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Radiotherapy, a treatment method employing radiation to eradicate tumor cells and subsequently reduce or eliminate tumor masses, is widely applied in the management of numerous patients with tumors. However, its therapeutic effectiveness is somewhat constrained by various drug-resistant factors. Recent studies have highlighted the ubiquitination/deubiquitination system, a reversible molecular modification pathway, for its dual role in influencing tumor behaviors. It can either promote or inhibit tumor progression, impacting tumor proliferation, migration, invasion, and associated therapeutic resistance. Consequently, delving into the potential mechanisms through which ubiquitination and deubiquitination systems modulate the response to radiotherapy in malignant tumors holds paramount significance in augmenting its efficacy. In this paper, we comprehensively examine the strides made in research and the pertinent mechanisms of ubiquitination and deubiquitination systems in governing radiotherapy resistance in tumors. This underscores the potential for developing diverse radiosensitizers targeting distinct mechanisms, with the aim of enhancing the effectiveness of radiotherapy.
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http://dx.doi.org/10.3390/biomedicines11123240 | DOI Listing |
Front Pharmacol
August 2025
Department of Pharmacy, Zigong Maternal and Child Health Care Hospital, Zigong, China.
This review comprehensively summarizes the current understanding of ubiquitin-specific protease 30 (USP30), covering its structural characteristics, functions in cellular processes, associations with diseases, diagnostic and therapeutic strategies, as well as controversies and future perspectives. USP30, a deubiquitinating enzyme, plays crucial roles in mitochondrial quality control, autophagy regulation, and cellular homeostasis. It is implicated in the progression of several malignancies, including hepatocellular carcinoma, breast carcinoma, and glioblastoma, as well as neurodegenerative disorders such as Parkinson's disease.
View Article and Find Full Text PDFPhytomedicine
September 2025
Department of Cardiology, Laboratory of Heart Center, Zhujiang Hospital, Southern Medical University, Guangzhou, Guangdong, China; Heart Center of Zhujiang Hospital, Guangdong Provincial Biomedical Engineering Technology Research Center for Cardiovascular Disease, Guangzhou, Guangdong, China; Heart
Background: Impaired autophagic flux is an essential contributor to doxorubicin (DOX)-induced cardiotoxicity (DIC). TFEB is recognized as a key regulator of DOX-induced autolysosome accumulation; however, the mechanisms by which DOX suppresses TFEB expression remain unclear. 20-Deoxyingenol (20-DOI) is a small-molecule compound whose potential protective effects against DIC has not yet been elucidated.
View Article and Find Full Text PDFRedox Biol
September 2025
Department of Cardiology, Shanghai General Hospital, Shanghai Jiaotong University School of Medicine, 201620, China. Electronic address:
Pathological cardiac hypertrophy, driven by mitochondrial dysfunction and maladaptive remodeling, remains a therapeutic challenge. This study explores the cardioprotective properties of tectorigenin (Tec) in the context of transverse aortic constriction (TAC)-induced hypertrophy, focusing on mitochondrial homeostasis. In animal models, administration of Tec improved survival rates, reduced cardiac dysfunction, and decreased hypertrophy and fibrosis in TAC mice, while preserving mitochondrial function.
View Article and Find Full Text PDFFront Mol Biosci
August 2025
Yan'an Medical College, Yan'an University, Yan'an, China.
Ubiquitination and deubiquitination are common forms of protein post-translational modifications that play crucial roles in the regulation of intracellular homeostasis. As a member of deubiquitination enzyme USP family, USP36 maintains the stability of substrate proteins by mediating their deubiquitination, thereby playing a significant role in various pathophysiological processes. Here we focus on discussing how USP36 participates in regulating ribosome biosynthesis and responds to ribotoxic stress response.
View Article and Find Full Text PDFJ Biol Chem
September 2025
Department of Systems Biology, College of Life Science and Biotechnology, Yonsei University, Seoul, 03722, Korea. Electronic address:
Leucine-rich repeat kinase 2 (LRRK2), a large protein with kinase and GTPase activities, regulates various cellular pathways, including autophagy, endocytosis, and mitochondrial dynamics. LRRK2, extensively studied in the context of Parkinson's disease, is functionally impaired in other pathological conditions as well, including inflammatory bowel disease, cancer, and cardiovascular diseases. Despite its critical functions, the mechanisms controlling LRRK2 protein stability are not fully understood.
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