Non-enzymatic function of QSOX2 directly regulates the JUNB-ITGB4 axis and enhanced resistance to osimertinib in EGFR-mutation lung adenocarcinoma

Third-generation epidermal growth factor receptor tyrosine kinase inhibitors (EGFR-TKIs) represent a significant advancement in the targeted therapy of lung adenocarcinoma (LUAD), markedly prolonging patient overall survival. However, resistance remains a major barrier to sustained clinical benefit. Beyond the classical EGFR resistance pathways, EGFR-independent bypass mechanisms have emerged as a critical research focus. Quiescent sulfhydryl oxidase 2 (QSOX2), linked to poor outcomes in various cancers, remains poorly studied in LUAD, with its role in tumor progression mechanisms largely unknown. In this study, we demonstrated that the specific high expression of QSOX2 in LUAD induced osimertinib resistance (OR). Mechanistically, QSOX2 directly binds to and stabilizes the transcription factor JUNB via a non-enzymatic interaction, promoting JUNB phosphorylation and nuclear translocation through AKT pathway activation. This results in the transcriptional activation of ITGB4, which in turn initiates FAK/AKT signaling to establish a positive feedback loop that ultimately drives osimertinib bypass resistance. In conclusion, this study innovatively identified the non-enzymatic function of QSOX2 in regulating OR in EGFR-mutant LUAD through the JUNB-ITGB4-FAK/AKT pathway. The QSOX2/JUNB-ITGB4 signaling axis represents a potential therapeutic target for overcoming OR and offers a novel strategy to improve outcomes in LUAD patients.

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Publication Details

Journal
Cell Death Discovery
Published
2026-04-01
DOI
https://doi.org/10.1038/s41420-026-02969-4
Primary Topic
14-3-3 protein interactions
Type
article
Field-Weighted Citation Impact
0.00

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article

Non-enzymatic function of QSOX2 directly regulates the JUNB-ITGB4 axis and enhanced resistance to osimertinib in EGFR-mutation lung adenocarcinoma

Chaoxing Liu, Jianxiong Deng, Feng Qiu, Guohua Zhang et al.
Cell Death Discovery
14-3-3 protein interactions
article

Non-enzymatic function of QSOX2 directly regulates the JUNB-ITGB4 axis and enhanced resistance to osimertinib in EGFR-mutation lung adenocarcinoma

Chaoxing Liu, Jianxiong Deng, Feng Qiu, Guohua Zhang, Weiguo Gu, Jinyu Gan, Chao Shi, Feng Yu, Siya Wang, Ke Fang, Rong Qi, Chen Fang
article en

Abstract

Third-generation epidermal growth factor receptor tyrosine kinase inhibitors (EGFR-TKIs) represent a significant advancement in the targeted therapy of lung adenocarcinoma (LUAD), markedly prolonging patient overall survival. However, resistance remains a major barrier to sustained clinical benefit. Beyond the classical EGFR resistance pathways, EGFR-independent bypass mechanisms have emerged as a critical research focus. Quiescent sulfhydryl oxidase 2 (QSOX2), linked to poor outcomes in various cancers, remains poorly studied in LUAD, with its role in tumor progression mechanisms largely unknown. In this study, we demonstrated that the specific high expression of QSOX2 in LUAD induced osimertinib resistance (OR). Mechanistically, QSOX2 directly binds to and stabilizes the transcription factor JUNB via a non-enzymatic interaction, promoting JUNB phosphorylation and nuclear translocation through AKT pathway activation. This results in the transcriptional activation of ITGB4, which in turn initiates FAK/AKT signaling to establish a positive feedback loop that ultimately drives osimertinib bypass resistance. In conclusion, this study innovatively identified the non-enzymatic function of QSOX2 in regulating OR in EGFR-mutant LUAD through the JUNB-ITGB4-FAK/AKT pathway. The QSOX2/JUNB-ITGB4 signaling axis represents a potential therapeutic target for overcoming OR and offers a novel strategy to improve outcomes in LUAD patients.

Cell Death Discovery
Nanchang University (CN), First Affiliated Hospital of Jiangxi Medical College (CN), First Affiliated Hospital of Nanchang University (CN)
National Natural Science Foundation of China, Natural Science Foundation of Jiangxi Province
Openalex Percentile: Top 27%
14-3-3 protein interactions
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