OTUD4 deubiquitination stabilizes EGFR and activates the PI3K/AKT pathway to promote the invasiveness of triple-negative breast cancer

The deubiquitinating enzyme OTUD4 functions as an oncogene in various cancers, but its role in triple-negative breast cancer (TNBC) remains unclear. Through bioinformatics analysis and experimental validation, we demonstrate that OTUD4 is overexpressed in TNBC and correlates with poor prognosis. OTUD4 downregulation reduces TNBC invasiveness, highlighting its oncogenic role. Mechanistically, OTUD4 promotes TNBC progression by stabilizing EGFR expression and activating the PI3K/AKT pathway. This stabilization occurs through two mechanisms: direct interaction between OTUD4 (568-1114aa) and EGFR (958-1210aa) and OTUD4-mediated cleavage of K48-linked polyubiquitin chains. Additionally, OTUD4 is recruited by NRP1 to deubiquitinate and further stabilize EGFR. These findings enhance our understanding of EGFR signaling in TNBC and may inform novel therapeutic strategies.

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Publication Details

Journal
Cell Death and Disease
Published
2026-02-23
DOI
https://doi.org/10.1038/s41419-026-08482-x
Primary Topic
Ubiquitin and proteasome pathways
Type
article
Field-Weighted Citation Impact
0.00

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article

OTUD4 deubiquitination stabilizes EGFR and activates the PI3K/AKT pathway to promote the invasiveness of triple-negative breast cancer

Yu Ren, Fulin Zhou, Shu Liu, Senguo Yang et al.
Cell Death and Disease
Ubiquitin and proteasome pathways
article

OTUD4 deubiquitination stabilizes EGFR and activates the PI3K/AKT pathway to promote the invasiveness of triple-negative breast cancer

Yu Ren, Fulin Zhou, Shu Liu, Senguo Yang, Mai Zhang, Shaolin Zhang, Zhihua Tan, Yonglin Zhang, Yumei Fu
article en

Abstract

The deubiquitinating enzyme OTUD4 functions as an oncogene in various cancers, but its role in triple-negative breast cancer (TNBC) remains unclear. Through bioinformatics analysis and experimental validation, we demonstrate that OTUD4 is overexpressed in TNBC and correlates with poor prognosis. OTUD4 downregulation reduces TNBC invasiveness, highlighting its oncogenic role. Mechanistically, OTUD4 promotes TNBC progression by stabilizing EGFR expression and activating the PI3K/AKT pathway. This stabilization occurs through two mechanisms: direct interaction between OTUD4 (568-1114aa) and EGFR (958-1210aa) and OTUD4-mediated cleavage of K48-linked polyubiquitin chains. Additionally, OTUD4 is recruited by NRP1 to deubiquitinate and further stabilize EGFR. These findings enhance our understanding of EGFR signaling in TNBC and may inform novel therapeutic strategies.

Cell Death and DiseaseVol. 17(1)
Guiyang Medical University (CN), Affiliated Hospital of Guizhou Medical University (CN), Guiyang University (CN), Liupanshui Normal University (CN), The First People's Hospital of Guiyang (CN), Qujiang People's Hospital (CN)
Guizhou Medical University, National Health Commission of the People's Republic of China
No poverty
Openalex Percentile: Top 45%
Ubiquitin and proteasome pathways
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