{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nTRBP (TAR‐binding protein 2) plays a central role in the canonical RNA interference pathway by acting as an essential cofactor in the RISC‐loading complex. It partners with Dicer and Argonaute proteins to facilitate the precise cleavage of double‐stranded precursor microRNAs and the subsequent selection of the correct guide strand. Structural and biochemical studies have revealed that TRBP uses its multiple double‐stranded RNA binding domains to recognize and bind both pre‐miRNAs and siRNAs, thereby promoting efficient maturation and strand transfer‐to‐Ago complexes. These investigations have also underscored its ability to interact directly with Dicer, modulate pre‐miRNA processing fidelity, and even influence steroid receptor–mediated transcription through its association with nuclear factors."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its core role in miRNA biogenesis, TRBP modulates the precision and efficiency of RNA processing. It influences the cleavage kinetics of pre‐miRNAs, alters the production of length‐variant (isomiR) species, and undergoes post‐translational modifications—such as phosphorylation and SUMOylation—that fine‐tune its activity. These regulatory mechanisms, in turn, impact the effective loading of mature miRNAs into Argonaute proteins and consequently determine the potency of gene silencing."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its functions in RNA silencing, TRBP interfaces with multiple cellular signaling networks that influence antiviral responses and tumor biology. By inhibiting the activation of protein kinase R (PKR) and modulating innate immune signaling (including interactions that affect RIG‐I and interferon regulatory factors), TRBP contributes to the regulation of virus–host dynamics and the suppression of antiviral cytokine production. 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