An Ago2HA/HA mouse model combined with super-resolution microscopy, molecular and biochemical assays allowed us to stringently characterize AGO2 regulation in vivo. We found that in quiescent splenocytes, AGO2 localizes almost exclusively to the nucleus, where it binds to the RNA of young mobile transposons and represses their expression through its catalytic domain.
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References
Sala, L., Chandrasekhar, S. & Vidigal, J. A. AGO unchained: canonical and non-canonical roles of Argonaute proteins in mammals. Front. Biosci. 25, 1–42 (2020). A review article that discusses the roles of AGO proteins in vivo.
La Rocca, G. et al. In vivo, Argonaute-bound microRNAs exist predominantly in a reservoir of low molecular weight complexes not associated with mRNA. Proc. