Protein argonaute-4 (AGO4)

Protein argonaute-4 (AGO4) is a member of the Argonaute protein family, which is highly conserved across species and functions as a core component of the RNA-induced silencing complex (RISC)[1][2][4][5][6]. In humans, AGO4 binds microRNAs (miRNAs) and small interfering RNAs (siRNAs), guiding RISC to complementary target mRNAs, leading primarily to translational repression or mRNA destabilization via base pairing between the miRNA and target mRNA[1][2]. Structurally, AGO4 contains the N, PAZ, MID, and PIWI domains characteristic of Argonautes; however, it lacks the full catalytic ("slicer") activity seen in Argonaute-2 (AGO2), as it does not possess all required active site residues for endonucleolytic cleavage[1][2]. In plant systems, AGO4 is involved in siRNA-guided DNA methylation and chromatin modification, but human AGO4's function is primarily post-transcriptional gene silencing and its specific physiological roles are less well defined compared to other Argonautes[1][3][6]. While general dysregulation of Argonaute proteins and miRNA pathways is implicated in cancer and other diseases, AGO4 itself is not a prominent therapeutic target, nor are there drugs that directly act on it.

Other names

EIF2C4KIAA1567hAgo4Argonaute4Argonaute RISC catalytic component 4Eukaryotic translation initiation factor 2C 4FLJ20033eIF-2C 4RISC catalytic component 4argonaute RISC catalytic component 4eIF2C 4hAGO4

Not applicable. No drugs are known to bind to or modulate AGO4 directly.