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TRIM25

ABSTRACT: TRIM25

PROVIDER: PRJNA316328 | ENA |

REPOSITORIES: ENA

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Dataset's files

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			Action	DRS
	SRR3290840_1.fastq.gz	Fastqsanger.gz
	SRR3290840_2.fastq.gz	Fastqsanger.gz
	SRR3290850_1.fastq.gz	Fastqsanger.gz
	SRR3290850_2.fastq.gz	Fastqsanger.gz
	SRR3290860_1.fastq.gz	Fastqsanger.gz

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Similar Datasets

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.

2018-07-27 | GSE104949 | GEO

Genome-wide maps of TRIM25 binding sites in triple negative breast cancer cell

Project description:We report high-throughput profiling of TRIM25 binding sites in triple negative breast cancer cells.

2017-04-01 | GSE79588 | GEO

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.

2024-09-20 | GSE276465 | GEO

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.

2023-07-11 | GSE236661 | GEO

Identification of mRNA bound by TRIM25 binding in triple negative breast cancer

Project description:We report high-throughput profiling of TRIM25 bound mRNA in triple negative breast cancer cells.

2017-04-01 | GSE79587 | GEO

Effect of depletion of TRIM25 and inhibition of p300 on gene expression in breast cancer cells

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

2022-10-11 | GSE215084 | GEO

Ubiquitination of DEAD-box RNA helicase DDX3X by TRIM25

Project description:Tripartite motif protein 25 (TRIM25) is an E3 ligase that ubiquitinates multiple substrates within the RLR signalling cascade and plays both RING (really interesting new gene)-dependent and RING-independent roles in RIG-I-mediated IFN induction. We report that the PRY-SPRY domain of TRIM25 interacts with the N-terminal extension (NTE) of DEAD-box helicase 3X (DDX3X), a host protein with multiple roles in RLR signalling. Gene reporter assays and knockdown studies reveal DDX3X and TRIM25 cooperate to activate the IFN- promoter following RIG-I activation independent of DDX3X’s catalytic activity. We also show that TRIM25 ubiquitinates DDX3X at several lysine residues in vitro and in cells.

2021-09-08 | PXD028122 | Pride

The long noncoding RNA Lnczc3h7a promotes TRIM25-mediated RIG-I antiviral innate immune response

Project description:In this study, we employed a combination of RIP-seq and iCLIP-seq technologies to identify long non-coding RNA associated with cytoplasmic TRIM25 and RIG-I protein in mouse macrophages cells.

2019-03-12 | GSE112175 | GEO

Substrate trapping approach identifies TRIM25 ubiquitination targets involved in diverse cellular and antiviral processes

Project description:The tripartite motif (TRIM) family of E3 ubiquitin ligases is well known for its roles in antiviral restriction and innate immunity regulation, in addition to many other cellular pathways. In particular, TRIM25-mediated ubiquitination affects both carcinogenesis and antiviral response. While individual substrates have been identified for TRIM25, it remains unclear how it regulates diverse processes. Here we characterized a mutation, R54P, critical for TRIM25 catalytic activity, which we successfully utilized to “trap” substrates. We demonstrated that TRIM25 targets proteins implicated in stress granule formation (G3BP1/2), nonsense-mediated mRNA decay (UPF1), and nucleoside synthesis (NME1). R54P abolishes TRIM25 inhibition of alphaviruses independently of the host interferon response, suggesting that this antiviral effect is a direct consequence of ubiquitination. Consistent with that, we observed diminished antiviral activity upon knockdown of several TRIM25-R54P specific interactors including NME1. Our findings highlight that multiple substrates mediate the cellular and antiviral activities of TRIM25, illustrating the multi-faceted role of this ubiquitination network in diverse biological processes.

2022-08-02 | PXD034024 | Pride

Proximity labeling proteins differences between TRIM25 and G3BP1 interactions or not, and Proximity labeling proteins differences between G3BP1 and TRIM25 in the presence or absence of poly(I:C) stimulation

Project description:This project investigates G3BP1 proximity proteins by constructing a G3BP1-BirA* fusion protein using G3BP1 as a decoy protein and BirA* as a biotin ligase. The changes in G3BP1 proximity proteins were studied in the presence or absence of poly(I:C) stimulation conditions, using poly(I:C) stimulation as a variable. This project investigated the TRIM25 proximity protein by constructing a TRIM25-BirA* fusion protein with TRIM25 as the decoy protein and BirA* as the biotin ligase. The changes of TRIM25 proximity proteins under the conditions of TRIM25 interacting with or without G3BP1 were studied by performing PTFG sequence deletion on TRIM25; the changes in TRIM25 proximity proteins were studied in the presence or absence of poly(I:C) stimulation conditions, using poly(I:C) stimulation as a variable.

2023-07-07 | PXD043603 |

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