E3 ubiquitin ligase tripartite motif-containing 71 promotes the proliferation of non-small cell lung cancer through the inhibitor of kappaB-α/nuclear factor kappaB pathway

Ren, Hongjiu; Xu, Yitong; Wang, Qiongzi; Jiang, Jun; Wudumuli,; Hui, Lian; Zhang, Qingfu; Zhang, Xiupeng; Wang, Enhua; Sun, Liankun; Qiu, Xueshan

doi:10.18632/oncotarget.19075

Cited by 25 publications

(32 citation statements)

References 35 publications

(22 reference statements)

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“…Consistent with our findings, TRIM71 has also been shown to have a tumor suppressive role in lung and colon cancer cells by mediating degradation of LIN28B and consequently upregulating the tumor suppressive microRNA let-7 38,39 . But, it has also been reported that TRIM71 might act as an oncoprotein to activate the NF-κB signaling pathway by degrading IκB-α, or repress the Argonautes-microRNA pathway, leading to development of lung and liver carcinomas 40,41 . These divergent findings may reflect the complexity and heterogeneity of cancers.…”

Section: Discussionmentioning

confidence: 99%

Ubiquitin ligase TRIM71 suppresses ovarian tumorigenesis by degrading mutant p53

et al. 2019

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Hotspot p53 mutants augment cancer cell proliferation, metastasis and metabolism through their gain-of-function (GOF). Ovarian cancer sustains the highest frequency of TP53 mutations, but the mechanisms underlying regulation of mutant p53s’ GOF in this type of cancer remain incompletely understood. Herein, we identified the E3-ubiquitin ligase TRIM71 as a novel mutant p53-binding protein. Ectopic TRIM71-induced ubiquitination and proteasomal degradation of mutant p53 by binding to its transactivation (TA) domain, and inhibited the expression of a broad spectrum of mutant p53 target genes. Ectopic TRIM71 also restrained, whereas ablation of TRIM71 endorsed, ovarian carcinoma cell growth in vitro and in vivo. Significantly, TRIM71 overexpression is highly associated with favorable prognosis, particularly, in TP53-mutated ovarian carcinomas. Altogether, our findings unveil the anti-tumor function of TRIM71 in ovarian cancer development and prognosis by downregulating mutant p53s.

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Section: Discussionmentioning

confidence: 99%

Ubiquitin ligase TRIM71 suppresses ovarian tumorigenesis by degrading mutant p53

et al. 2019

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“…Other TRIMs, although do not exert a specific role in the regulation of cell cycle phase transitions, are yet involved in controlling carcinogenesis and cancer progression (Table 1). Most of these TRIMs, like TRIM11 [70,71,72,73,74], TRIM23 [75], TRIM24 [76], TRIM25 [77,78,79], TRIM31 [80], TRIM37 [81], TRIM47 [82,83], TRIM65 [84], and TRIM71 [85] are up-regulated in cancer cells and tissues, playing an oncogenic role in different types of cancer. These TRIMs are often associated with unfavorable prognosis and promote cancer cells proliferation and migration, being often associated with proteins of central signaling pathways.…”

Section: Trims and Cell Cycle Progressionmentioning

confidence: 99%

E3 Ubiquitin Ligase TRIM Proteins, Cell Cycle and Mitosis

Venuto

Merla

2019

Cells

112

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The cell cycle is a series of events by which cellular components are accurately segregated into daughter cells, principally controlled by the oscillating activities of cyclin-dependent kinases (CDKs) and their co-activators. In eukaryotes, DNA replication is confined to a discrete synthesis phase while chromosome segregation occurs during mitosis. During mitosis, the chromosomes are pulled into each of the two daughter cells by the coordination of spindle microtubules, kinetochores, centromeres, and chromatin. These four functional units tie chromosomes to the microtubules, send signals to the cells when the attachment is completed and the division can proceed, and withstand the force generated by pulling the chromosomes to either daughter cell. Protein ubiquitination is a post-translational modification that plays a central role in cellular homeostasis. E3 ubiquitin ligases mediate the transfer of ubiquitin to substrate proteins determining their fate. One of the largest subfamilies of E3 ubiquitin ligases is the family of the tripartite motif (TRIM) proteins, whose dysregulation is associated with a variety of cellular processes and directly involved in human diseases and cancer. In this review we summarize the current knowledge and emerging concepts about TRIMs and their contribution to the correct regulation of cell cycle, describing how TRIMs control the cell cycle transition phases and their involvement in the different functional units of the mitotic process, along with implications in cancer progression.

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“…Tripartite motif (TRIM) family proteins are considered as a kind of E3 ubiquitin ligase, with more than 80 members identified in humans to date [ 10 ]. They exert diverse biological functions in human, such as cell proliferation, apoptosis, invasion, innate immunity, and autophagy [ 11 – 15 ]. TRIM52 is a novel TRIM family protein.…”

Section: Introductionmentioning

confidence: 99%

Tripartite Motif Containing 52 (TRIM52) Promotes Cell Proliferation in Hepatitis B Virus-Associated Hepatocellular Carcinoma

Zhang

Chen

et al. 2017

Med Sci Monit

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BackgroundChronic hepatitis B virus (HBV) infection is the major cause of hepatocellular carcinoma (HCC). HBV X protein (HBx) plays a crucial role in the development of HCC. Moreover, many tripartite motif (TRIM) family proteins exert diverse biological functions in hepatocarcinogenesis. However, as a novel member of this family, the specific effect of TRIM52 is still largely obscure. In the present study, we investigated the expression and function of TRIM52 in HBV-associated HCC.Material/MethodsFluorescence quantitative polymerase chain reaction (FQ-PCR) was performed to detect the HBV DNA levels in the peripheral blood of HCC patients. Quantitative real-time PCR (qRT-PCR) and Western blot analysis were performed to detect the expression of TRIM52, HBx, and NF-κB p65. HBx-pcDNA3.1 and TRIM52-shRNA were used to induce HBx ectopic expression and TRIM52 silencing, respectively. Pyrrolidine dithiocarbamate (PDTC) was used to block the activation of NF-κB. Cell proliferation was detected using the Cell Counting Kit-8 (CCK-8) assay.ResultsTRIM52 expression was up-regulated together with HBx in HBV-associated HCC tissues. Ectopic expression of HBx elevated TRIM52 expression in HepG2 cells. TRIM52 silencing repressed the proliferation of HepG2.2.15 cells. Moreover, NF-κB p65 expression was increased in HCC cell lines. Blocking NF-κB activation with PDTC suppressed TRIM52 expression and attenuated the viability of HepG2.2.15 cells.ConclusionsThese findings indicate that TRIM52 can promote cell proliferation and HBx may regulate TRIM52 expression via the NF-κB signaling pathway in HBV-associated HCC.

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E3 ubiquitin ligase tripartite motif-containing 71 promotes the proliferation of non-small cell lung cancer through the inhibitor of kappaB-α/nuclear factor kappaB pathway

Cited by 25 publications

References 35 publications

Ubiquitin ligase TRIM71 suppresses ovarian tumorigenesis by degrading mutant p53

Ubiquitin ligase TRIM71 suppresses ovarian tumorigenesis by degrading mutant p53

E3 Ubiquitin Ligase TRIM Proteins, Cell Cycle and Mitosis

Tripartite Motif Containing 52 (TRIM52) Promotes Cell Proliferation in Hepatitis B Virus-Associated Hepatocellular Carcinoma

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