Evidence map›Paper›PMID 41315221›Full record

ArticleCell death & disease2025

TRIM25 degrades BRD7 protein stability through the ubiquitin proteasome pathway to promote breast cancer progression and paclitaxel resistance by activating YB1/Bcl-2 transcription axis.

Changning Xue, Qingqing Wei, Mengna Li, Jianxia Wei, Lemei Zheng, Zubing Wu, Huizhen Xin, Yumei Duan, Songqing Fan, Wei Xiong and 4 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 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing 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

2 citing papers in PubMed.

  1. Article
  2. Review
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

14 authors.

Changning XueNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Qingqing WeiNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Mengna LiNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Jianxia WeiNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Lemei ZhengNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Zubing WuNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Huizhen XinNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Yumei DuanCancer Research Institute and School of Basic Medical Sciences, Central South University, Changsha, China.
Songqing FanDepartment of Pathology, the Second Xiangya Hospital, Central South University, Changsha, China.ORCID http://orcid.org/0000-0002-1486-9909
Wei XiongNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.ORCID http://orcid.org/0000-0003-1635-8173
Guiyuan LiNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Faqing TangNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.ORCID http://orcid.org/0000-0001-5794-4975
Hongyu DengNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China.
Ming ZhouNHC Key Laboratory of Carcinogenesis, Hunan Key Laboratory of Oncotarget Gene, Hunan Cancer Hospital and the Affiliated Cancer Hospital of Xiangya School of Medicine, Central South University, Changsha, China. zhouming2013@csu.edu.cn.ORCID http://orcid.org/0000-0003-4938-5397

Funding

National Natural Science Foundation of China (National Science Foundation of China) 82172592, 82473262 and 82403005
6 · The paper itself

Abstract

Paclitaxel (PTX) is one of the most common chemotherapeutic drugs for treating breast cancer (BC), but resistance to PTX chemotherapy remains the major cause of treatment failure in BC patients. Our previous studies demonstrated that BRD7 participates in the paclitaxel-mediated chemotherapy sensitization and inhibits the malignant progression of breast cancer. Furthermore, TRIM25 was screened by IP-MS as a potential E3 ubiquitin ligase interacting with BRD7. Nevertheless, the functions and mechanisms of TRIM25 in the malignant progression of breast cancer and PTX resistance, as well as its regulatory relationship with BRD7, are still not clear. Our investigation revealed that TRIM25 effectively promoted cell proliferation, cell cycle progression, and paclitaxel chemoresistance of BC cells. Mechanistically, TRIM25 interacted with BRD7, and the PRYSPRY region of TRIM25 bond to the N-terminal region of BRD7. Additionally, TRIM25 decreased the protein stability of BRD7 through the ubiquitin proteasome pathway by increasing the K48-linked ubiquitination of BRD7 at the K119 site, and then activated the YB1/Bcl-2 signal axis, thus mediating malignant progression and PTX resistance of breast cancer. We further demonstrated that restoration of BRD7 rescued the inhibitory effect of TRIM25 knockdown on the malignant progression and PTX resistance of BC cells. Furthermore, high expression of TRIM25 was found in clinical breast cancer tissues compared to noncancerous breast tissues, which was positively associated with poor prognosis in BC patients. The expression of TRIM25 was negatively correlated with BRD7 expression, and the combined expression of TRIM25 and BRD7 might be a potential molecular marker for the prediction of malignant progression and prognosis of breast cancer. Our findings demonstrate that targeting the TRIM25/BRD7/YB1/Bcl-2 signal axis might be a potential therapeutic strategy for the treatment of breast cancer.

Indexed as

Breast NeoplasmsDrug Resistance, NeoplasmPaclitaxelSignal TransductionTranscription FactorsTripartite Motif ProteinsUbiquitin-Protein LigasesAnimalsBromodomain Containing ProteinsCell Line, TumorCell ProliferationChromosomal Proteins, Non-HistoneDisease ProgressionFemaleHumansMiceBCL2 protein, humanBRD7 protein, humanBromodomain Containing ProteinsChromosomal Proteins, Non-HistonePaclitaxelProteasome Endopeptidase ComplexProto-Oncogene Proteins c-bcl-2Transcription FactorsTRIM25 protein, humanTripartite Motif ProteinsUbiquitinUbiquitin-Protein LigasesY-Box-Binding Protein 1YBX1 protein, human

Identifiers

PMID41315221
PMCPMC12663559

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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.