Ask about this productRelated genes to: TRIM55 Blocking Peptide
- Gene:
- TRIM55 NIH gene
- Name:
- tripartite motif containing 55
- Previous symbol:
- RNF29
- Synonyms:
- MURF-2
- Chromosome:
- 8q13.1
- Locus Type:
- gene with protein product
- Date approved:
- 2001-07-02
- Date modifiied:
- 2014-11-19
Related products to: TRIM55 Blocking Peptide
Related articles to: TRIM55 Blocking Peptide
- Head and neck squamous cell carcinoma (HNSCC) is often diagnosed at advanced stages, resulting in poor clinical outcomes. Ferroptosis resistance presents a major challenge in the treatment of HNSCC, highlighting the need to elucidate the mechanisms that enable HNSCC cells to evade ferroptosis. Here, we conducted a genome-wide CRISPR-Cas9 knockout screen and identified trafficking protein particle complex subunit 4 (TRAPPC4) as a key regulator of ferroptosis resistance in HNSCC. Across a comprehensive set of experimental models, including HNSCC cell lines, patient-derived organoids, cell-derived xenografts, patient-derived xenografts, Trappc4-conditional knockout mice, and lymph node and lung metastasis models, TRAPPC4 promoted tumor progression by inhibiting ferroptosis. Mechanistically, TRAPPC4 decreased chromatin accessibility at a distal regulatory element upstream of TRIM55, thereby limiting FOS-dependent transcription. This repression reduced TRIM55-mediated GPX4 ubiquitination and degradation, resulting in GPX4 stabilization and ferroptosis resistance. Structure-based high-throughput virtual screening identified pitavastatin calcium as a TRAPPC4-binding compound that promoted TRAPPC4 degradation. Notably, pitavastatin calcium synergized with the ferroptosis inducer RSL3 to enhance ferroptotic activity and suppress HNSCC progression. These findings delineate a TRAPPC4-FOS-TRIM55-GPX4 signaling axis that drives ferroptosis resistance and tumor progression and highlight TRAPPC4 as a promising therapeutic target for ferroptosis-based intervention in HNSCC. - Source: PubMed
Publication date: 2026/04/13
Ding ZhaoHan YanxunLiu WeiweiZhang WentaoXie ZihuiZhou PingtingJiang ShangshangLu JiLi JuanjuanLi YueJi MengyuanXue HaoTang JialuWang ZixiXia KangruiLi DapengWu JingWang YinKim Laura MinhuiNaseem Danial FLi GuojunZafereo Mark EYao ChangyuTao YeZha XiaojunLiu Yehai - Background: Heat shock protein beta 1 (HSPB1) is confirmed to be a ferroptosis-related gene and plays an important role in the progression of diabetic cardiomyopathy (DCM). However, the specific functions and underlying molecular mechanisms of HSPB1 in DCM progression remain to be revealed. Methods: Cardiomyocytes were exposed to high glucose (HG) to mimic DCM cell models. The levels of HSPB1, tripartite motif-containing 55 (TRIM55), upstream stimulating factor 1 (USF1) and fibrosis-related markers were detected using western blot. Cell viability, apoptosis, inflammation, ferroptosis and mitochondrial membrane potential depolarization were assessed by CCK8 assay, flow cytometry, ELISA, corresponding kit and JC-1 staining. The interaction between TRIM55 and HSPB1 or USF1 was confirmed by Co-IP assay, ubiquitination assay, and dual-luciferase reporter assay. Diabetic mouse models were constructed by streptozotocin to assess the role of HSPB1 in vivo. Results: Overexpression of HSPB1 suppressed HG-induced cardiomyocyte apoptosis, ferroptosis, inflammation, mitochondrial dysfunction and fibrosis. TRIM55 enhanced the protein degradation of HSPB1 through ubiquitination, and the inhibitory effect of TRIM55 knockdown on HG-induced cardiomyocyte injury could be reversed by HSPB1 silencing. USF1 bound to TRIM55 promoter to activate its transcription. USF1 knockdown inhibited HG-induced cardiomyocyte injury by mediating the TRIM55/HSPB1 axis. In animal study, HSPB1 overexpression could improve cardiac function, alleviate inflammation and fibrosis in diabetic mouse models. Conclusion: The USF1/TRIM55/HSPB1 axis proposed in this study provides a potential molecular target for the treatment of DCM. - Source: PubMed
Publication date: 2026/04/10
Huang LiuZheng ChengHe CuizhuQiu XiangWei HuiqingYan JieCui KunYang WenhuiYao LizhuoWei YulianNie XiaohongGuo Bingyan - Spinal cord injury (SCI) is a neurological disorder characterized by severe and often irreversible damage to the spinal cord, for which no effective treatments currently exist. Ubiquitination, a reversible post-translational modification, plays a critical role in regulating protein degradation and stabilization. Tripartite motif-containing 55 (TRIM55), an E3 ubiquitin ligase, belongs to the TRIM protein family. This study aimed to explore the potential mechanism of TRIM55 in SCI. - Source: PubMed
Publication date: 2025/05/26
Li Yang - - Source: PubMed
Publication date: 2024/09/23
Andreis MarcoPaolocci Nazareno - Tripartite motif-containing 55 (Trim55) is mainly expressed in myocardium and skeletal muscle, which plays an important role in promoting the embryonic development of the mouse heart. We investigated the role of Trim55 in myocardial infarction and the associated molecular mechanisms. We studied both gain and loss of function in vivo and in vitro. The results showed that Trim55 knockout improved cardiac function and apoptosis after myocardial infarction, and overexpression aggravated cardiac function damage. The mechanism is that Trim55 interacts with nuclear factor, erythroid derived 2 (Nrf2) to accelerate its degradation and inhibit the expression of heme oxygenase 1, thereby promoting cardiomyocyte apoptosis. - Source: PubMed
Publication date: 2024/08/14
Bu YuxinLiu YanxiaLiu MeiliYan ChenghuiWang JingWu HanlinSong HaixuZhang DaliXu KaiLiu DanHan Yaling