Fbxo45 promotes the malignant development of esophageal squamous cell carcinoma by targeting GGNBP2 for ubiquitination and degradation

Wang, Qi; Wu, Linhui; Cao, Ruoxue; Gao, Jing; Chai, Damin; Qin, Yanzi; Ma, Li; Wu, Shiwu; Tao, Yisheng; Ma, Jia; Wang, Zhi-wei

doi:10.1038/s41388-022-02468-7

Cited by 14 publications

(6 citation statements)

References 49 publications

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“…Cao et al reported that lncRNA CACNA1C-AS2 regulated the expression of FBXO45 and PI3K/Akt/mTOR pathways, contributing to suppression of invasion, migration and proliferation in glioma [ 38 ]. Wang and colleagues reported that FBXO45 accelerated tumor malignant progression via regulation of ubiquitination and degradation of GGNBP2 in esophageal squamous cell carcinoma [ 39 ]. Using a chemically induced mouse model of HCC, one study revealed that FBXO45 promoted fibrosis and inflammation in HCC [ 40 ].…”

Section: Discussionmentioning

confidence: 99%

Fbxo45 facilitates the malignant progression of breast cancer by targeting Bim for ubiquitination and degradation

Zheng,

Wu,

Xiao

et al. 2024

BMC Cancer

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Background Breast cancer is one of the common malignancies in women. Evidence has demonstrated that FBXO45 plays a pivotal role in oncogenesis and progression. However, the role of FBXO45 in breast tumorigenesis remains elusive. Exploration of the regulatory mechanisms of FBXO45 in breast cancer development is pivotal for potential therapeutic interventions in patients with breast cancer. Methods Hence, we used numerous approaches to explore the functions of FBXO45 and its underlaying mechanisms in breast cancer pathogenesis, including CCK-8 assay, EdU assay, colony formation analysis, apoptosis assay, RT-PCR, Western blotting, immunoprecipitation, ubiquitination assay, and cycloheximide chase assay. Results We found that downregulation of FBXO45 inhibited cell proliferation, while upregulation of FBXO45 elevated cell proliferation in breast cancer. Silencing of FBXO45 induced cell apoptosis, whereas overexpression of FBXO45 inhibited cell apoptosis in breast cancer. Moreover, FBXO45 interacted with BIM and regulated its ubiquitination and degradation. Furthermore, knockdown of FBXO45 inhibited cell proliferation via regulation of BIM pathway. Notably, overexpression of FBXO45 facilitated tumor growth in mice. Strikingly, FBXO45 expression was associated with poor survival of breast cancer patients. Conclusion Our study could provide the rational for targeting FBXO45 to obtain benefit for breast cancer patients. Altogether, modulating FBXO45/Bim axis could be a promising strategy for breast cancer therapy.

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Section: Discussionmentioning

confidence: 99%

Fbxo45 facilitates the malignant progression of breast cancer by targeting Bim for ubiquitination and degradation

Zheng,

Wu,

Xiao

et al. 2024

BMC Cancer

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“…In addition, the ubiquitinproteasome pathway also plays an important role in the development of ESCC. For example, Fbxo45 promotes ESCC oncology by targeting ubiquitous degradation of the tumor inhibitory factor GGNBP2 [25].…”

Section: Discussionmentioning

confidence: 99%

RIG-I Promotes Cell Proliferation in Esophageal Squamous Cell Carcinoma by Facilitating p21 Degradation

Wang,

Zhang,

Gao

et al. 2023

Preprint

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Background Retinoic acid-inducible gene-I (RIG-I) is considered a key sensor for host recognition of RNA virus infections. Recent studies have shown that RIG-I also regulates carcinogenesis. However, the role of RIG-I in esophageal squamous cell carcinoma (ESCC) remains unclear. Method We investigated the RIG-I expression in ESCC cells using a public database, immunohistochemistry, and Western blotting. We evaluated the proliferative activity of ESCC cells using CCK-8, colony formation, and EdU staining assays. Further, we determined the ESCC cell cycle changes using flow cytometry and the ubiquitination of p21 in the cells using cycloheximide chase and ubiquitination assays. Finally, we verified the in vivo effects of RIG-I on ESCC cells by constructing xenograft models. Results RIG-I was highly expressed in ESCC cells and significantly promoted their proliferation and cell cycle. Moreover, RIG-I knockdown inhibited xenograft growth in nude mice. Furthermore, RIG-I accelerated the cell cycle by promoting the ubiquitination and degradation of p21. Conclusion Overall, this study revealed that the increased expression of RIG-I due to ESCC accelerated the progression of esophageal cancer by promoting the ubiquitination and degradation of p21, which is related to the prognosis of ESCC. Thus, RIG-I may be a novel therapeutic target for ESCC treatment.

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“…F-box protein is a subunit of SCF E3 ligase complexes and has been characterized to involve in numerous biological functions in human cancer, such as apoptosis, invasion, cell cycle, proliferation, autophagy, drug resistance, EMT, cancer stem cells and metastasis (31)(32)(33)(34). SCF E3 ligase consists of adaptor SKP1, scaffold Cullin-1, RBX1 or RBX2 and F-box protein.…”

Section: F-box Proteinsmentioning

confidence: 99%

The E3 ubiquitin ligases regulate PD-1/PD-L1 protein levels in tumor microenvironment to improve immunotherapy

et al. 2023

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The tumor microenvironment (TME) is the tumor surrounding environment, which is critical for tumor development and progression. TME is also involved in clinical intervention and treatment outcomes. Modulation of TME is useful for improving therapy strategies. PD-L1 protein on tumor cells interacts with PD-1 protein on T cells, contributing to T cell dysfunction and exhaustion, blockage of the immune response. Evidence has demonstrated that the expression of PD-1/PD-L1 is associated with clinical response to anti-PD-1/PD-L1 therapy in cancer patients. It is important to discuss the regulatory machinery how PD-1/PD-L1 protein is finely regulated in tumor cells. In recent years, studies have demonstrated that PD-1/PD-L1 expression was governed by various E3 ubiquitin ligases in TME, contributing to resistance of anti-PD-1/PD-L1 therapy in human cancers. In this review, we will discuss the role and molecular mechanisms of E3 ligases-mediated regulation of PD-1 and PD-L1 in TME. Moreover, we will describe how E3 ligases-involved PD-1/PD-L1 regulation alters anti-PD-1/PD-L1 efficacy. Altogether, targeting E3 ubiquitin ligases to control the PD-1/PD-L1 protein levels could be a potential strategy to potentiate immunotherapeutic effects in cancer patients.

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Fbxo45 promotes the malignant development of esophageal squamous cell carcinoma by targeting GGNBP2 for ubiquitination and degradation

Cited by 14 publications

References 49 publications

Fbxo45 facilitates the malignant progression of breast cancer by targeting Bim for ubiquitination and degradation

Fbxo45 facilitates the malignant progression of breast cancer by targeting Bim for ubiquitination and degradation

RIG-I Promotes Cell Proliferation in Esophageal Squamous Cell Carcinoma by Facilitating p21 Degradation

The E3 ubiquitin ligases regulate PD-1/PD-L1 protein levels in tumor microenvironment to improve immunotherapy

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