Evidence map›Paper›PMID 41290618›Full record

ArticleNature communications2025

The E3 ligase tripartite motif 7 drives the progression of non-alcoholic fatty liver disease by targeting DUSP10 degradation in male mice.

Feng-Juan Yan, Han Ding, Ning Zhang, Shi-Ran Yan, Mei-Xin Huang, Jing-Wei Lu, Yong-Jian Wang, Yu-Jie Yan, Rong-Peng Li, Qun Wang

Abstract read
In one paragraph

Article in Nature communications, 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. E3 Ubiquitin Ligases in MASH-Associated Liver Fibrosis: Mechanisms and Therapeutic Opportunities.Liver international : official journal of the International Association for the Study of the Liver · 2026
    Review
  2. 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

10 authors.

Feng-Juan YanSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China. yanfengjuan@whu.edu.cn.ORCID http://orcid.org/0000-0002-5816-8282
Han DingSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China.
Ning ZhangSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China.
Shi-Ran YanDepartment of Cardiology, Heze Municipal Hospital Affiliated to Shandong First Medical University, Heze, Shandong, PR China.
Mei-Xin HuangSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China.
Jing-Wei LuSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China.
Yong-Jian WangSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China.
Yu-Jie YanSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China.
Rong-Peng LiSchool of Life Science, Jiangsu Normal University, Xuzhou, Jiangsu, PR China. lirongpeng@jsnu.edu.cn.ORCID http://orcid.org/0000-0002-8623-9068
Qun WangDepartment of Hepatopancreatobiliary Surgery, Hubei Cancer Hospital, Tongji Medical College, Huazhong University of Science and Technology, Wuhan, Hubei, PR China. swander@126.com.ORCID http://orcid.org/0000-0001-6558-3671

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Non-alcoholic fatty liver disease (NAFLD) and its more severe form, nonalcoholic steatohepatitis (NASH), have emerged as a burgeoning global epidemic and impose an enormous socioeconomic burden. However, the lack of effective pharmacotherapies is due to incomplete understanding of the molecular mechanisms of NASH. In the present study, we observe that E3 ligase TRIM7 expression is significantly increased in both liver tissues and hepatocytes from NAFLD models. In vivo gain- and loss-of-function experiments reveal that hepatic-specific TRIM7 deletion significantly alleviates hepatic steatosis, inflammation and insulin resistance in diet-induced male mouse models, whereas overexpression of wild-type TRIM7 (but not its E3-deficient mutant) shows diametrically opposite effects. Mechanistic studies reveal that TRIM7 interacts with and catalyzes DUSP10 ubiquitination and proteasomal degradation, thus leading to hyperactivation of IKKβ-NF-κB and JNK/p38 MAPK signaling pathways. Importantly, silencing DUSP10 expression abrogates the protective effects of hepatic TRIM7 deficiency on NAFLD-related pathological phenotypes. Collectively, our findings identify TRIM7 as a key regulator of the pathogenesis of NAFLD/NASH and provide a promising therapeutic strategy for NAFLD by targeting the TRIM7-DUSP10 axis.

Indexed as

Dual-Specificity PhosphatasesMitogen-Activated Protein Kinase PhosphatasesNon-alcoholic Fatty Liver DiseaseTripartite Motif ProteinsUbiquitin-Protein LigasesAnimalsDiet, High-FatDisease Models, AnimalDisease ProgressionHepatocytesHumansInsulin ResistanceLiverMaleMiceMice, Inbred C57BLDual-Specificity PhosphatasesDusp10 protein, mouseMitogen-Activated Protein Kinase PhosphatasesTripartite Motif ProteinsUbiquitin-Protein Ligases

Identifiers

PMID41290618
PMCPMC12647708

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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.