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Articles de revues sur le sujet « TRIM18 »

Auteur : Grafiati

Publié le 1 avril 2023

Mis à jour le 31 juillet 2025

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1

Kimsa, Malgorzata W., B. Strzalka-Mrozik, M. C. Kimsa, et al. "Differential Expression of Tripartite Motif-Containing Family in Normal Human Dermal Fibroblasts in Response to Porcine Endogenous Retrovirus Infection." Folia Biologica 60, no. 3 (2014): 144–51. http://dx.doi.org/10.14712/fb2014060030144.

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Antiretroviral restriction factors may play an essential role in the safety of xenotransplantation. Therefore, the present study focused on investigation of the changes in the tripartite motif-containing family (TRIM) gene expression in normal human dermal fibroblasts with and without lipopolysaccharide stimulation in response to porcine endogenous retrovirus infection. Analysis of the expression profile of TRIMs was performed using oligonucleotide microarrays and QRT-PCR. Nine (TRIM1, TRIM2, TRIM5, TRIM14, TRIM16, TRIM18, TRIM22, TRIM27 and TRIM31) statistically significantly differentially e

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Panhwar, S. N., C. Huang, Q. Luo, et al. "OVERVIEW OF CLASS-I TRIPARTITE MOTIF (TRIM) PROTEINS SPECIFICALLY TRIM67." Pakistan Journal of Agriculture, Agricultural Engineering and Veterinary Sciences 40, no. 2 (2024): 108–19. https://doi.org/10.47432/2024.40.2.8.

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The TRIM family is a group of genes expressed during embryogenesis. This review emphasized data on Class-I TRIM genes, including TRIM1, TRIM9, TRIM36, TRIM46, TRIM67, TRIM18, and TRIM76. This article will discuss the structure and function of these genes and their roles in various physiological processes such as embryonic development, and immune regulation. Class-I TRIM proteins develop as E3 ubiquitin ligases and work with E2 ubiquitin-conjugating enzymes. TRIM9 is expressed in the stem cells of mice and linked to various neuronal functions and neurological diseases. TRIM18 is found in microt

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Yap, Melvyn W., Mark P. Dodding, and Jonathan P. Stoye. "Trim-Cyclophilin A Fusion Proteins Can Restrict Human Immunodeficiency Virus Type 1 Infection at Two Distinct Phases in the Viral Life Cycle." Journal of Virology 80, no. 8 (2006): 4061–67. http://dx.doi.org/10.1128/jvi.80.8.4061-4067.2006.

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ABSTRACT The Trim5α protein from several primates restricts retroviruses in a capsid (CA)-dependent manner. In owl monkeys, the B30.2 domain of Trim5 has been replaced by cyclophilin A (CypA) following a retrotransposition. Restriction of human immunodeficiency virus type 1 (HIV-1) by the resulting Trim5-CypA fusion protein depends on CA binding to CypA, suggesting both that the B30.2 domain might be involved in CA binding and that the tripartite RING motif, B-BOX, and coiled coil (RBCC) motif domain can function independently of the B30.2 domain in restriction. To investigate the potential of

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Tran, Pham-Tue-Hung, Mir Himayet Kabir, Naveed Asghar, et al. "Identification of TRIM21 and TRIM14 as Antiviral Factors Against Langat and Zika Viruses." Viruses 17, no. 5 (2025): 644. https://doi.org/10.3390/v17050644.

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Flaviviruses are usually transmitted to humans via mosquito or tick bites, whose infections may lead to severe diseases and fatality. During intracellular infection, they remodel the endoplasmic reticulum (ER) membrane to generate compartments scaffolding the replication complex (RC) where replication of the viral genome takes place. In this study, we purified the ER membrane fraction of virus infected cells to identify the proteins that were enriched during flavivirus infection. We found that tripartite motif-containing proteins (TRIMs) including TRIM38, TRIM21, and TRIM14 were significantly

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De La Cruz-Herrera, Carlos F., Michael H. Tatham, Umama Z. Siddiqi, et al. "Changes in SUMO-modified proteins in Epstein-Barr virus infection identifies reciprocal regulation of TRIM24/28/33 complexes and the lytic switch BZLF1." PLOS Pathogens 19, no. 7 (2023): e1011477. http://dx.doi.org/10.1371/journal.ppat.1011477.

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SUMO modifications regulate the function of many proteins and are important in controlling herpesvirus infections. We performed a site-specific proteomic analysis of SUMO1- and SUMO2-modified proteins in Epstein-Barr virus (EBV) latent and lytic infection to identify proteins that change in SUMO modification status in response to EBV reactivation. Major changes were identified in all three components of the TRIM24/TRIM28/TRIM33 complex, with TRIM24 being rapidly degraded and TRIM33 being phosphorylated and SUMOylated in response to EBV lytic infection. Further experiments revealed TRIM24 and T

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Sebastian, Sarah, Christian Grütter, Caterina Strambio de Castillia та ін. "An Invariant Surface Patch on the TRIM5α PRYSPRY Domain Is Required for Retroviral Restriction but Dispensable for Capsid Binding". Journal of Virology 83, № 7 (2009): 3365–73. http://dx.doi.org/10.1128/jvi.00432-08.

