Evidence map›Paper›PMID 40050998›Full record

ArticleCell communication and signaling : CCS2025

TFE3 fusion proteins promote the progression of TFE3 rearranged renal cell carcinoma via enhancing chaperone-mediated lipophagy.

Wenliang Ma, Yi Chen, Guijuan Chen, Lei Yang, Yanwen Lu, Xiang Dong, Dongmei Li, Weidong Gan

Abstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Cell communication and signaling : CCS, 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. TFE3 fusion proteins driveFrontiers in immunology · 2026
    Article
  3. 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

8 authors.

Wenliang Ma *Department of Urology, Affiliated Drum Tower Hospital, Medical School of Nanjing University, No. 321 Zhongshan Road, Nanjing, Jiangsu Province, 210008, China.
Yi Chen *Department of Cardiology, Children's Hospital of Nanjing Medical University, Nanjing, Jiangsu, 210008, China.
Guijuan Chen *State Key Laboratory of Analytical Chemistry for Life Science, Division of Anatomy and Histo-embryology, Medical School, Nanjing University, Nanjing, Jiangsu, 210093, China.
Lei YangState Key Laboratory of Analytical Chemistry for Life Science, Division of Anatomy and Histo-embryology, Medical School, Nanjing University, Nanjing, Jiangsu, 210093, China.
Yanwen LuDepartment of Urology, Affiliated Drum Tower Hospital, Medical School of Nanjing University, No. 321 Zhongshan Road, Nanjing, Jiangsu Province, 210008, China.
Xiang DongDepartment of Urology, Affiliated Drum Tower Hospital, Medical School of Nanjing University, No. 321 Zhongshan Road, Nanjing, Jiangsu Province, 210008, China.
Dongmei LiState Key Laboratory of Analytical Chemistry for Life Science, Division of Anatomy and Histo-embryology, Medical School, Nanjing University, Nanjing, Jiangsu, 210093, China.
Weidong GanDepartment of Urology, Affiliated Drum Tower Hospital, Medical School of Nanjing University, No. 321 Zhongshan Road, Nanjing, Jiangsu Province, 210008, China. gwd@nju.edu.cn.

Funding

the Medical Research Project of Jiangsu Province Health Commission No. ZD2022013the Project of Natural Science Foundation of Jiangsu Province of China BK20221444
6 · The paper itself

Abstract

backgroundTFE3 rearranged renal cell carcinoma (TFE3 rRCC), classified as a distinct entity of RCCs, exhibits aggressive biological behavior and possesses unique metabolic characteristics. In the present study, TFE3 rRCC with high expression of TFE3 fusion proteins was employed to investigate the features of lipid metabolism and its underlying mechanism in cancer progression.

methodsFluorescence microscope and flow cytometry were employed to detect lipid droplets (LDs). GPO-PAP method and Oil Red O staining were used to quantify triacylglycerol levels. The data for bioinformatics analysis were sourced from GEO and iProX. The biological roles of TFE3 and LAMP2A were investigated by CCK8 assay, EdU staining, seahorse, transwell assay, colony, and sphere formation assay. The regulatory mechanisms involving TFE3, LAMP2A and Hsc70 were investigated using western blotting, immunohistochemistry, qRT-PCR, luciferase assays, Co-IP techniques, and ChIP analyses.

resultsThe level of LDs accumulation in TFE3 rRCC was relatively low, and the knockdown of TFE3 led to an increase in LDs accumulation while inhibiting tumor progression. The underlying mechanism revealed that TFE3 fusion proteins inhibited the biosynthesis of LDs within the endoplasmic reticulum by promoting the degradation of DGAT1 and DGAT2 via autophagy. Furthermore, TFE3 fusion proteins upregulated LAMP2A, thereby enhancing chaperone-mediated autophagy pathways. The process facilitated the degradation of LDs and promoted oxidative metabolism of long-chain fatty acids in mitochondria.

conclusionsTFE3 fusion proteins facilitated the progression of TFE3 rRCC through enhancing the degradation of LDs via chaperone-mediated lipophagy. LAMP2A could serve as a novel potential prognostic biomarker and therapeutic targets.

Indexed as

Basic Helix-Loop-Helix Leucine Zipper Transcription FactorsCarcinoma, Renal CellChaperone-Mediated AutophagyDisease ProgressionKidney NeoplasmsOncogene Proteins, FusionAnimalsAutophagyCell Line, TumorHumansLipid DropletsLysosomal-Associated Membrane Protein 2MaleMiceMice, NudeBasic Helix-Loop-Helix Leucine Zipper Transcription FactorsLAMP2 protein, humanLysosomal-Associated Membrane Protein 2Oncogene Proteins, FusionTFE3 protein, humanAutophagyCancer progressionLipid dropletsLipid metabolismTFE3 rearranged renal cell carcinoma

Identifiers

PMID40050998
PMCPMC11887198

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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.