Tripartite Motif Containing 25 Proteins (TRIM25)

Human Tripartite Motif Containing 25 (TRIM25) interaction partners

1. formation of unanchored K63-linked poly-ubiquitin chains is unchanged by NS1 binding, indicating that RING dimerisation of TRIM25 is not affected by NS1

2. The RNA-binding activity of TRIM25 is mediated by its PRY/SPRY domain, which we postulate to be a novel RNA-binding domain.

3. TRIM25 inhibits hepatocellular carcinoma progression by targeting MTA1.

4. TRIM25 is a key determinant of breast cancer metastasis.

5. V interaction with TRIM25 and RIG-I prevents TRIM25-mediated ubiquitination of RIG-I and disrupts downstream RIG-I signaling to the mitochondrial antiviral signaling protein.

6. HPV E6 oncoprotein antagonizes the activation of the cytoplasmic innate immune sensor RIG-I by targeting its upstream regulatory enzymes TRIM25 and USP15. We further show that the RIG-I signaling cascade is important for an antiviral innate immune response to HPV16 infection

7. this study shows thatTRIM25 targets ERG for degradation in prostate cancer

8. TRIM25 actively participates in higher-order assembly of the RIG-I signalosome.

9. Our results indicate that TRIM25 is associated with cisplatin resistance and 14-3-3sigma-MDM2-p53 signaling pathway is involved in this process, suggesting targeting TRIM25 may be a potential strategy for the reversal of cisplatin resistance.

10. expression of TRIM25 might be critical for lung cancer cell migration, proliferation as well as doxorubicin resistance.

11. Disturbed p53-MDM2 feedback loop contributing to the pathogenesis of thoracic aortic dissection may be linked to TRIM25 overexpression.

12. the data uncover TRIM25 as a bona fide zinc-finger antiviral protein cofactor that leads to increased zinc-finger antiviral protein modification enhancing its translational inhibition activity.

13. Studies showed that 70% of breast cancer patients were positive for Trim25 expression.

14. we provide a detailed characterization of the TRIM ligases TRIM25 and TRIM32 and show how their oligomeric state is linked to catalytic activity

15. The severe acute respiratory syndrome coronavirus N protein was found to bind to the SPRY domain of the tripartite motif protein 25 (TRIM25) E3 ubiquitin ligase, thereby interfering with the association between TRIM25 and retinoic acid-inducible gene I (RIG-I) and inhibiting TRIM25-mediated RIG-I ubiquitination and activation.

16. TRIM25 is required for Zinc finger antiviral protein optimal binding to target mRNA.

17. TRIM25 may exert its function through TGF-beta pathway.

18. TRIM25 plays an additional role in RIG-I/MDA5 signaling other than RIG-I ubiquitination via activation of NF-kappaB.

19. Data show that TRIM25 enhances p53 and Mdm2 abundance by preventing their proteasomal degradation. At the same time, TRIM25 inhibits p53's transcriptional activity and dampens the response to DNA damage.

20. The PR-2B DENV-2 produced increased levels of subgenomic flavivirus RNA (sfRNA) relative to genomic RNA during replication. PR-2B sfRNA showed sequence dependent binding to and prevention of tripartite motif 25 (TRIM25) deubiquitylation, which is critical for sustained and amplified retinoic acid-inducible gene 1 (RIG-I)-induced type I interferon expression.

Mouse (Murine) Tripartite Motif Containing 25 (TRIM25) interaction partners

1. TRIM25 as a key determinant of breast cancer metastasis.

2. Studies indicated that mice with disrupted Trim25 were viable and fertile, uterine response to oestrogen was greatly attenuated and the uteri were underdeveloped.

3. Two key residues (Asp(488) and Trp(621)) in the TRIM25 B30.2 domain are critical for binding to the RIG-I CARDs.

4. Two well-known E3 ubiquitin ligases, Trim25 (also called Efp) and Trim71 (also called Lin41), are validated as RNA-binding proteins, revealing a potential link between RNA biology and protein-modification pathways.