Evidence map›Paper›PMID 26926077›Full record

ArticleScientific reports2016

Interaction with Pyruvate Kinase M2 Destabilizes Tristetraprolin by Proteasome Degradation and Regulates Cell Proliferation in Breast Cancer.

Liangqian Huang, Zhenhai Yu, Zhenchao Zhang, Wenjing Ma, Shaoli Song, Gang Huang

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.7field-weighted citation impact, top 18% 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

24 citing papers in PubMed, 38 citations in OpenAlex.

  1. Promising Role of PKM2 in the Diagnosis and Prognosis of Ovarian Cancer.Anti-cancer agents in medicinal chemistry · 2026
    Review
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  13. Emerging roles of aerobic glycolysis in breast cancer.Clinical & translational oncology : official publication of the Federation of Spanish Oncology Societies and of the National Cancer Institute of Mexico · 2020
    Review
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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

6 authors at 4 institutions in 1 country.

Liangqian HuangInstitute of Health Sciences, Shanghai Institutes for Biological Sciences (SIBS), Chinese Academy of Sciences (CAS) &Shanghai Jiao Tong University School of Medicine (SJTUSM), Shanghai 200025, China.
Zhenhai YuDepartment of Nuclear Medicine, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200127, China.
Zhenchao ZhangInstitute of Health Sciences, Shanghai Institutes for Biological Sciences (SIBS), Chinese Academy of Sciences (CAS) &Shanghai Jiao Tong University School of Medicine (SJTUSM), Shanghai 200025, China.
Wenjing MaInstitute of Health Sciences, Shanghai Institutes for Biological Sciences (SIBS), Chinese Academy of Sciences (CAS) &Shanghai Jiao Tong University School of Medicine (SJTUSM), Shanghai 200025, China.
Shaoli SongDepartment of Nuclear Medicine, Renji Hospital, School of Medicine, Shanghai Jiao Tong University, Shanghai 200127, China.
Gang HuangInstitute of Health Sciences, Shanghai Institutes for Biological Sciences (SIBS), Chinese Academy of Sciences (CAS) &Shanghai Jiao Tong University School of Medicine (SJTUSM), Shanghai 200025, China.
Renji Hospital · CNShanghai Jiao Tong University · CNChinese Academy of Sciences · CNShanghai Institutes for Biological Sciences · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Pyruvate kinase M2 (PKM2), which is predominantly expressed in most cancers, plays a key role in the Warburg effect. However, how PKM2 functions as a tumor supportive protein has not been fully elucidated. Here, we identified tristetraprolin (TTP), an AU-rich, element-binding protein that regulates mRNA stability, as a new binding partner of PKM2. Our data reveal that PKM2 suppresses TTP protein levels by promoting its phosphorylation, ubiquitination, and proteasome degradation, reducing its mRNA turnover ability and ultimately impairing cell viability in breast cancer cells. The p38/mitogen-activated protein kinase (MAPK) pathway might be involved in PKM2-mediated TTP degradation, while treatment with the p38 inhibitor or siRNA abolished PKM2-induced TTP protein degradation. These findings demonstrate that PKM2-TTP association is crucial for regulating breast cancer cell proliferation and is therefore a potential therapeutic target in cancer.

Indexed as

Alternative SplicingBreast NeoplasmsCarrier ProteinsCell Line, TumorCell ProliferationCell SurvivalFemaleHEK293 CellsHumansMCF-7 CellsMembrane Proteinsp38 Mitogen-Activated Protein KinasesPhosphorylationProteasome Endopeptidase ComplexProtein BindingPyruvate KinaseCarrier ProteinsMembrane Proteinsp38 Mitogen-Activated Protein KinasesProteasome Endopeptidase ComplexPyruvate KinaseRNA, MessengerRNA, Small InterferingThyroid Hormone-Binding ProteinsThyroid HormonesTristetraprolin

Identifiers

PMID26926077
PMCPMC4772106
OpenAlexW2291178245

What OpenQuestion holds

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LicenceCC BY
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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.