Evidence map›Paper›PMID 29410405›Full record

ArticleNature communications2018

Acetylation accumulates PFKFB3 in cytoplasm to promote glycolysis and protects cells from cisplatin-induced apoptosis.

Fu-Long Li, Jin-Ping Liu, Ruo-Xuan Bao, GuoQuan Yan, Xu Feng, Yan-Ping Xu, Yi-Ping Sun, Weili Yan, Zhi-Qiang Ling, Yue Xiong and 2 more

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 128 papers.

0numbers the graph read from it
0cells of the map it votes in
128citing papers in PubMed
6.0field-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

128 citing papers in PubMed, 189 citations in OpenAlex.

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  12. Hypoxia-induced circ_0017521 enhances glycolysis and promotes NSCLC progression via upregulating the PFKFB3/PI3K-AKT pathway.Mammalian genome : official journal of the International Mammalian Genome Society · 2026
    Article
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  16. Anticancer Activity of Benzomalvin Derivatives Isolated fromJournal of microbiology and biotechnology · 2025
    Article
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  18. Review
  19. Article
  20. Article

68 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 4 institutions in 2 countries.

Fu-Long LiThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.
Jin-Ping LiuThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.
Ruo-Xuan BaoThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.
GuoQuan YanInstitutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.
Xu FengThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.
Yan-Ping XuLineberger Comprehensive Cancer Center, Department of Biochemistry and Biophysics, University of North Carolina at Chapel Hill, Chapel Hill, NC, 27599, USA.
Yi-Ping SunThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.
Weili YanDepartment of Clinical Epidemiology, Children's Hospital of Fudan University, Shanghai, 201102, China.
Zhi-Qiang LingZhejiang Cancer Research Institute, Zhejiang Province Cancer Hospital Zhejiang Cancer Center, Hangzhou, 310022, China.ORCID http://orcid.org/0000-0003-2155-1111
Yue XiongThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.
Kun-Liang GuanThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China.ORCID http://orcid.org/0000-0003-1892-0174
Hai-Xin YuanThe Fifth People's Hospital of Shanghai and the Molecular and Cell Biology Research Lab of the Institutes of Biomedical Sciences, Fudan University, Shanghai, 200032, China. yuanhaixin@fudan.edu.cn.
Fudan University · CNUniversity of North Carolina at Chapel Hill · USChildren's Hospital of Fudan University · CNZhejiang Cancer Hospital · CN

Funding

PROTEIN PHOSPHORYLATION AND GROWTH FACTOR FUNCTIONR01GM051586 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI BROWN, JOAN HELLER · 1994 to 2024
$7.9M
The ROC-Cullin Family of E3 Ubiquitin LigasesR01GM067113 · NIGMS · UNIV OF NORTH CAROLINA CHAPEL HILL · PI XIONG, YUE · 2003 to 2019
$5.4M
The mTOR and Hippo pathway in cell growth and cancerR35CA196878 · NCI · UNIVERSITY OF CALIFORNIA, SAN DIEGO · PI GUAN, KUN-LIANG · 2015 to 2019
$4.0M
NCI NIH HHS R35 CA196878NIGMS NIH HHS R01 GM051586NIGMS NIH HHS R01 GM067113
6 · The paper itself

Abstract

Enhanced glycolysis in cancer cells has been linked to cell protection from DNA damaging signals, although the mechanism is largely unknown. The 6-phosphofructo-2-kinase/fructose-2,6-biphosphatase 3 (PFKFB3) catalyzes the generation of fructose-2,6-bisphosphate, a potent allosteric stimulator of glycolysis. Intriguingly, among the four members of PFKFB family, PFKFB3 is uniquely localized in the nucleus, although the reason remains unclear. Here we show that chemotherapeutic agent cisplatin promotes glycolysis, which is suppressed by PFKFB3 deletion. Mechanistically, cisplatin induces PFKFB3 acetylation at lysine 472 (K472), which impairs activity of the nuclear localization signal (NLS) and accumulates PFKFB3 in the cytoplasm. Cytoplasmic accumulation of PFKFB3 facilitates its phosphorylation by AMPK, leading to PFKFB3 activation and enhanced glycolysis. Inhibition of PFKFB3 sensitizes tumor to cisplatin treatment in a xenograft model. Our findings reveal a mechanism for cells to stimulate glycolysis to protect from DNA damage and potentially suggest a therapeutic strategy to sensitize tumor cells to genotoxic agents by targeting PFKFB3.

Indexed as

A549 CellsAcetylationAdenylate KinaseAntineoplastic AgentsApoptosisCell Line, TumorCisplatinCytoplasmGlycolysisHCT116 CellsHeLa CellsHumansNuclear Localization SignalsPhosphofructokinase-2PhosphorylationAdenylate KinaseAntineoplastic AgentsCisplatinNuclear Localization SignalsPFKFB3 protein, humanPhosphofructokinase-2

Identifiers

PMID29410405
PMCPMC5802808
OpenAlexW2794941471

What OpenQuestion holds

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LicenceCC BY
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.