ArticleRNA (New York, N.Y.)2025
The molecular chaperone TRAP1 promotes translation of
Article in RNA (New York, N.Y.), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.
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Abstract
Heat shock proteins have been increasingly identified in RNA-interactomes, suggesting potential roles beyond their canonical functions. Among those, the cancer-linked chaperone TRAP1 has been mainly characterized for its regulatory role on respiratory complex activity and protein synthesis, while its specific function as an RNA-binding protein (RBP) remains unclear. In this study, we confirmed the RNA-binding activity of TRAP1 in living cells using both protein- and RNA-centric approaches and demonstrated that multiple TRAP1 regions cooperate in such binding. Enhanced cross-linking and immunoprecipitation (eCLIP) in high-grade serous ovarian cancer cells revealed that TRAP1 primarily binds cytosolic protein-coding genes, with the majority coding for splicing-related factors. Notably, among TRAP1 most significantly bound transcripts, we identified the splicing factor LUC7L3, a U1 snRNP component involved in cell proliferation. We confirmed TRAP1 binding to the
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