Evidence map›Paper›PMID 37011206›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2023

The moonlighting function of glycolytic enzyme enolase-1 promotes choline phospholipid metabolism and tumor cell proliferation.

Qingxia Ma, Hongfei Jiang, Leina Ma, Gaoxiang Zhao, Qianqian Xu, Dong Guo, Ningning He, Hao Liu, Zhaoyuan Meng, Juanjuan Liu and 7 more

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed, 1 pooled it
24.2field-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

74 citing papers in PubMed, 1 synthesis or guideline pooled it, 101 citations in OpenAlex.

  1. Pooled it
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  15. Review
  16. The moonlighting functions of glycolytic enzymes in tumorigenesis.Cellular oncology (Dordrecht, Netherlands) · 2026
    Review
  17. Glycolysis enzymes and cellular lactylation in tumour.Clinical and translational medicine · 2026
    Review
  18. Article
  19. Review
  20. Article

14 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

17 authors at 3 institutions in 1 country.

Qingxia MaDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Hongfei JiangDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.ORCID 0000-0001-5869-5253
Leina MaDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Gaoxiang ZhaoDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Qianqian XuDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Dong GuoZhejiang Provincial Key Laboratory of Pancreatic Disease, The First Affiliated Hospital and Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310029, China.ORCID 0000-0001-7057-2838
Ningning HeDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Hao LiuDepartment of Neurosurgery, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, China.
Zhaoyuan MengDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Juanjuan LiuDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Lei ZhuDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Qian LinDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Xiaolin WuDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.ORCID 0000-0002-6200-7000
Min LiZhejiang Provincial Key Laboratory of Pancreatic Disease, The First Affiliated Hospital and Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310029, China.
Shudi LuoZhejiang Provincial Key Laboratory of Pancreatic Disease, The First Affiliated Hospital and Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310029, China.
Jing FangDepartment of Oncology, The Affiliated Hospital of Qingdao University, Qingdao Cancer Institute, Qingdao, Shandong 266000, China.
Zhimin LuZhejiang Provincial Key Laboratory of Pancreatic Disease, The First Affiliated Hospital and Institute of Translational Medicine, Zhejiang University School of Medicine, Hangzhou, Zhejiang 310029, China.ORCID 0000-0002-2859-2736
Qingdao University · CNZhejiang University · CNSichuan University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Aberrantly upregulated choline phospholipid metabolism is a novel emerging hallmark of cancer, and choline kinase α (CHKα), a key enzyme for phosphatidylcholine production, is overexpressed in many types of human cancer through undefined mechanisms. Here, we demonstrate that the expression levels of the glycolytic enzyme enolase-1 (ENO1) are positively correlated with CHKα expression levels in human glioblastoma specimens and that ENO1 tightly governs CHKα expression via posttranslational regulation. Mechanistically, we reveal that both ENO1 and the ubiquitin E3 ligase TRIM25 are associated with CHKα. Highly expressed ENO1 in tumor cells binds to I199/F200 of CHKα, thereby abrogating the interaction between CHKα and TRIM25. This abrogation leads to the inhibition of TRIM25-mediated polyubiquitylation of CHKα at K195, increased stability of CHKα, enhanced choline metabolism in glioblastoma cells, and accelerated brain tumor growth. In addition, the expression levels of both ENO1 and CHKα are associated with poor prognosis in glioblastoma patients. These findings highlight a critical moonlighting function of ENO1 in choline phospholipid metabolism and provide unprecedented insight into the integrated regulation of cancer metabolism by crosstalk between glycolytic and lipidic enzymes.

Indexed as

CholineGlioblastomaPhosphopyruvate HydrataseBiomarkers, TumorCell Line, TumorCell ProliferationDNA-Binding ProteinsHumansPhospholipidsTumor Suppressor ProteinsBiomarkers, TumorCholineDNA-Binding ProteinsENO1 protein, humanPhospholipidsPhosphopyruvate HydrataseTumor Suppressor ProteinsCHKαenolaseTRIM25

Identifiers

PMID37011206
PMCPMC10104498
OpenAlexW4362523783

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-ND
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.