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Destruction of VISTA by TRIM25 ablation in T cells potentiates cancer immunotherapy

ABSTRACT: To gain deeper insights into the role of Trim25 expression in T cells in regulating tumor microenvironment dynamics, we performed single-cell RNA sequencing on purified CD45+ immune cells isolated from MC38 xenografts harvested from either Trim25 cKO or WT C57BL/6 mice.

ORGANISM(S): Mus musculus

PROVIDER: GSE281314 | GEO | 2025/09/15

REPOSITORIES: GEO

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Destruction of VISTA by TRIM25 ablation in T cells potentiates cancer immunotherapy

Project description:Destruction of VISTA by TRIM25 ablation in T cells potentiates cancer immunotherapy

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Destruction of VISTA by TRIM25 ablation in T cells potentiates cancer immunotherapy

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Exogenous RNA surveillance by proton-sensing TRIM25

Project description:Exogenous mRNAs require cellular machinery for delivery and translation but also encounter inhibitory factors. To investigate their regulation, we performed genome-wide CRISPR screens with in vitro-transcribed mRNAs in lipid nanoparticles (LNPs). Heparan sulfate proteoglycans and vacuolar ATPase were identified as mediators of LNP uptake and endosomal escape, respectively. TRIM25 emerged as a key suppressor inducing turnover of both linear and circular mRNAs. Endoribonucleases, N4BP1 and KHNYN, along with ZAP, act redundantly in TRIM25-dependent surveillance. TRIM25 specifically targets mRNAs delivered via endosomes, and its RNA affinity increases at acidic pH, suggesting activation by protons released from ruptured endosomes. N1-methylpseudouridine (m1Ψ) modification reduces TRIM25’s RNA binding, helping RNAs evade its suppressive effect. This study comprehensively maps cellular pathways regulating LNP-mRNAs, offering insights into RNA immunity and therapeutics.

2025-04-04 | GSE264535 | GEO

RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain and is required for ubiquitination

Project description:TRIM25 E3 ubiquitin ligase is a new RNA-binding protein. We present the first high-throughput analysis of the molecular interactomes of TRIM25. We show that TRIM25 is a bona fide RNA-binding protein that interacts with numerous coding and non-coding transcripts. This suggests that TRIM25 could play a role in the regulation of RNA metabolism.

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The molecular dissection of TRIM25‘s RNA-binding mechanism provides key insights into its antiviral activity

Project description:TRIM25 is an RNA-binding ubiquitin E3 ligase with central but poorly understood roles in the innate immune response to RNA viruses. The link between TRIM25’s RNA binding and its role in innate immunity has not been established. Thus, we utilized a multitude of biophysical techniques to identify key RNA-binding residues of TRIM25 and developed an RNA-binding deficient mutant (TRIM25-m9). Using iCLIP2 in virus-infected and uninfected cells, we identified TRIM25’s RNA sequence and structure specificity, that it binds specifically to viral RNA, and that the interaction with RNA is critical for its antiviral activity.

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UFL1 ablation in T cells suppresses PD-1 UFMylation to enhance anti-tumor immunity

Project description:To better understand the impact of Ufl1 expression in T cells on regulating tumor microenvironment dynamics, we performed single-cell RNA sequencing on purified CD45+ immune cells from MC38 xenografts harvested from Ufl1 cKO or WT C57BL/6 mice.

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TRIM25 promotes glioblastoma cell growth and invasion via regulation of the PRMT1/c-MYC pathway by targeting the splicing factor NONO

Project description:Ubiquitination plays an important role in proliferating and invasive characteristic of glioblastoma (GBM), similar to many other cancers. Tripartite motif 25 (TRIM25) is a member of the TRIM family of proteins, which are involved in tumorigenesis through substrate ubiquitination. Here, we found TRIM25 is upregulated in GBM and promotes glioblastoma cell growth and invasion, both in vitro and in vivo. Subsequently, we screened a panel of proteins that interact with TRIM25; mass spectrometry and co-immunoprecipitation showed that NONO was a potential substrate of TRIM25. TRIM25 knockdown reduced the K63-linked ubiquitination of NONO, which suppressed the splicing function of NONO. The dysfunctional NONO further leads to the retention of the second intron in the pre-mRNA of PRMT1 and inhibit the activation of the PRMT1/c-MYC pathway. In summary, we demonstrated that TRIM25 promotes glioblastoma cell growth and invasion by regulating the PRMT1/c-MYC pathway through mediation of the splicing factor NONO. Efforts to target the E3 ligase activity of TRIM25 or the complex interactions between TRIM25 and NONO may be useful in the treatment of GBM.

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Project description:To analyze the effect of TRIM25 on gene expression, TRIM25 was knocked out in MCF7 cells. To understand a possible contribution of p300 on this gene regulation, p300 was inhibited. RNA seq was performed to see changes in the whole transcriptome

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