Uncovering the Assembly of the RISC-Loading Complex

Result code in IS VaVaI
<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F00216224%3A14740%2F25%3A00143661" target="_blank" >RIV/00216224:14740/25:00143661 - isvavai.cz</a>
Result on the web
<a href="https://argonautes.img.cas.cz/" target="_blank" >https://argonautes.img.cas.cz/</a>
DOI - Digital Object Identifier
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Result language
angličtina
Original language name
Uncovering the Assembly of the RISC-Loading Complex
Original language description
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.
Czech name
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Czech description
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Project
<a href="/en/project/EH22_008%2F0004575" target="_blank" >EH22_008/0004575: RNA for therapy</a><br>
Continuities
P - Projekt vyzkumu a vyvoje financovany z verejnych zdroju (s odkazem do CEP)

Publication year
2025
Confidentiality
S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

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