Informace o publikaci
Uncovering the Assembly of the RISC-Loading Complex
| Autoři | |
|---|---|
| Rok publikování | 2025 |
| Druh | Konferenční abstrakty |
| Fakulta / Pracoviště MU | |
| Citace | |
| Přiložené soubory | |
| Popis | Argonaute and Dicer proteins are key components of RNA-dependent gene silencing. In mammals, Argonaute-2 (Ago2) functions as the primary effector of microRNA (miRNA)-mediated gene regulation. Following Dicer-mediated processing of precursor miRNAs (pre-miRNAs), Ago2 is selectively loaded with mature miRNA guides to form the RNA-induced silencing complex (RISC). Despite more than two decades of extensive research, the molecular rules and structural basis governing guide-strand selection and loading remain only partially understood. Notably, multiple studies suggest that Dicer and its cofactor TARBP2 (or PACT) play important roles in facilitating the accurate and efficient loading of Ago2. Here, we present our preliminary efforts to characterize the molecular interactions between Ago2 and the Dicer–TARBP2 complex, as well as the specific contributions of each component during the RISC-loading process. Our structural biology approach provides insights into the roles of the individual components and sheds light on the overall mechanism of RISC assembly. |