Comprehensive profiling of the TRIpartite motif family to identify pivot genes in hepatocellular carcinoma

Wu, Lingyun; Yin, Xin; Jiang, Kan; Yin, Jie; Yu, Hao; Yang, Lingling; Ma, Chiyuan; Yan, Senxiang

doi:10.1002/cam4.4552

Cited by 7 publications

(3 citation statements)

References 62 publications

(166 reference statements)

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“…Besides, bioinformatic mining revealed that TRIM28, TRIM37, TRIM45, and TRIM59 could serve as efficient biomarkers in predicting OS, PFS, DSS, and RFS based on TCGA [ 63 , 64 ]. Another study built a TRIM gene-based signature (including TRIM5, MID1(TRIM18), TRIM21, TRIM32, TRIM44, and TRIM47), which shows decent efficiency in predicting OS [HR: 6.630 (3.030–14.504), p < 0.001] in TCGA and GSE76427.…”

Section: Expression Pattern and Biological Functions Of Trim Proteins...mentioning

confidence: 99%

TRIM proteins in hepatocellular carcinoma

Pan

Huang

et al. 2022

J Biomed Sci

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The tripartite motif (TRIM) protein family is a highly conserved group of E3 ligases with 77 members known in the human, most of which consist of a RING-finger domain, one or two B-box domains, and a coiled-coil domain. Generally, TRIM proteins function as E3 ligases to facilitate specific proteasomal degradation of target proteins. In addition, E3 ligase independent functions of TRIM protein were also reported. In hepatocellular carcinoma, expressions of TRIM proteins are both regulated by genetic and epigenetic mechanisms. TRIM proteins regulate multiple biological activities and signaling cascades. And TRIM proteins influence hallmarks of HCC. This review systematically demonstrates the versatile roles of TRIM proteins in HCC and helps us better understand the molecular mechanism of the development and progression of HCC.

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Section: Expression Pattern and Biological Functions Of Trim Proteins...mentioning

confidence: 99%

TRIM proteins in hepatocellular carcinoma

Pan

Huang

et al. 2022

J Biomed Sci

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“…AML TRIM62 [23] / HCC TRIM26 [24], TRIM28, TRIM37, TRIM45, TRIM59 [25], TRIM59 [26] TRIM11 [27,28], TRIM16 [29], TRIM24 [30], TRIM25 [31], TRIM27 [32], TRIM31 [33], TRIM37 [34], TRIM50 [26], TRIM3, TRIM5, TRIM21, TRIM27, TRIM32, TRIM44, TRIM47, TRIM72 [35] RCC / TRIM27 [36], TRIM37 [37], TRIM44 [38] UCB / TRIM65 [39] GBC TRIM31 [40] PTC / TRIM14 [41] HEC / TRIM44 [42] TGCT / TRIM44 [43] NPC / TRIM11 [44] OC TRIM50 [45] TRIM59 [46] CRC TRIM1, TRIM2, TRIM6, TRIM13, TRIM26, TRIM35,TRIM55 [47], TRIM58 [48] TRIM23 [49], TRIM24 [50], TRIM27 [51], TRIM47 [47], TRIM39 [52] Pancreatic carcinoma TRIM36 [53], TRIM50 [54] TRIM11 [55], TRIM15 [56], TRIM37 [57], TRIM47 [58], TRIM59 [59] Gastric carcinoma TRIM3 [60], TRIM21 [61] TRIM14 [62], TRIM15 [63], TRIM23 [64], TRIM29 [65], TRIM32…”

Section: Cancer Type Low Expression Level High Expression Levelmentioning

confidence: 99%

TRIM family contribute to tumorigenesis, cancer development, and drug resistance

et al. 2022

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The tripartite-motif (TRIM) family represents one of the largest classes of putative single protein RING-finger E3 ubiquitin ligases. TRIM family is involved in a variety of cellular signaling transductions and biological processes. TRIM family also contributes to cancer initiation, progress, and therapy resistance, exhibiting oncogenic and tumor-suppressive functions in different human cancer types. Moreover, TRIM family members have great potential to serve as biomarkers for cancer diagnosis and prognosis. In this review, we focus on the specific mechanisms of the participation of TRIM family members in tumorigenesis, and cancer development including interacting with dysregulated signaling pathways such as JAK/STAT, PI3K/AKT, TGF-β, NF-κB, Wnt/β-catenin, and p53 hub. In addition, many studies have demonstrated that the TRIM family are related to tumor resistance; modulate the epithelial–mesenchymal transition (EMT) process, and guarantee the acquisition of cancer stem cells (CSCs) phenotype. In the end, we havediscussed the potential of TRIM family members for cancer therapeutic targets.

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“…The extent of ubiquitination is determined by the concerted actions of ubiquitinases and deubiquitinases. In this regard, tripartite motif-containing (TRIM-containing) proteins comprise a large family of RING domain-containing E3 ubiquitin ligases that regulate inflammation, immunity, fibrosis, and cancer (11)(12)(13)(14). However, only a few members of the TRIM family have been investigated in the context of metabolic disorders thus far.…”

Section: Introductionmentioning

confidence: 99%

TRIM56 protects against nonalcoholic fatty liver disease by promoting the degradation of fatty acid synthase

Xu,

Wu,

Wang

et al. 2024

Journal of Clinical Investigation

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Nonalcoholic fatty liver disease (NAFLD) encompasses a disease continuum from simple steatosis to nonalcoholic steatohepatitis (NASH). However, there are currently no approved pharmacotherapies for NAFLD, although several drugs are in advanced stages of clinical development. Because of the complex pathophysiology and heterogeneity of NAFLD, the identification of potential therapeutic targets is clinically important. Here, we demonstrated that tripartite motif 56 (TRIM56) protein abundance was markedly downregulated in the livers of individuals with NAFLD and of mice fed a high-fat diet. Hepatocyte-specific ablation of TRIM56 exacerbated the progression of NAFLD, while hepatic TRIM56 overexpression suppressed it. Integrative analyses of interactome and transcriptome profiling revealed a pivotal role of TRIM56 in lipid metabolism and identified the lipogenesis factor fatty acid synthase (FASN) as a direct binding partner of TRIM56. TRIM56 directly interacted with FASN and triggered its K48-linked ubiquitination–dependent degradation. Finally, using artificial intelligence–based virtual screening, we discovered an orally bioavailable small-molecule inhibitor of FASN (named FASstatin) that potentiates TRIM56-mediated FASN ubiquitination. Therapeutic administration of FASstatin improved NAFLD and NASH pathologies in mice with an optimal safety, tolerability, and pharmacokinetics profile. Our findings provide proof of concept that targeting the TRIM56/FASN axis in hepatocytes may offer potential therapeutic avenues to treat NAFLD.

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Comprehensive profiling of the TRIpartite motif family to identify pivot genes in hepatocellular carcinoma

Abstract: This is an open access article under the terms of the Creative Commons Attribution License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited.

Cited by 7 publications

References 62 publications

TRIM proteins in hepatocellular carcinoma

TRIM proteins in hepatocellular carcinoma

TRIM family contribute to tumorigenesis, cancer development, and drug resistance

TRIM56 protects against nonalcoholic fatty liver disease by promoting the degradation of fatty acid synthase

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