Evidence map›Paper›PMID 40643801›Full record

ArticleScience China. Life sciences2025

SUMO-activating enzyme subunit 1 (SAE1) promotes non-small cell lung cancer metastasis by promoting the epithelial-mesenchymal transition through the SUMOylation of N-cadherin.

Yaru Wang, Xijun Wang, Huan Zhao, Jie Song, Wenhao Hou, Zhenrong Liu, Xin Yang, Sheng Ma, Ruiqi Zheng, Huiqin Guo and 2 more

Abstract read
PubMed Publisher
In one paragraph

Article in Science China. Life sciences, 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. BMJ open gastroenterology · 2026
    Article
  2. 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

12 authors.

Yaru WangState Key Laboratory of Molecular Oncology, Department of Etiology and Carcinogenesis, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Xijun WangState Key Laboratory of Molecular Oncology, Department of Etiology and Carcinogenesis, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Huan ZhaoDepartment of Pathology, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Jie SongState Key Laboratory of Molecular Oncology, Department of Etiology and Carcinogenesis, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Wenhao HouState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, Beijing, 102206, China.
Zhenrong LiuState Key Laboratory of Molecular Oncology, Department of Etiology and Carcinogenesis, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Xin YangDepartment of Pathology, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Sheng MaState Key Laboratory of Molecular Oncology, Department of Etiology and Carcinogenesis, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Ruiqi ZhengState Key Laboratory of Molecular Oncology, Department of Etiology and Carcinogenesis, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China.
Huiqin GuoDepartment of Pathology, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China. ghqin2006@163.com.
Wantao YingState Key Laboratory of Proteomics, National Center for Protein Sciences (Beijing), Beijing Proteome Research Center, Beijing Institute of Lifeomics, Beijing, 102206, China. yingwantao@nspsb.org.cn.
Ting XiaoState Key Laboratory of Molecular Oncology, Department of Etiology and Carcinogenesis, National Cancer Center/National Clinical Research Center for Cancer/Cancer Hospital, Chinese Academy of Medical Sciences and Peking Union Medical College, Beijing, 100021, China. xiaot@cicams.ac.cn.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein SUMOylation is a newly discovered process similar to protein ubiquitination and is crucial for protein stability and protein localization. SAE1 is an important enzyme that initiates protein SUMOylation, but its role in the progression of non-small cell lung cancer remains unknown. We analyzed the protein expression profiles of non-small cell lung cancer tissues and single-cell sequencing data and confirmed that SAE1 is highly expressed in non-small cell lung cancer cells and is associated with a malignant phenotype. Knockdown of SAE1 decreased the growth, cell cycle progression, and metastasis of non-small cell lung cancer cells both in vitro and in vivo. Mechanistically, using the protein expression profile of non-small cell lung cancer cell lines with altered SAE1 expression, we showed that SAE1, a key molecule mediating protein SUMOylation, can SUMOylate the epithelial-mesenchymal transition-related protein N-cadherin, stabilize N-cadherin and promote the occurrence of the EMT in non-small cell lung cancer cells, leading to lung cancer invasion and metastasis. In clinical application, we used sputum samples from patients with lung cancer or chronic pulmonary obstructive pulmonary disease for protein profiling and further used sputum-based thin-slice technology for experimental verification, which confirmed the application potential of SAE1 in the diagnosis of lung cancer patients. In summary, our findings reveal a critical role for SAE1 as an oncogene in lung cancer cells and suggest that SAE1 may be used for the diagnosis of lung cancer patients.

Indexed as

Antigens, CDCadherinsCarcinoma, Non-Small-Cell LungEpithelial-Mesenchymal TransitionLung NeoplasmsUbiquitin-Activating EnzymesAnimalsCell Line, TumorCell ProliferationGene Expression Regulation, NeoplasticHumansMiceMice, NudeNeoplasm MetastasisSumoylationAntigens, CDCadherinsCDH2 protein, humanSAE1 protein, humanUbiquitin-Activating Enzymesdiagnostic biomarkerepithelial-mesenchymal transitionnon-small cell lung cancerprotein SUMOylation

Identifiers

PMID40643801

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.