Evidence map›Paper›PMID 24786789›Full record

ArticleCancer research2014

Oxidative stress activates SIRT2 to deacetylate and stimulate phosphoglycerate mutase.

Yanping Xu, Fulong Li, Lei Lv, Tingting Li, Xin Zhou, Chu-Xia Deng, Kun-Liang Guan, Qun-Ying Lei, Yue Xiong

Open access · bronzeAbstract read
In one paragraph

Article in Cancer research, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 82 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
82citing papers in PubMed, 1 pooled it
9.4field-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

82 citing papers in PubMed, 1 synthesis or guideline pooled it, 154 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Article
  4. The Yin-Yang balance of SIRT1 and SIRT2 in cancer metabolic remodeling.International journal of biological sciences · 2026
    Review
  5. Article
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  8. Review
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  11. The role of acetylation and deacetylation in cancer metabolism.Clinical and translational medicine · 2025
    Review
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  13. Article
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  15. Article
  16. Review
  17. Review
  18. Review
  19. Article
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22 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

9 authors at 5 institutions in 3 countries.

Yanping XuMolecular and Cell Biology Lab, Institutes of Biomedical Sciences, School of Life Sciences, Fudan University, Shanghai, PR China;
Fulong LiMolecular and Cell Biology Lab, Institutes of Biomedical Sciences, School of Life Sciences, Fudan University, Shanghai, PR China;
Lei LvAuthors' Affiliations: Ministry of Education Key Laboratory of Molecular Medicine, and Department of Biochemistry and Molecular Biology, Shanghai Medical College, Molecular and Cell Biology Lab, Institutes of Biomedical Sciences.
Tingting LiMolecular and Cell Biology Lab, Institutes of Biomedical Sciences, School of Life Sciences, Fudan University, Shanghai, PR China;
Xin ZhouMolecular and Cell Biology Lab, Institutes of Biomedical Sciences, School of Life Sciences, Fudan University, Shanghai, PR China;
Chu-Xia DengGenetics of Development and Disease Branch, National Institute of Diabetes, Digestive and Kidney Diseases, NIH, Bethesda, Maryland;
Kun-Liang GuanAuthors' Affiliations: Ministry of Education Key Laboratory of Molecular Medicine, and Department of Biochemistry and Molecular Biology, Shanghai Medical College, Molecular and Cell Biology Lab, Institutes of Biomedical Sciences, Department of Pharmacology and Moores Cancer Center, University of California at San Diego, La Jolla, California; and yxiong@email.unc.edu kuguan@ucsd.edu qlei@fudan.edu.cn.
Qun-Ying LeiAuthors' Affiliations: Ministry of Education Key Laboratory of Molecular Medicine, and Department of Biochemistry and Molecular Biology, Shanghai Medical College, Molecular and Cell Biology Lab, Institutes of Biomedical Sciences, yxiong@email.unc.edu kuguan@ucsd.edu qlei@fudan.edu.cn.
Yue XiongAuthors' Affiliations: Ministry of Education Key Laboratory of Molecular Medicine, and Department of Biochemistry and Molecular Biology, Shanghai Medical College, Molecular and Cell Biology Lab, Institutes of Biomedical Sciences, Department of Biochemistry and Biophysics, Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, North Carolina yxiong@email.unc.edu kuguan@ucsd.edu qlei@fudan.edu.cn.
Institute of Biomedical Science · GBFudan University · CNShanghai Medical College of Fudan University · CNNational Institute of Diabetes and Digestive and Kidney Diseases · USUniversity of California, San Diego · US

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI David Darr · 1985 to 2026
$201.5M
The Physiological Function and Regulation of INK4 GenesR01CA068377 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI MARZLUFF, WILLIAM F. · 1995 to 2021
$6.5M
Mechanisms of Metabolic Gene Mutations in CancerR01CA163834 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI BALDWIN, ALBERT SIDNEY · 2012 to 2023
$3.1M
NCI NIH HHS P30 CA016086NCI NIH HHS R01 CA068377NCI NIH HHS R01 CA163834
6 · The paper itself

Abstract

Glycolytic enzyme phosphoglycerate mutase (PGAM) plays an important role in coordinating energy production with generation of reducing power and the biosynthesis of nucleotide precursors and amino acids. Inhibition of PGAM by small RNAi or small molecule attenuates cell proliferation and tumor growth. PGAM activity is commonly upregulated in tumor cells, but how PGAM activity is regulated in vivo remains poorly understood. Here we report that PGAM is acetylated at lysine 100 (K100), an active site residue that is invariably conserved from bacteria, to yeast, plant, and mammals. K100 acetylation is detected in fly, mouse, and human cells and in multiple tissues and decreases PGAM2 activity. The cytosolic protein deacetylase sirtuin 2 (SIRT2) deacetylates and activates PGAM2. Increased levels of reactive oxygen species stimulate PGAM2 deacetylation and activity by promoting its interaction with SIRT2. Substitution of endogenous PGAM2 with an acetylation mimetic mutant K100Q reduces cellular NADPH production and inhibits cell proliferation and tumor growth. These results reveal a mechanism of PGAM2 regulation and NADPH homeostasis in response to oxidative stress that impacts cell proliferation and tumor growth.

Indexed as

AcetylationAnimalsCell Line, TumorCell ProliferationGene Expression Regulation, NeoplasticGlycolysisHEK293 CellsHumansLung NeoplasmsMiceMice, Inbred C57BLMice, NudeMutationNADPOxidative StressPhosphoglycerate MutaseNADPPhosphoglycerate MutaseReactive Oxygen SpeciesSIRT2 protein, humanSirtuin 2

Identifiers

PMID24786789
PMCPMC4303242
OpenAlexW2042898532

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.