E3 Ubiquitin ligase RNF126 regulates the progression of tongue cancer

Wang, Lina; Wang, Xin; Zhao, Yang; Niu, Weidong; Ma, Guowu; Shi, Chun

doi:10.1002/cam4.771

Cited by 16 publications

(27 citation statements)

References 17 publications

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“…Therefore, we further determined the activation of AKT, the critical component of PI3K/AKT signal pathway. Although it has several phosphorylation sites, phosphorylation of Ser308 and Thr473 is the sign of AKT activation . Our results suggested that knockdown of MG53 significantly promoted the phosphorylation of AKT Ser308 and AKT Thr473 in SCC25 cells ( Figure ).…”

Section: Resultsmentioning

confidence: 57%

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MG53 Inhibits the Progression of Tongue Cancer Cells through Regulating PI3K‐AKT Signaling Pathway: Evidence from 3D Cell Culture and Animal Model

Liu

Bian

2019

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MG53 is transcriptionally activated by the IRS‐1/PI3K/AKT signal pathway, which is closely related with oncogenesis of several tumors. Here, the role of MG53 in the tumorigenesis of tongue cancer is analyzed in vitro and in vivo. The stable MG53 overexpression/knockdown SCC9 and SCC25 cells are constructed through retrovirus infection. Then a PLGA cylinder is used to provide a 3D culture environment for cell growth. Cell counting results suggest that overexpression of MG53 inhibits the cell proliferation and colony formation of SCC9 and SCC25 cells. While knockdown of MG53 has the opposite effect. Furthermore, knockdown of MG53 significantly promotes the invasion of SCC9 and SCC25 cells. Western blotting data confirm that MG53 affects the expression of the AKT signaling pathway. In a xenograft assay, knockdown of MG53 promotes the growth of xenograft which is induced by SCC25 cells in nude mice. The findings demonstrate that MG53 affects the biological behavior of human tongue cancer SCC9 and SCC25 cells.

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Section: Resultsmentioning

confidence: 57%

“…Cell Culture, Plasmid and RNAi Construction : Human tongue cancer cell lines, SCC9 and SCC25 cells, were cultured in complete DMEM medium which had 10% FBS and 1% Penicillin–Streptomycin. Mammalian expression plasmids, MG53 and MG53‐RNAi, were constructed with the same protocol of the previous report …”

Section: Methodsmentioning

confidence: 99%

MG53 Inhibits the Progression of Tongue Cancer Cells through Regulating PI3K‐AKT Signaling Pathway: Evidence from 3D Cell Culture and Animal Model

Liu

Bian

2019

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“…A literature review of the other 5 targets showed that some of these genes have been previously studied in tumor diseases. RNF126 promotes the proliferation and viability of tongue cancer by regulating the AKT signaling pathway [ 36 ]. RNF126 was found to positively regulate BRCA1 by directly interacting with E2F1 for homologous recombination in breast and ovarian cancer [ 37 ].…”

Section: Discussionmentioning

confidence: 99%

Upregulation of DARS2 by HBV promotes hepatocarcinogenesis through the miR-30e-5p/MAPK/NFAT5 pathway

