AI Article Synopsis
- TRIM29 is a protein involved in inflammatory and cancer processes, particularly in gastric cancer, where its role has not been fully understood.
- Researchers found that TRIM29 levels are lower in gastric cancer tissues compared to normal tissues, and this reduction is linked to hypermethylation of its gene.
- TRIM29 enhances T-cell immunity against tumors by interacting with another protein, IGF2BP1, which affects the stability of PD-L1, suggesting that this axis could be a useful marker and target for gastric cancer treatment.
Article Abstract
Tripartite motif-containing protein 29 (TRIM29) is a member of TRIM family protein which has been reported to play a role in the progress of inflammatory and cancer diseases. However, its specific role in gastric cancer (GC) has yet to be fully understood. Here, we investigated the expression of TRIM29 in gastric cancer and its functions in the antitumor immunity. TRIM29 expression was lower in tumor tissues than that in paired normal tissues. Lower expression of TRIM29 was related to aberrant hypermethylation of CpG islands in TRIM29 gene. Comprehensive proteomics and immunoprecipitation analyses identified IGF2BP1 as TRIM29 interactors. TRIM29 interacted with IGF2BP1 and induced its ubiquitination at Lys440 and Lys450 site by K48-mediated linkage for protein degradation. IGF2BP1 promoted PD-L1 mRNA stability and expression in a 3'UTR and mA-dependent manner. Functionally, TRIM29 enhanced antitumor T-cell immunity in gastric cancer dependent on the IGF2BP1/PD-L1 axis in vivo and in vitro. Clinical correlation analysis revealed that TRIM29 expression in patient samples was associated with CD8 immune cell infiltration in the GC microenvironment and the overall survival rates of GC patients. Our findings revealed a crucial role of TRIM29 in regulating the antitumor T-cell immunity in GC. We also suggested that the TRIM29/IGF2BP1/PD-L1 axis could be used as a diagnostic and prognostic marker of gastric cancer and a promising target for GC immunotherapy.
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| http://dx.doi.org/10.1016/j.canlet.2023.216510 | DOI Listing |
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