Evidence map›Paper›PMID 41184227›Full record

ArticleCell death & disease2025

TRIM8-dependent K63-ubiquitinated PGK1 promotes glycolysis and angiogenesis in gastric cancer via interaction with ACAT1.

Anqi Feng, Jianbin Zhang, Zeyu Wang, Zhukai Chen, Kang Fang, Zhaoxing Li, Hanyu Jiang, Zhuyun Leng, Shihan Zhang, Yuan Chu and 5 more

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell death & disease, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.

0numbers the graph read from it
0cells of the map it votes in
3citing papers in PubMed
–field-weighted citation impact
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

3 citing papers in PubMed.

  1. Review
  2. Review
  3. Retinol saturase in the mitochondria antagonizes IDH2 and GLUD1 acetylation to mediate heart repair.Proceedings of the National Academy of Sciences of the United States of America · 2026
    Article
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

15 authors.

Anqi Feng *Endoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.ORCID http://orcid.org/0000-0002-9306-0189
Jianbin Zhang *Endoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Zeyu Wang *Endoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Zhukai ChenEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Kang FangEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Zhaoxing LiEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Hanyu JiangEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Zhuyun LengEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Shihan ZhangEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Yuan ChuEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Jingjing LianEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.
Tao ChenEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China.ORCID http://orcid.org/0000-0002-8016-9732
Lechi YeDepartment of Colorectal Surgery, Zhongshan Hospital, Fudan University, Address: No.180, Fenglin Road, Xuhui District, Shanghai, China. ye.lechi@zs-hospital.sh.cn.
Meidong XuEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China. 1800512@tongji.edu.cn.ORCID http://orcid.org/0000-0002-7219-5826
Lingnan HeEndoscopy Center, Department of Gastroenterology, Shanghai East Hospital, School of Medicine, Tongji University, No.150, Jimo Road, Pudong New Area, Shanghai, China. lingnan_he@tongji.edu.cn.ORCID http://orcid.org/0000-0002-0760-9789

Funding

Health and Family Planning Committee of Pudong New Area (Health and Family Planning Committee of Pudong New District) Nos. PWRq2024-10Health and Family Planning Committee of Pudong New Area (Health and Family Planning Committee of Pudong New District) PWZxq2022-6National Natural Science Foundation of China (National Science Foundation of China) 82172816National Natural Science Foundation of China (National Science Foundation of China) 82203341
6 · The paper itself

Abstract

Glycolysis is crucial for promoting cancer progression. However, the precise mechanism underlying glycolysis regulating the angiogenic process remains to be defined. Here, we demonstrate that in human gastric cancer cells, the E3 ligase TRIM8 promotes the K63-linked ubiquitination of the glycolytic enzyme PGK1 and improves its stability, which leads to acetyltransferase ACAT1 recruitment, increased interaction of PGK1 with ACAT1, and subsequent PGK1 acetylation-dependent glycolytic activity. This activity facilitates PGK1-mediated glycolysis, lactate accumulation and triggers a significant increase in endothelial cell migration and tube formation, which ultimately accelerates tumor angiogenesis in gastric cancer. TRIM8 levels are positively correlated with tumor angiogenesis and poor prognosis in gastric cancer patients. These findings elucidate a novel mechanism underlying the upregulation of angiogenesis mediated by K63 ubiquitination-regulated glycolysis in tumor cells and provide a molecular basis for eliminating gastric cancer angiogenesis by targeting TRIM8-dependent PGK1 K63 ubiquitination.

Indexed as

GlycolysisNeovascularization, PathologicPhosphoglycerate KinaseStomach NeoplasmsTripartite Motif ProteinsUbiquitin-Protein LigasesAngiogenesisAnimalsCell Line, TumorCell MovementHumansMiceMice, NudeN-Terminal Acetyltransferase AN-Terminal Acetyltransferase EUbiquitinationNAA10 protein, humanN-Terminal Acetyltransferase AN-Terminal Acetyltransferase EPGK1 protein, humanPhosphoglycerate KinaseTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID41184227
PMCPMC12583530

What OpenQuestion holds

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Registered trials

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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.