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ABSTRACT TRIM5α is a retrovirus restriction factor in the host cell cytoplasm that blocks infection before provirus establishment. Restriction activity requires capsid (CA)-specific recognition by the PRYSPRY domain of TRIM5α. To better understand the restriction mechanism, nine charge-cluster-to-triple-alanine mutants in the TRIM5α PRYSPRY domain were assessed for CA-specific restriction activity. Five mutants distributed along the TRIM5α PRYSPRY primary sequence disrupted restriction activity against N-tropic murine leukemia virus and equine infectious anemia virus. Modeling of the TRIM5α PR

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Margalit, Liad, Carmit Strauss, Ayellet Tal, and Sharon Schlesinger. "Trim24 and Trim33 Play a Role in Epigenetic Silencing of Retroviruses in Embryonic Stem Cells." Viruses 12, no. 9 (2020): 1015. http://dx.doi.org/10.3390/v12091015.

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Embryonic stem cells (ESC) have the ability to epigenetically silence endogenous and exogenous retroviral sequences. Trim28 plays an important role in establishing this silencing, but less is known about the role other Trim proteins play. The Tif1 family is a sub-group of the Trim family, which possess histone binding ability in addition to the distinctive RING domain. Here, we have examined the interaction between three Tif1 family members, namely Trim24, Trim28 and Trim33, and their function in retroviral silencing. We identify a complex formed in ESC, comprised of these three proteins. We f

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Toka, Felix N., Kiera Dunaway, Matylda Mielcarska, Felicia Smaltz, and Magdalena Bossowska-Nowicka. "Expression pattern of TRIM genes in bovine macrophages stimulated with PAMPs." Journal of Immunology 198, no. 1_Supplement (2017): 129.7. http://dx.doi.org/10.4049/jimmunol.198.supp.129.7.

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Abstract In mammals innate immune mechanisms form the first line of defence against invading pathogens. Detection of viruses early in infection relies on intracellular receptors that sense microbial molecular patterns, subsequently leading to gene transcription that eventually produces IFN type I and II. Type I and II IFNs act to prevent replication of viruses. Tripartite Motif-containing (TRIM) proteins belong to a superfamily of RING-domain E3 ubiquitin ligases. They represent a novel class of antiviral molecules involved in innate immunity. These enzymes function in a wide variety of import

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Rybakowska, Paulina, Nina Wolska, Arkadiusz Klopocki, et al. "Multiple TRIM proteins are targets of autoimmune response in lupus and Sjogren's syndrome. (HUM7P.308)." Journal of Immunology 192, no. 1_Supplement (2014): 184.17. http://dx.doi.org/10.4049/jimmunol.192.supp.184.17.

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Abstract TRIM21 belongs to the large family of tripartite motif containing proteins, and is often targeted by autoantibodies in lupus and Sjogren’s syndrome. Considering the significant protein domain homology between different TRIM proteins, we hypothesized that additional TRIM proteins are targets of autoimmunity. Based on the literature, in this study we investigated autoantibody responses to TRIM38. While 9% of lupus patients (n=149) had anti-TRIM38 antibodies, the incidence in Sjogren’s syndrome patients (n=150) was 12%, and in controls (n=50) it was 4%. With respect to TRIM21, the incide

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Agarwal, Neeraj, Sebastien Rinaldetti, Bassem B. Cheikh, et al. "TRIM28 is a transcriptional activator of the mutant TERT promoter in human bladder cancer." Proceedings of the National Academy of Sciences 118, no. 38 (2021): e2102423118. http://dx.doi.org/10.1073/pnas.2102423118.

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Bladder cancer (BC) has a 70% telomerase reverse transcriptase (TERT or hTERT in humans) promoter mutation prevalence, commonly at −124 base pairs, and this is associated with increased hTERT expression and poor patient prognosis. We inserted a green fluorescent protein (GFP) tag in the mutant hTERT promoter allele to create BC cells expressing an hTERT-GFP fusion protein. These cells were used in a fluorescence-activated cell sorting–based pooled CRISPR-Cas9 Kinome knockout genetic screen to identify tripartite motif containing 28 (TRIM28) and TRIM24 as regulators of hTERT expression. TRIM28

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Stevens, Rebecca V., Diego Esposito, and Katrin Rittinger. "Characterisation of class VI TRIM RING domains: linking RING activity to C-terminal domain identity." Life Science Alliance 2, no. 3 (2019): e201900295. http://dx.doi.org/10.26508/lsa.201900295.

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TRIM E3 ubiquitin ligases regulate multiple cellular processes, and their dysfunction is linked to disease. They are characterised by a conserved N-terminal tripartite motif comprising a RING, B-box domains, and a coiled-coil region, with C-terminal domains often mediating substrate recruitment. TRIM proteins are grouped into 11 classes based on C-terminal domain identity. Class VI TRIMs, TRIM24, TRIM33, and TRIM28, have been described as transcriptional regulators, a function linked to their C-terminal plant homeodomain and bromodomain, and independent of their ubiquitination activity. It is

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Zanchetta, Melania E., Luisa M. R. Napolitano, Danilo Maddalo, and Germana Meroni. "The E3 ubiquitin ligase MID1/TRIM18 promotes atypical ubiquitination of the BRCA2-associated factor 35, BRAF35." Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 1864, no. 10 (2017): 1844–54. http://dx.doi.org/10.1016/j.bbamcr.2017.07.014.

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McAvera, Roisin M., and Lisa J. Crawford. "TIF1 Proteins in Genome Stability and Cancer." Cancers 12, no. 8 (2020): 2094. http://dx.doi.org/10.3390/cancers12082094.

