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Open AccessDOI: 10.3724/abbs.2026044Original Research

Ubiquitin-dependent degradation of MBD3 by TRIM59 promotes lung adenocarcinoma

🇨🇳 Original Chinese Title: Ubiquitin-dependent degradation of MBD3 by TRIM59 promotes lung adenocarcinoma

Wenhui Yang¹,Jin Ren¹,Yufang Wang¹,Jiahe Shi¹,Ziwan Cai¹,Cuihong Cai¹,Jing Zheng¹,Jingjing Qu¹,Jianya Zhou¹

Department of Respiratory Disease, Thoracic Disease Center, The First Affiliated Hospital, College of Medicine, Zhejiang University, Hangzhou 310003, China

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Ubiquitin-dependent degradation of MBD3 by TRIM59 promotes lung adenocarcinoma
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Published In
Acta Biochimica et Biophysica Sinica
Published:January 15, 2026Edition:Vol 68, Issue 12 • pp. 100-112Citation:Wenhui Yang et al. (2026), Acta Biochimica et Biophysica Sinica
Impact FactorPremier Chinese Biomedical Journal indexed in SinoBioData: Acta Biochimica et Biophysica Sinica (生物化学与生物物理学报).
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Key Takeaways & Executive Findings

  • • TRIM59 is identified as the E3 ubiquitin ligase that targets MBD3 for proteasomal degradation, with key ubiquitination sites at K41, K90, and K92. • The TRIM59-MBD3 axis derepresses HSF1 and HSF2, promoting malignant proliferation and tumor progression in lung adenocarcinoma. • TRIM59 and MBD3 show inverse expression patterns in LUAD tissues, with TRIM59 upregulated and MBD3 downregulated, supporting oncogenesis. • The TRIM59-MBD3 ubiquitination cascade represents a potential therapeutic vulnerability in lung adenocarcinoma.
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Abstract

Methyl-CpG binding domain protein 3 (MBD3) functions as a critical tumor suppressor in lung adenocarcinoma (LUAD), yet the ubiquitin-dependent mechanisms orchestrating its proteasomal turnover remain elusive. Here, we demonstrate that MBD3 undergoes ubiquitination and identify tripartite motif-containing protein 59 (TRIM59) as the cognate E3 ligase. TRIM59 physically associates with the N-terminal MBD domain of MBD3 and catalyzes its polyubiquitination and degradation, and mass spectrometry mapping reveals that this process occurs primarily at lysine residues K41, K90, and K92. Functional characterization of the TRIM59-MBD3 axis in vivo reveals its role in derepressing the heat shock transcription factors HSF1 and HSF2, thereby driving malignant proliferation and tumor progression. Tissue microarray immunohistochemistry reveals that TRIM59 is upregulated, whereas MBD3 is downregulated in LUAD tissues, establishing an inverse expression pattern that supports oncogenesis. Our findings unveil an unappreciated layer of MBD3 regulation and identify the TRIM59-MBD3 ubiquitination cascade as a potential therapeutic vulnerability in LUAD.

1. Introduction

Lung cancer remains the leading cause of cancer-related mortality worldwide, with lung adenocarcinoma (LUAD) representing the most common histological subtype [1]. Despite advances in targeted therapies and immunotherapy, the 5-year survival rate for advanced LUAD remains dismal, largely due to acquired drug resistance and metastatic progression [2,3]. This clinical challenge underscores the urgent need to elucidate the molecular mechanisms driving LUAD pathogenesis and to identify novel therapeutic targets that regulate tumor cell proliferation and survival.

Post-translational modifications, particularly ubiquitination, play pivotal roles in maintaining protein homeostasis and regulating cellular signaling pathways implicated in cancer development [4,5]. The ubiquitin-proteasome system (UPS) mediates the selective degradation of key regulatory proteins, with E3 ubiquitin ligases serving as critical determinants of substrate specificity [4]. Dysregulation of E3 ligase activity frequently contributes to oncogenesis, either through the destabilization of tumor suppressors or the stabilization of oncoproteins [6–9]. Understanding the specific E3 ligase-substrate networks operational in cancer cells therefore offers significant potential for therapeutic intervention.

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Cite This Research Paper
Wenhui Yang, Jin Ren, Yufang Wang, Jiahe Shi, Ziwan Cai, Cuihong Cai, Jing Zheng, Jingjing Qu, Jianya Zhou (2026). Ubiquitin-dependent degradation of MBD3 by TRIM59 promotes lung adenocarcinoma. Acta Biochimica et Biophysica Sinica. https://doi.org/10.3724/abbs.2026044
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Frequently Asked Questions

What is the role of MBD3 in lung adenocarcinoma?

MBD3 functions as a critical tumor suppressor in lung adenocarcinoma (LUAD), suppressing cancer cell proliferation and clonogenic growth.

How does TRIM59 regulate MBD3?

TRIM59 acts as an E3 ubiquitin ligase that binds to the N-terminal MBD domain of MBD3 and catalyzes its polyubiquitination and degradation via the proteasome, primarily at lysine residues K41, K90, and K92.

What are the downstream effects of TRIM59-mediated MBD3 degradation?

Degradation of MBD3 by TRIM59 derepresses heat shock transcription factors HSF1 and HSF2, driving malignant proliferation and tumor progression in lung adenocarcinoma.

What is the clinical significance of TRIM59 and MBD3 expression in LUAD?

In LUAD tissues, TRIM59 is upregulated while MBD3 is downregulated, showing an inverse expression pattern that supports oncogenesis. This suggests the TRIM59-MBD3 axis as a potential therapeutic target.

How was the TRIM59-MBD3 interaction identified?

The study used mass spectrometry mapping and co-immunoprecipitation to identify TRIM59 as the cognate E3 ligase for MBD3 and to map the ubiquitination sites.

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