
Chaperones choreograph AGO2 loading to form active RISC
Nature reports a structural study showing how the AGO–HSP90–p23 maturation complex (AMC) traps AGO2 in an RNA-free state and uses a duplex RNA to drive AGO folding and loading, revealing an open AGO2 conformation that accommodates dsRNA. A 5′-phosphate-containing RNA duplex acts as a cofactor guiding domain assembly, enabling de novo RISC formation and productive RNA silencing, with implications for designing siRNA therapeutics and understanding chaperone-guided protein folding.