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Genomic instability is a hallmark of cancer cells which results in excessive DNA damage. To counteract this, cells have evolved a tightly regulated DNA damage response (DDR) to rapidly sense DNA damage and promote its repair whilst halting cell cycle progression. The DDR functions predominantly within the context of chromatin and requires the action of chromatin-binding proteins to coordinate the appropriate response. TRIM24, TRIM28, TRIM33 and TRIM66 make up the transcriptional intermediary factor 1 (TIF1) family of chromatin-binding proteins, a subfamily of the large tripartite motif (TRIM)

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Herquel, B., K. Ouararhni, K. Khetchoumian, et al. "Transcription cofactors TRIM24, TRIM28, and TRIM33 associate to form regulatory complexes that suppress murine hepatocellular carcinoma." Proceedings of the National Academy of Sciences 108, no. 20 (2011): 8212–17. http://dx.doi.org/10.1073/pnas.1101544108.

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Lascano, Josefina, Pradeep D. Uchil, Walther Mothes, and Jeremy Luban. "TRIM5 Retroviral Restriction Activity Correlates with the Ability To Induce Innate Immune Signaling." Journal of Virology 90, no. 1 (2015): 308–16. http://dx.doi.org/10.1128/jvi.02496-15.

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ABSTRACTHost restriction factor TRIM5 inhibits retroviral transduction in a species-specific manner by binding to and destabilizing the retroviral capsid lattice before reverse transcription is completed. However, the restriction mechanism may not be that simple since TRIM5 E3 ubiquitin ligase activity, the proteasome, autophagy, and TAK1-dependent AP-1 signaling have been suggested to contribute to restriction. Here, we show that, among a panel of seven primate and Carnivora TRIM5 orthologues, each of which has potential for potent retroviral restriction activity, all activated AP-1 signaling

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Kimura, Tomonori, Ashish Jain, Seong Won Choi, et al. "TRIM-mediated precision autophagy targets cytoplasmic regulators of innate immunity." Journal of Cell Biology 210, no. 6 (2015): 973–89. http://dx.doi.org/10.1083/jcb.201503023.

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The present paradigms of selective autophagy in mammalian cells cannot fully explain the specificity and selectivity of autophagic degradation. In this paper, we report that a subset of tripartite motif (TRIM) proteins act as specialized receptors for highly specific autophagy (precision autophagy) of key components of the inflammasome and type I interferon response systems. TRIM20 targets the inflammasome components, including NLRP3, NLRP1, and pro–caspase 1, for autophagic degradation, whereas TRIM21 targets IRF3. TRIM20 and TRIM21 directly bind their respective cargo and recruit autophagic

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Palomba, Tommaso, Giusy Tassone, Carmine Vacca, et al. "Exploiting ELIOT for Scaffold-Repurposing Opportunities: TRIM33 a Possible Novel E3 Ligase to Expand the Toolbox for PROTAC Design." International Journal of Molecular Sciences 23, no. 22 (2022): 14218. http://dx.doi.org/10.3390/ijms232214218.

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The field of targeted protein degradation, through the control of the ubiquitin–proteasome system (UPS), is progressing considerably; to exploit this new therapeutic modality, the proteolysis targeting chimera (PROTAC) technology was born. The opportunity to use PROTACs engaging of new E3 ligases that can hijack and control the UPS system could greatly extend the applicability of degrading molecules. To this end, here we show a potential application of the ELIOT (E3 LIgase pocketOme navigaTor) platform, previously published by this group, for a scaffold-repurposing strategy to identify new lig

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Kong, EunBin, and Norbert Polacek. "TRIM21 modulates stability of pro-survival non-coding RNA vtRNA1–1 in human hepatocellular carcinoma cells." PLOS Genetics 21, no. 3 (2025): e1011614. https://doi.org/10.1371/journal.pgen.1011614.

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Recent studies expanded our knowledge of diverse pro-survival functions of short non-coding vault RNAs. One of the human vault RNA paralogs, vtRNA1-1, modulates several intracellular processes, including proliferation, apoptosis, autophagy, and drug resistance in various types of human cancer cells. However, protein interaction partners and mechanisms by which vtRNA1-1 levels are controlled within the cells remained elusive. Here, we describe a regulatory process for vtRNA1-1 stabilization mediated by the newly identified interacting proteins, TRIM21 and TRIM25, in human hepatocellular carcino

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Reddi, Tejaswini S., Philipp E. Merkl, So-Yon Lim, Norman L. Letvin, and David M. Knipe. "Tripartite Motif 22 (TRIM22) protein restricts herpes simplex virus 1 by epigenetic silencing of viral immediate-early genes." PLOS Pathogens 17, no. 2 (2021): e1009281. http://dx.doi.org/10.1371/journal.ppat.1009281.

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Intrinsic resistance is a crucial line of defense against virus infections, and members of the Tripartite Ring Interaction Motif (TRIM) family of proteins are major players in this system, such as cytoplasmic TRIM5α or nuclear promyelocytic leukemia (PML/TRIM19) protein. Previous reports on the antiviral function of another TRIM protein, TRIM22, emphasized its innate immune role as a Type I and Type II interferon-stimulated gene against RNA viruses. This study shows that TRIM22 has an additional intrinsic role against DNA viruses. Here, we report that TRIM22 is a novel restriction factor of HS

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Lionnard, Loïc, Pauline Duc, Margs S. Brennan, et al. "TRIM17 and TRIM28 antagonistically regulate the ubiquitination and anti-apoptotic activity of BCL2A1." Cell Death & Differentiation 26, no. 5 (2018): 902–17. http://dx.doi.org/10.1038/s41418-018-0169-5.