Qin

Guo

et al. 2017

J Exp Clin Cancer Res

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BackgroundInfection with the hepatitis B virus (HBV) is closely associated with the development of hepatocellular carcinoma (HCC). The osmoregulatory transcription factor nuclear factor of activated T-cells 5 (NFAT5) has been shown to play an important role in the development of many types of human cancers. The role of NFAT5 in HBV-associated HCC has never previously been investigated.MethodsWe compared expression profiles of NFAT5, DARS2 and miR-30e-5p in HCC samples, adjacent nontumor tissues and different hepatoma cell lines by quantitative real-time polymerase chain reaction and /or Western blot. Clinical data of HCC patients for up to 80 months were analyzed. The regulatory mechanisms upstream and convergent downstream pathways of NFAT5 in HBV-associated HCC were investigated by ChIP-seq, MSP, luciferase report assay and bioinformation anaylsis.ResultsWe first found that higher levels of NFAT5 expression predict a good prognosis, suggesting that NFAT5 is a potential tumor-suppressing gene, and verified that NFAT5 promotes hepatoma cell apoptosis and inhibits cell growth in vitro. Second, our results showed that HBV could suppress NFAT5 expression by inducing hypermethylation of the AP1-binding site in the NFAT5 promoter in hepatoma cells. In addition, HBV also inhibited NFAT5 through miR-30e-5p targeted MAP4K4, and miR-30e-5p in turn inhibited HBV replication. Finally, we demonstrated that NFAT5 suppressed DARS2 by directly binding to its promoter. DARS2 was identified as an HCC oncogene that promotes HCC cell cycle progression and inhibits HCC cell apoptosis.ConclusionHBV suppresses NFAT5 through the miR-30e-5p/mitogen-activated protein kinase (MAPK) signaling pathway upstream of NFAT5 and inhibits the NFAT5 to enhance HCC tumorigenesis via the downstream target genes of DARS2.Electronic supplementary materialThe online version of this article (10.1186/s13046-017-0618-x) contains supplementary material, which is available to authorized users.

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“…RNF126 has been implicated in a number of physiological and pathological processes, such as cancer progression, membrane receptor trafficking, and immune response modulation. RNF126 was shown to ubiquitinate and promote the degradation of the tumor suppressor p21 ( Zhi et al., 2013 ) and to enhance the Akt signaling pathway ( Wang et al., 2016 ). Moreover, it was shown to regulate the endosomal sorting of the epidermal growth factor receptor (EGFR) ( Smith et al., 2013 ) and cation-independent mannose 6-phosphate receptor (CI-MPR) ( Smith and McGlade, 2014 ) and to induce ubiquitination of the activation-induced cytidine deaminase (AID), an enzyme involved in the process of antibody diversification in the immune system ( Delker et al., 2013 ).…”

Section: Discussionmentioning

confidence: 99%

E3 Ligase RNF126 Directly Ubiquitinates Frataxin, Promoting Its Degradation: Identification of a Potential Therapeutic Target for Friedreich Ataxia

et al. 2017

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SummaryFriedreich ataxia (FRDA) is a severe genetic neurodegenerative disease caused by reduced expression of the mitochondrial protein frataxin. To date, there is no therapy to treat this condition. The amount of residual frataxin critically affects the severity of the disease; thus, attempts to restore physiological frataxin levels are considered therapeutically relevant. Frataxin levels are controlled by the ubiquitin-proteasome system; therefore, inhibition of the frataxin E3 ligase may represent a strategy to achieve an increase in frataxin levels. Here, we report the identification of the RING E3 ligase RNF126 as the enzyme that specifically mediates frataxin ubiquitination and targets it for degradation. RNF126 interacts with frataxin and promotes its ubiquitination in a catalytic activity-dependent manner, both in vivo and in vitro. Most importantly, RNF126 depletion results in frataxin accumulation in cells derived from FRDA patients, highlighting the relevance of RNF126 as a new therapeutic target for Friedreich ataxia.

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E3 Ubiquitin ligase RNF126 regulates the progression of tongue cancer

Cited by 16 publications

References 17 publications

MG53 Inhibits the Progression of Tongue Cancer Cells through Regulating PI3K‐AKT Signaling Pathway: Evidence from 3D Cell Culture and Animal Model

MG53 Inhibits the Progression of Tongue Cancer Cells through Regulating PI3K‐AKT Signaling Pathway: Evidence from 3D Cell Culture and Animal Model

Upregulation of DARS2 by HBV promotes hepatocarcinogenesis through the miR-30e-5p/MAPK/NFAT5 pathway

E3 Ligase RNF126 Directly Ubiquitinates Frataxin, Promoting Its Degradation: Identification of a Potential Therapeutic Target for Friedreich Ataxia

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