ArticleDiscover oncology2025
OTUB1 promotes colorectal cancer progression by stabilizing GPX4 and inhibiting ferroptosis.
Article in Discover oncology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- OTUB1 Promotes HCC Progression by Regulating Glycolysis Through Deubiquitination of PKM2.Molecular carcinogenesis · 2026Article
- Deubiquitinating enzymes-mediated post-translational modifications of ferroptosis regulates cancer drug resistance.Discover oncology · 2026Review
- OTU deubiquitinases as immune-circuit editors: from human immunopathology to therapeutic prioritization.Frontiers in immunology · 2026Review
- Multidimensional analysis of deubiquitinating enzymes in colorectal cancer: biological mechanisms and targeted therapeutic strategies.Frontiers in oncology · 2026Review
- Ferroptosis-Mediated Cell-Specific Damage: Molecular Cascades and Therapeutic Breakthroughs in Diabetic Retinopathy.Antioxidants (Basel, Switzerland) · 2025Review
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundTherapeutic resistance in colorectal cancer (CRC) is frequently linked to dysregulated protein homeostasis, which enables tumor cells to evade cell death. The ubiquitin-proteasome system (UPS) plays a pivotal role in regulating protein stability and has been implicated in ferroptosis, an iron-dependent form of cell death driven by lipid peroxidation. Otubain1 (OTUB1), a deubiquitinase within the UPS, is hypothesized to regulate ferroptosis by stabilizing GPX4, a key inhibitor of ferroptosis.
aimThis study investigates the regulatory role of OTUB1 in ferroptosis through its interaction with GPX4, aiming to uncover a novel therapeutic axis for CRC.
methodsOTUB1 expression was manipulated in CRC cells using siRNA-mediated knockdown and plasmid-based overexpression. GPX4 expression, ROS levels, lipid peroxidation, and cell viability were assessed using qRT-PCR, Western blotting, and functional assays. Co-immunoprecipitation (Co-IP) assay was performed to confirm the interaction between OTUB1 and GPX4.
resultsOTUB1 knockdown led to a significant reduction in GPX4 protein levels, leading to elevated ROS, increased lipid peroxidation, and decreased cell viability. Conversely, GPX4 overexpression in OTUB1-knockdown cells restored cell viability and reversed ferroptosis markers (P < 0.01). Co-IP assay confirmed that OTUB1 interacted with GPX4 and prevented its ubiquitin-mediated degradation, thereby stabilizing GPX4.
conclusionThis study identifies OTUB1 as a novel regulator of ferroptosis in CRC through the stabilization of GPX4. Targeting the OTUB1-GPX4 axis may provide a new therapeutic approach for inducing ferroptosis in CRC cells, potentially overcoming resistance to conventional therapies and improving patient outcomes.
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