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Li, Xing, Yuan Li, Matthew Stremlau та ін. "Functional Replacement of the RING, B-Box 2, and Coiled-Coil Domains of Tripartite Motif 5α (TRIM5α) by Heterologous TRIM Domains". Journal of Virology 80, № 13 (2006): 6198–206. http://dx.doi.org/10.1128/jvi.00283-06.

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ABSTRACT Tripartite motif 5α (TRIM5α) restricts some retroviruses, including human immunodeficiency virus type 1 (HIV-1), from infecting the cells of particular species. TRIM5α is a member of the TRIM family of proteins, which contain RING, B-box, coiled-coil (CC), and, in some cases, B30.2(SPRY) domains. Here we investigated the abilities of domains from TRIM proteins (TRIM6, TRIM34, and TRIM21) that do not restrict HIV-1 infection to substitute for the domains of rhesus monkey TRIM5α (TRIM5αrh). The RING, B-box 2, and CC domains of the paralogous TRIM6 and TRIM34 proteins functionally replac

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Luo, Jing, Qi Min, Xueliang Sun, et al. "Comparative Whole-Genome Analysis of Production Traits and Genetic Structure in Baiyu and Chuanzhong Black Goats." Animals 14, no. 24 (2024): 3616. https://doi.org/10.3390/ani14243616.

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Natural selection and artificial breeding are crucial methods for developing new animal groups. The Baiyu black goats and Chuanzhong black goats are indigenous goat breeds from distinct ecological regions in Sichuan Province, with dramatically different growth and reproductivity. This study aimed to systematically elucidate the differences in production performance and genetic traits between Baiyu black goats and Chuanzhong black goats. We quantified growth and reproductive attributes for both breeds. Furthermore, we conducted a comprehensive analysis of genetic diversity, population structure

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Roshanazadeh, Mohammadreza, mojtaba rashidi, Arash sanaei, Hossein azizi dariuni, amirnader emami razavi, and Maryam Adelipour. "TRIM14 and TRIM29 as potential tumor markers for breast cancer diagnosis." Journal of Breast Disease 16, no. 4 (2023): 4–20. http://dx.doi.org/10.61186/ijbd.16.4.4.

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Lin, Jia-Yi, Wei-Wei Zhang, Qing-Jie Li, et al. "Abstract 1113: USP18 impairs the sensitivity of radiotherapy for nasopharyngeal carcinoma by promoting the ubiquitination and nuclear translocation of TRIM29." Cancer Research 84, no. 6_Supplement (2024): 1113. http://dx.doi.org/10.1158/1538-7445.am2024-1113.

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Abstract Radiotherapy is the main and preferred treatment for nasopharyngeal carcinoma (NPC), owing to its high sensitivity to radiation. However, there are ~20% patients suffering from tumor recurrence. Accumulating evidences show that protein ubiquitination plays a vital role in radiation caused DNA damage response. Here, we identified that the deubiquitinase USP18 is highly expressed in NPC tissues, and inversely associated with radiosensitivity of NPC cells. USP18 interacts with TRIM29 and promotes its K27-linked ubiquitination independent of its deubiquitinase activity. Further investigat

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Jacques, David, Cy Jeffries, Matthew Caines, et al. "TRIM protein domain topology and implications for antiviral immunity." Acta Crystallographica Section A Foundations and Advances 70, a1 (2014): C243. http://dx.doi.org/10.1107/s2053273314097563.

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The tripartite motif (TRIM) proteins are a large family of >100 members, several of which have important roles in antiviral immunity and innate immune signaling. TRIM5α associates with incoming HIV-1 capsids, interfering with controlled disassembly and targeting them for degradation by the proteasome. TRIM21 is a cytosolic antibody receptor, which also targets incoming viral capsids for proteasomal degradation. TRIM25 is also involved in innate immunity, being essential for the ubiquitination of RIG-I. Recent positive selection analysis has predicted another 10 TRIM proteins with antiviral

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Lassot, Iréna, Stéphan Mora, Suzanne Lesage та ін. "The E3 Ubiquitin Ligases TRIM17 and TRIM41 Modulate α-Synuclein Expression by Regulating ZSCAN21". Cell Reports 25, № 9 (2018): 2484–96. http://dx.doi.org/10.1016/j.celrep.2018.11.002.

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Azuma, Kotaro, and Satoshi Inoue. "Efp/TRIM25 and Its Related Protein, TRIM47, in Hormone-Dependent Cancers." Cells 11, no. 15 (2022): 2464. http://dx.doi.org/10.3390/cells11152464.

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Increasing attention has been paid to the biological roles of tripartite motif-containing (TRIM) family proteins, which typically function as E3 ubiquitin ligases. Estrogen-responsive finger protein (Efp), a member of the TRIM family proteins, also known as TRIM25, was originally identified as a protein induced by estrogen and plays critical roles in promoting endocrine-related cancers, including breast cancer, endometrial cancer, and prostate cancer. The pathophysiological importance of Efp made us interested in the roles of other TRIM family proteins that share a similar structure with Efp.

