Psychiatry related information on AGO2

• Unlike wild type, nuclear division is asynchronous in ago-2 embryos and there are defects in chromosome condensation, nuclear kinesis, and assembly of spindle apparatus [1].

High impact information on AGO2

• The mRNA-cleavage step of RNA interference is mediated by an endonuclease, Argonaute2 (Ago2), within the RNA-induced silencing complex (RISC) [2].
• Here we show that Argonaute-2 (ago-2) is required for proper nuclear migration, pole cell formation, and cellularization during the early stages of embryonic development in Drosophila [1].
• Drosophila argonaute-2 is required early in embryogenesis for the assembly of centric/centromeric heterochromatin, nuclear division, nuclear migration, and germ-cell formation [1].
• The RNA-induced silencing complex component Argonaute2 and orthologues of LSm4 and Xrn1 (Pacman) associated with 5'-3' mRNA degradation localize to some GWBs [3].
• By using a bioinformatics method that combines sequence-profile analysis with predicted protein secondary structure, we found homology between the PIWI domain of Ago-2 and endonuclease V and identified potential active-site amino acid residues within the PIWI domain of Ago-2 [4].

Biological context of AGO2

• Here we show that AGO2 is an essential component for siRNA-directed RNA interference (RNAi) response and is required for the unwinding of siRNA duplex and in consequence assembly of siRNA into RISC in Drosophila embryos [5].
• Moreover, AGO1 and AGO2 silence the expression of a common set of mobile genetic elements [6].
• The possibility that AGO2 and Dicer2 involve, at least in part, poly(A) length maintenance of transgene mRNA suggests a potentially important link between transgene silencing and poly(A) tails [7].
• Furthermore, Dcr2 and Ago2 display reduced genetic diversity, indicative of a recent selective sweep in both genes [8].

Anatomical context of AGO2

• We show here that RNAi in a hemocyte cell line of Anopheles gambiae, the principal malaria vector in Africa, requires expression of dicer-2, Ago2 and Ago3 proteins [9].
• In the developing lung, we found expression of Ago1 and Ago2 localized to branching regions, in distal epithelium and mesenchyme, respectively [10].

Other interactions of AGO2

• Together, these results indicate that the functional overlap between AGO1 and AGO2 in Drosophila is more important than previously thought [6].
• We show that in Drosophila, the orientation of the Dicer-2/R2D2 protein heterodimer on the siRNA duplex determines which siRNA strand associates with the core RISC protein Argonaute 2 [11].

References