerland) · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. COVID-19-related hyperglycemia is associated with infection of hepatocytes and stimulation of gluconeogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  11. Article
  12. Article
  13. Review
  14. Structure of the NuA4 histone acetyltransferase complex.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Review
  20. Review

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

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

12 authors at 6 institutions in 2 countries.

Yu-yi LinHigh Throughput Biology Center, Johns Hopkins University School of Medicine, Baltimore, MD 21205, USA.
Jin-ying Lu
Junmei Zhang
Wendy Walter
Weiwei Dang
Jun Wan
Sheng-Ce Tao
Jiang Qian
Yingming Zhao
Jef D Boeke
Shelley L Berger
Heng Zhu
Johns Hopkins University · USThe Wistar Institute · USHigh Throughput Biology (United States) · USThe University of Texas Southwestern Medical Center · USJohns Hopkins Medicine · USNational Taiwan University · TW

Funding

TCP5: ACTIVE SITE LABELING REAGENT FOR ACETYLTRANSFERASESU54RR020839 · NCRR · JOHNS HOPKINS UNIVERSITY · PI BOEKE, JEF D · 2004 to 2011
$27.4M
Global characterization of lysine acetylation in cancer by a proteomics approachR01CA126832 · NCI · UT SOUTHWESTERN MEDICAL CENTER · PI ZHAO, YINGMING · 2008 to 2012
$1.6M
Computational Analysis of Retinal Regulatory Interactions: structure and dynamicsR01EY017589 · NEI · JOHNS HOPKINS UNIVERSITY · PI QIAN, JIANG · 2007 to 2010
$1.1M
NCI NIH HHS R01 CA126832NCI NIH HHS R01CA126832NCRR NIH HHS U54 RR 020839NCRR NIH HHS U54 RR020839NEI NIH HHS R01 EY017589NEI NIH HHS R01EY017589
6 · The paper itself

Abstract

Histone acetyltransferases (HATs) and histone deacetylases (HDACs) conduct many critical functions through nonhistone substrates in metazoans, but only chromatin-associated nonhistone substrates are known in Saccharomyces cerevisiae. Using yeast proteome microarrays, we identified and validated many nonchromatin substrates of the essential nucleosome acetyltransferase of H4 (NuA4) complex. Among these, acetylation sites (Lys19 and 514) of phosphoenolpyruvate carboxykinase (Pck1p) were determined by tandem mass spectrometry. Acetylation at Lys514 was crucial for enzymatic activity and the ability of yeast cells to grow on nonfermentable carbon sources. Furthermore, Sir2p deacetylated Pck1p both in vitro and in vivo. Loss of Pck1p activity blocked the extension of yeast chronological life span caused by water starvation. In human hepatocellular carcinoma (HepG2) cells, human Pck1 acetylation and glucose production were dependent on TIP60, the human homolog of ESA1. Our findings demonstrate a regulatory function for the NuA4 complex in glucose metabolism and life span by acetylating a critical metabolic enzyme.

Indexed as

GluconeogenesisAcetylationGene Knockdown TechniquesGlucoseHistone AcetyltransferasesHistone DeacetylasesHumansIntracellular Signaling Peptides and ProteinsLysine Acetyltransferase 5Multiprotein ComplexesPhosphoenolpyruvate Carboxykinase (GTP)Protein Array AnalysisSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsSirtuinsWaterGlucoseHistone AcetyltransferasesHistone DeacetylasesIntracellular Signaling Peptides and ProteinsKAT5 protein, humanLysine Acetyltransferase 5Multiprotein ComplexesNuA4 protein, S cerevisiaePCK1 protein, humanPhosphoenolpyruvate Carboxykinase (GTP)Saccharomyces cerevisiae ProteinsSirtuinsWater

Identifiers

PMID19303850
PMCPMC2696288
OpenAlexW2085872107

What OpenQuestion holds

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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.