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Chang, Yao-Jen, Steven Lin, Zhi-Fu Kang, et al. "Acetylation-Mimic Mutation of TRIM28-Lys304 to Gln Attenuates the Interaction with KRAB-Zinc-Finger Proteins and Affects Gene Expression in Leukemic K562 Cells." International Journal of Molecular Sciences 24, no. 12 (2023): 9830. http://dx.doi.org/10.3390/ijms24129830.

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TRIM28/KAP1/TIF1β is a crucial epigenetic modifier. Genetic ablation of trim28 is embryonic lethal, although RNAi-mediated knockdown in somatic cells yields viable cells. Reduction in TRIM28 abundance at the cellular or organismal level results in polyphenism. Posttranslational modifications such as phosphorylation and sumoylation have been shown to regulate TRIM28 activity. Moreover, several lysine residues of TRIM28 are subject to acetylation, but how acetylation of TRIM28 affects its functions remains poorly understood. Here, we report that, compared with wild-type TRIM28, the acetylation-m

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Zhang, Wen, Zhengquan Cai, Mingzhu Kong, et al. "Prognostic significance of TRIM28 expression in patients with breast carcinoma." Open Medicine 16, no. 1 (2021): 472–80. http://dx.doi.org/10.1515/med-2021-0263.

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Abstract Background Tripartite motif 28 (TRIM28) plays a role in multiple biological functions. The expression and function of TRIM28 in breast carcinoma (BC) remain unclear. The aim of this study was to explore potential association of TRIM28 with tumor features and survival. Materials and methods Specimens were collected from BC and adjacent normal tissues. Quantitative reverse transcription PCR (RT-qPCR) and immunohistochemistry (IHC) were performed to detect TRIM28 expression. The correlation of TRIM28 with clinicopathological features was evaluated by Chi-square test. The relationship bet

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Xu, Weiqi, Lihong Zhuang, Hongxu Zhu, Anrong Mao, Jiamin Zhou та Lu Wang. "TRIM14 Overexpression Induces Chemoresistance and Malignant Behaviors of Hepatocellular Carcinoma Cells by Activating the STAT3/HIF-1α Pathway". International Journal of Molecular Sciences 24, № 16 (2023): 12589. http://dx.doi.org/10.3390/ijms241612589.

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Members of the tripartite motif (TRIM)-containing protein family have been found to be involved in the progression of hepatocellular carcinoma (HCC). TRIM14 exerts a promotive impact on several cancers. This study aimed to explore the function and mechanism of TRIM14 in HCC. TRIM14 expression in HCC tissues and HCC cell lines was detected. The overexpression or knockdown model of TRIM14 was established in HCC cell lines. Cell Counting Kit-8 (CCK-8) assay, flow cytometry, Transwell assay, RT-PCR, Western blot, and immunofluorescence were performed to verify the influence of TRIM14 on cell proli

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He, Jing, Yulian Kuang, Kui Xu, et al. "TRIM38 Inhibits Zika Virus by Upregulating RIG-I/MDA5 Pathway and Promoting Ubiquitin-Mediated Degradation of Viral NS3 Protein." Viruses 17, no. 2 (2025): 199. https://doi.org/10.3390/v17020199.

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Members of the tripartite motif (TRIM)-containing protein family play crucial roles in regulating immune system responses. The TRIM38 protein regulates host innate immunity and directly degrades some viral proteins through its E3 ubiquitin ligase activity. This study demonstrated that Zika virus (ZIKV) infection can promote the expression of TRIM38 in human glioma cells (U251). TRIM38 overexpression restricted ZIKV replication in U251 cells, while TRIM38 knockout enhanced ZIKV replication. TRIM38 overexpression upregulated the RIG-I/MDA5 pathway and promoted the level of IFN-β early during vir

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Terui, Yasuhito, Ryoko Kuniyoshi, Yuji Mishima, Yuko Mishima, and Kiyohiko Hatake. "Ubiquitin E3 Ligase, Tripartite Motif Protein 68 (TRIM68) Inhibits TCP-1 b Function by Proteasome-Mediated Degradation and May Overcome Imatinib-Resistance." Blood 114, no. 22 (2009): 3789. http://dx.doi.org/10.1182/blood.v114.22.3789.3789.

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Abstract Abstract 3789 Poster Board III-725 [Background] Imatinib mesylate is effective therapy against Philadelphia chromosome-positive leukemia, but the resistance develops in all phases of the disease. The identification of new proteins induced by imatinib may lead to find the novel potent molecular targets in imatinib-resistant CML. [Methods] K562 cells were treated with or without 1 mM imatinib for 24 hours, and then differential display between them was performed. TRIM68 expression was examined by RT-PCR, and in vivo ubiquitination or sumoylation assay was performed by transfection exper

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Lu, Hsin-Pin, Chieh-Ju Lin, Wen-Ching Chen, et al. "TRIM28 Regulates Dlk1 Expression in Adipogenesis." International Journal of Molecular Sciences 21, no. 19 (2020): 7245. http://dx.doi.org/10.3390/ijms21197245.

