Evidence map›Paper›PMID 24362262›Full record

ArticleThe Journal of biological chemistry2014

Glyceraldehyde-3-phosphate dehydrogenase is activated by lysine 254 acetylation in response to glucose signal.

Tingting Li, Mengxi Liu, Xu Feng, Zhen Wang, Indrani Das, Yanping Xu, Xin Zhou, Yiping Sun, Kun-Liang Guan, Yue Xiong and 1 more

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed, 1 pooled it
4.9field-weighted citation impact, top 4% 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

47 citing papers in PubMed, 1 synthesis or guideline pooled it, 95 citations in OpenAlex.

  1. Pooled it
  2. Histone deacetylases in cancer metabolic reprogramming.Experimental & molecular medicine · 2026
    Review
  3. Article
  4. Article
  5. The role of acetylation and deacetylation in cancer metabolism.Clinical and translational medicine · 2025
    Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. 'Autophagy · 2023
    Article
  12. TgKDAC4: A Unique Deacetylase ofMicroorganisms · 2023
    Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Review
  18. Article
  19. Article
  20. Review
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

11 authors at 4 institutions in 2 countries.

Tingting LiFrom the Key Laboratory of Molecular Medicine, Ministry of Education, and Department of Biochemistry and Molecular Biology, Fudan University Shanghai Medical College, Shanghai 200032, China.
Mengxi Liu
Xu Feng
Zhen Wang
Indrani Das
Yanping Xu
Xin Zhou
Yiping Sun
Kun-Liang Guan
Yue Xiong
Qun-Ying Lei
Shanghai Medical College of Fudan University · CNFudan University · CNHarvard University Press · USUniversity of North Carolina at Chapel Hill · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The altered metabolism in most tumor cells consists of elevated glucose uptake and increased glycolysis even in the presence of high oxygen tension. Glyceraldehyde-3-phosphate dehydrogenase (GAPDH) is an obligatory enzyme in glycolysis. Here, we report that acetylation at lysine 254 (K254) increases GAPDH activity in response to glucose. Furthermore, acetylation of GAPDH (K254) is reversibly regulated by the acetyltransferase PCAF and the deacetylase HDAC5. Substitution of K254 to glutamine compromises the ability of GAPDH to support cell proliferation and tumor growth. Our study reveals a mechanism of GAPDH enzyme activity regulation by acetylation and its critical role in cellular regulation.

Indexed as

Cell ProliferationSignal TransductionAcetylationAnimalsCell Line, TumorEnzyme ActivationGlucoseGlyceraldehyde-3-Phosphate DehydrogenasesHEK293 CellsHistone DeacetylasesHumansMiceMice, Inbred BALB CMice, NudeNeoplasm ProteinsNeoplasmsGlucoseGlyceraldehyde-3-Phosphate DehydrogenasesHDAC5 protein, humanHistone DeacetylasesNeoplasm Proteinsp300-CBP-Associated Factorp300-CBP Transcription FactorsAcetylationCell GrowthGAPDHGlycolysisHDAC5Histone DeacetylaseLung CancerMetabolismPCAFTumorigenesis

Identifiers

PMID24362262
PMCPMC3916574
OpenAlexW2117096101

What OpenQuestion holds

Textmetadata
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.