Evidence map›Paper›PMID 39164728›Full record

ArticleJournal of experimental & clinical cancer research : CR2024

The deubiquitinase USP15 drives malignant progression of gastric cancer through glucose metabolism remodeling.

Longtao Huangfu, Huanbo Zhu, Gangjian Wang, Junbing Chen, Yongqi Wang, Biao Fan, Xiaoyang Wang, Qian Yao, Ting Guo, Jing Han and 5 more

Abstract read
In one paragraph

Article in Journal of experimental & clinical cancer research : CR, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing 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

13 citing papers in PubMed.

  1. Review
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  7. [Knockdown ofNan fang yi ke da xue xue bao = Journal of Southern Medical University · 2025
    Article
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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

15 authors.

Longtao Huangfu *Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Huanbo Zhu *Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Gangjian Wang *Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Junbing Chen *Key Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Yongqi WangKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Biao FanGastrointestinal Cancer Center, Peking University Cancer Hospital & Institute, Beijing, Fu-Cheng Road, Beijing, 100142, China.
Xiaoyang WangDepartment of Pharmacy, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Qian YaoDepartment of Pathology, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Ting GuoKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Jing HanKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Ying HuBiological Sample Bank, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Hong DuKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Xiaomei LiKey Laboratory of Carcinogenesis and Translational Research (Ministry of Education), Division of Gastrointestinal Cancer Translational Research Laboratory, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China.
Jiafu JiGastrointestinal Cancer Center, Peking University Cancer Hospital & Institute, Beijing, Fu-Cheng Road, Beijing, 100142, China. jijiafu@hsc.pku.edu.cn.
Xiaofang XingState Key Laboratory of Holistic Integrative Management of Gastrointestinal Cancers, Beijing Key Laboratory of Carcinogenesis and Translational Research, Peking University Cancer Hospital & Institute, Fu-Cheng Road, Beijing, 100142, China. xingxiaofang@bjmu.edu.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundUbiquitin-specific protease 15 (USP15) exhibits amplifications in various tumors, including gastric cancer (GC), yet its biological function and mechanisms in GC progression remain elusive.

methodsHere, we established stable USP15 knockdown or overexpression GC cell lines and explored the potential mechanism of USP15 in GC. Besides, we also identified interacting targets of USP15.

resultsUSP15 knockdown significantly impeded cell proliferation, invasion, epithelial-mesenchymal transition, and distal colonization in xenograft models, while enhancing oxaliplatin's antitumor effect. USP15 was involved in ubiquitination modification of glycolytic regulators. Silencing of USP15 suppressed glycolytic activity and impaired mitochondrial functions. Interference with USP15 expression reversed tumor progression and distal colonization in vivo. HKDC1 and IGF2BP3 were found as core interacting targets of USP15, and HKDC1 was identified as a substrate for ubiquitination modification by USP15, whereby USP15 regulated glucose metabolism activity by inhibiting the ubiquitination degradation of HKDC1.

conclusionsOur study unveiled aberrantly high expression of USP15 in GC tissues, correlating with malignant progression and nonresponse to neoadjuvant therapy. USP15 inhibitors, if developed, could be effective in promoting chemotherapy through glucose metabolism remodeling.

Indexed as

Disease ProgressionGlucoseStomach NeoplasmsUbiquitin-Specific ProteasesAnimalsCell Line, TumorCell ProliferationEpithelial-Mesenchymal TransitionFemaleHumansMaleMiceMice, NudeUbiquitinationXenograft Model Antitumor AssaysGlucoseUbiquitin-Specific ProteasesUSP15 protein, humanGastric cancerGlucose metabolismHexokinase domain containing 1Insulin like growth factor 2 mRNA binding protein 3Ubiquitin specific peptidase 15

Identifiers

PMID39164728
PMCPMC11334570

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LicenceCC BY
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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.