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The tripartite motif-containing protein 28 (TRIM28) is a transcription corepressor, interacting with histone deacetylase and methyltransferase complexes. TRIM28 is a crucial regulator in development and differentiation. We would like to investigate its function and regulation in adipogenesis. Knockdown of Trim28 by transducing lentivirus-carrying shRNAs impairs the differentiation of 3T3-L1 preadipocytes, demonstrated by morphological observation and gene expression analysis. To understand the molecular mechanism of Trim28-mediated adipogenesis, the RNA-seq was performed to find out the possib

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Wang, Zhaofeng, Xiaobo Xu, Wenxiao Tang, Youcai Zhu, Jichao Hu, and Xingen Zhang. "Tripartite Motif Containing 11 Interacts with DUSP6 to Promote the Growth of Human Osteosarcoma Cells through Regulating ERK1/2 Pathway." BioMed Research International 2019 (December 26, 2019): 1–10. http://dx.doi.org/10.1155/2019/9612125.

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Tripartite Motif Containing 11 (TRIM11), an E3 ubiquitin ligase, is identified as a carcinogen causing certain human cancers. However, the specific role of TRIM11 is still uncovered in human osteosarcoma (OS) cells. To explore the role of TRIM11 in OS cells, TRIM11 was induced by silencing and overexpression in OS cells using RNA interference (RNAi) and lentiviral vector, respectively. qRT-PCR and western blot were used to examine the transcription and translation levels of the target gene. Cell count kit-8 (CCK-8) assays were established to analyze cell proliferation. Cell apoptosis ratio was

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Zhang, Jiawei, Dijia Xin, Yili Fan, Luyao Wang, Boxiao Chen, and Yang Xu. "TRIM28 Regulates DHCR7-Mediated Cholesterol Biosynthesis to Promote Survival in B Cell Lymphoma." Blood 142, Supplement 1 (2023): 5729. http://dx.doi.org/10.1182/blood-2023-174433.

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Background: TRIM28, a member of the tripartite motif-containing (TRIM) protein family, is a critical regulator of gene expression, DNA damage response and protein degradation, but little is known about its role in lipid metabolism. Dysregulation of cholesterol metabolism has been implicated in the pathogenesis of diffuse large B-cell lymphoma (DLBCL). However, the role of TRIM28 in lymphomagenesis and its clinical relevance remain unclear. Methods: We searched public databases to characterize the gene expression pattern, clinical parameters, and survival data of TRIM28 in B-cell lymphoma, and

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Zhou, Ling, Heng Wang, Min Zhong та ін. "The E3 Ubiquitin Ligase TRIM11 Facilitates Gastric Cancer Progression by Activating the Wnt/β-Catenin Pathway via Destabilizing Axin1 Protein". Journal of Oncology 2022 (21 лютого 2022): 1–14. http://dx.doi.org/10.1155/2022/8264059.

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Background. Aberrant expression of tripartite motif 11 (TRIM11) and the Wnt/β-catenin pathway are essential for facilitating tumorigenesis and progression in multiple types of cancer. Aim. To investigate the molecular changes linking the dysregulation of TRIM11 and Wnt/β-catenin pathway activation in gastric cancer (GC) progression. Methods. The expression levels of TRIM11 were detected in GC tissues and cells by immunohistochemistry and western blotting. The role of TRIM11 in the growth, proliferation, and invasion of gastric cancer cells was observed by a series of cell functional experiment

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Wynne, Claire, Rowan Higgs, Christine Biron, and Caroline Jefferies. "The role of TRIM68 in Toll-like receptor and RIG-I-like receptor induced interferon production (72.5)." Journal of Immunology 188, no. 1_Supplement (2012): 72.5. http://dx.doi.org/10.4049/jimmunol.188.supp.72.5.

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Abstract Innate immune receptors such as Toll-like receptors (TLR) and RIG-I-like receptors (RLR) play key roles in viral recognition and interferon (IFN) production. Systemic Lupus Erythematosus (SLE) patients commonly present with an over production of type 1 IFNs which contribute to disease pathogenesis so understanding how to dampen down this response is of huge importance. The focus of this project is on the E3 ubiquitin ligase TRIM68, a known autoantigen in SLE. Results show TRIM68 to be a novel negative regulator of type 1 IFN production in both TLR- and RLR-dependent pathways. Proteomi

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Fang, Teng, Lanting Liu, Hao Sun, et al. "TRIM28 Serves As a Key Regulator of Protein Homeostasis and Mediates Proteasome Inhibitor Resistance in Multiple Myeloma." Blood 144, Supplement 1 (2024): 4668. https://doi.org/10.1182/blood-2024-204159.

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Introduction: The maintenance of intracellular protein homeostasis is a critical biological process necessary for the survival of multiple myeloma (MM) cells. Tripartite motif (TRIM) proteins, a subfamily of the RING-type E3 ubiquitin ligase family, are integral to protein quality control. In this study, we examined the role of TRIM28, a member of the TRIM family, as a regulator of protein homeostasis in MM. Methods: Bioinformatic analysis was utilized to elucidate the association between TRIM28 and genes involved in the proteasome and autophagy mediated protein degradation pathway. ShRNA knoc

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Liu, Jinjin, Jun Rao, Xuming Lou, Jian Zhai, Zhenhua Ni, and Xiongbiao Wang. "Upregulated TRIM11 Exerts its Oncogenic Effects in Hepatocellular Carcinoma Through Inhibition of P53." Cellular Physiology and Biochemistry 44, no. 1 (2017): 255–66. http://dx.doi.org/10.1159/000484678.

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Background/Aims: The tripartite motif containing (TRIM) family plays crucial roles in tumor development and progression. However, little is known about the function and mechanism of TRIM11 in hepatocellular carcinoma (HCC). Methods: The expression levels of TRIM11 were examined by real-time PCR, Western blot and Immunohistochemical (IHC) staining. TRIM11 knockdown cells were produced by lentivirus infection, and functional assays, such as MTT, colony formation assay, migration and invasion assays and a xenograft tumor model were used to investigate the role of TRIM11 in HCC. We also determined

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Shang, Rongxin, Jiakuan Chen, Yang Gao, Jijun Chen, and Guoliang Han. "TRIM58 Interacts with ZEB1 to Suppress NSCLC Tumor Malignancy by Promoting ZEB1 Protein Degradation via UPP." Disease Markers 2023 (January 5, 2023): 1–13. http://dx.doi.org/10.1155/2023/5899662.

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Background. Currently, how to successfully control refractory and metastatic diseases remains a fundamental goal for clinicians to improve therapeutic effects for patients with non-small cell lung cancer (NSCLC). Several studies have discovered that TRIM58, a member of tripartite motif protein family, shows antitumor effect in multiple types of cancer. In this study, we aimed to further clarify the molecular regulatory network of TRIM58 and corresponding targets for NSCLC patients. Methods. TRIM58 expression in clinical tumor tissue samples and cancer cell lines was examined. Functional experi

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Ma, Xin, Sheng Zhang, Meiling Zhang, et al. "TRIM28 down-regulation on methylation imprints in bovine preimplantation embryos." Zygote 26, no. 6 (2018): 449–56. http://dx.doi.org/10.1017/s0967199418000424.

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SummaryTRIM28/KAP1/TIF1β was identified as a universal transcriptional co-repressor and is critical for regulating post-fertilization methylation reprogramming in preimplantation embryos. In this study, three siRNAs (si647, si742, and si1153) were designed to target the TRIM28 mRNA sequence. After transfection of the mixture of the three siRNA (siMix) into bovine fibroblast cells, the most effective one for TRIM28 knockdown was selected. By injecting RNAi directed against TRIM28 mRNA, we found that TRIM28 knockdown in oocytes had the most effect on the H19 gene, in which differentially methyla

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Li, Lin, Qi Li, Zhengrong Zou, Zoufang Huang та Yijian Chen. "TRIM10 Is Downregulated in Acute Myeloid Leukemia and Plays a Tumor Suppressive Role via Regulating NF-κB Pathway". Cancers 15, № 2 (2023): 417. http://dx.doi.org/10.3390/cancers15020417.

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Background: Accumulating evidence suggests that members of the tripartite motif (TRIMs) family play a crucial role in the development and progression of hematological malignancy. Here, we explored the expression and potential role of TRIM10 in acute myeloid leukemia (AML). Methods: The expression levels of TRIM10 were investigated in AML patients and cell lines by RNA-seq, qRT-PCR and Western blotting analysis. Lentiviral infection was used to regulate the level of TRIM10 in AML cells. The effects of TRIM10 on apoptosis, drug sensitivity and proliferation of AML cells were evaluated by flow cy

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Tan, Hongwei, Jin Qi, Guanghua Chu, and Zhaoyang Liu. "Tripartite Motif 16 Inhibits the Migration and Invasion in Ovarian Cancer Cells." Oncology Research Featuring Preclinical and Clinical Cancer Therapeutics 25, no. 4 (2017): 551–58. http://dx.doi.org/10.3727/096504016x14758370595285.

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Tripartite motif 16 (TRIM16), a member of the RING B-box coiled-coil (RBCC)/tripartite motif (TRIM) protein family, has been shown to play a role in tumor development and progression. However, the role of TRIM16 in ovarian cancer has never been revealed. Thus, in this study, we investigated the roles and mechanisms of TRIM16 in ovarian cancer. Our results demonstrated that TRIM16 expression was low in ovarian cancer cell lines. In addition, overexpression of TRIM16 significantly inhibited the migration and invasion in vitro, as well as suppressed the epithelial‐mesenchymal transition (EMT) phe

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Jin, Xin, Bin Zhang, Hao Zhang, and Haixin Yu. "Smoking-associated upregulation of CBX3 suppresses ARHGAP24 expression to activate Rac1 signaling and promote tumor progression in lung adenocarcinoma." Oncogene 41, no. 4 (2021): 538–49. http://dx.doi.org/10.1038/s41388-021-02114-8.

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AbstractAlthough tobacco smoking is a risk factor for lung adenocarcinoma (LUAD), the mechanisms by which tobacco smoking induces LUAD development remain elusive. Histone methylation levels in human bronchial epithelial cells have been reported to increase after exposure to cigarettes. In this study, we explored the mechanisms regulating histone methylation in LUAD in response to smoking. We found that the histone H3K9 methylation reader CBX3 was upregulated in current smokers with LUAD, and that CBX3 overexpression promoted LUAD progression. Functional enrichment analyses revealed that CBX3 r

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Chiang, De Chen, and Beow Keat Yap. "TRIM25, TRIM28 and TRIM59 and Their Protein Partners in Cancer Signaling Crosstalk: Potential Novel Therapeutic Targets for Cancer." Current Issues in Molecular Biology 46, no. 10 (2024): 10745–61. http://dx.doi.org/10.3390/cimb46100638.

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Aberrant expression of TRIM proteins has been correlated with poor prognosis and metastasis in many cancers, with many TRIM proteins acting as key oncogenic factors. TRIM proteins are actively involved in many cancer signaling pathways, such as p53, Akt, NF-κB, MAPK, TGFβ, JAK/STAT, AMPK and Wnt/β-catenin. Therefore, this review attempts to summarize how three of the most studied TRIMs in recent years (i.e., TRIM25, TRIM28 and TRIM59) are involved directly and indirectly in the crosstalk between the signaling pathways. A brief overview of the key signaling pathways involved and their general c

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Di, Kaijun, Bhaskar C. Das, Daniela Alexandru Abrams, and Daniela A. Bota. "Abstract 5959: Targeting TRIM11 is a potential therapeutic strategy for malignant gliomas." Cancer Research 84, no. 6_Supplement (2024): 5959. http://dx.doi.org/10.1158/1538-7445.am2024-5959.

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Abstract Background: TRIM11 (tripartite motif-containing protein 11) belongs to the TRIM/RBCC (the RING B-box coiled-coil) family of E3 ubiquitin ligases. Emerging evidence has demonstrated that TRIM11 is a novel target against cancer and neurodegenerative diseases as it plays vital role in cellular proliferation, differentiation, tumor progression, and apoptosis. Our previous work demonstrated that TRIM11 is over-expressed in high-grade gliomas and promotes proliferation, invasion, migration and tumor growth, suggesting that TRIM11 may be used as a target for malignant glioma treatment. The t

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Han, Jiyu, Yanhong Wang, Haichao Zhou, Songtao Ai, and Daqian Wan. "Integrated Bioinformatics and Experimental Analysis Identified TRIM28 a Potential Prognostic Biomarker and Correlated with Immune Infiltrates in Liver Hepatocellular Carcinoma." Computational and Mathematical Methods in Medicine 2022 (October 4, 2022): 1–17. http://dx.doi.org/10.1155/2022/6267851.

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Background. Since the 1970s, liver hepatocellular carcinoma (LIHC) has experienced a constant rise in incidence and mortality rates, making the identification of LIHC biomarkers very important. Tripartite Motif-Containing 28 (TRIM28) is a protein-coding gene which encodes the tripartite motif-containing proteins (TRIMs) family and is associated with specific chromatin regions. TRIM28 expression and its prognostic value and impact on the immune system in LIHC patients are being investigated for the first time. Methods. The TRIM28 expression data from TCGA database was used to analyze TRIM28 exp

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Yuan, Peng, Yiyi Zhou, Rui Wang, et al. "TRIM58 Interacts with Pyruvate Kinase M2 to Inhibit Tumorigenicity in Human Osteosarcoma Cells." BioMed Research International 2020 (March 7, 2020): 1–9. http://dx.doi.org/10.1155/2020/8450606.

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Background. Tripartite motif containing 58 (TRIM58), an E3 ubiquitin ligase, is reported as a suppressor gene in certain human tumors. However, the biological function of TRIM58 in osteosarcoma (OS) is still less identified. Methods. In the present study, TRIM58 induced silencing and overexpression in OS cells using RNA interference (RNAi) and lentiviral-mediated vector, respectively. Cell proliferation profiles were analyzed using cell counting kit-8 (CCK-8) assay. Cell apoptosis profiles were determined using a flow cytometer. qRT-PCR and western blot were used to determine gene expression.

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Chang, Yao-Jen, Zhifu Kang, Jiayuan Bei, et al. "Generation of TRIM28 Knockout K562 Cells by CRISPR/Cas9 Genome Editing and Characterization of TRIM28-Regulated Gene Expression in Cell Proliferation and Hemoglobin Beta Subunits." International Journal of Molecular Sciences 23, no. 12 (2022): 6839. http://dx.doi.org/10.3390/ijms23126839.

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TRIM28 is a scaffold protein that interacts with DNA-binding proteins and recruits corepressor complexes to cause gene silencing. TRIM28 contributes to physiological functions such as cell growth and differentiation. In the chronic myeloid leukemia cell line K562, we edited TRIM28 using CRISPR/Cas9 technology, and the complete and partial knockout (KO) cell clones were obtained and confirmed using quantitative droplet digital PCR (ddPCR) technology. The amplicon sequencing demonstrated no off-target effects in our gene editing experiments. The TRIM28 KO cells grew slowly and appeared red, seem

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Neo, Shu Hui, Yoko Itahana, Jennifer Alagu, et al. "TRIM28 Is an E3 Ligase for ARF-Mediated NPM1/B23 SUMOylation That Represses Centrosome Amplification." Molecular and Cellular Biology 35, no. 16 (2015): 2851–63. http://dx.doi.org/10.1128/mcb.01064-14.

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The tumor suppressor ARF enhances the SUMOylation of target proteins; however, the physiological function of ARF-mediated SUMOylation has been unclear due to the lack of a known, associated E3 SUMO ligase. Here we uncover TRIM28/KAP1 as a novel ARF-binding protein and SUMO E3 ligase for NPM1/B23. ARF and TRIM28 cooperate to SUMOylate NPM1, a nucleolar protein that regulates centrosome duplication and genomic stability. ARF-mediated SUMOylation of NPM1 was attenuated by TRIM28 depletion and enhanced by TRIM28 overexpression. Coexpression of ARF and TRIM28 promoted NPM1 centrosomal localization

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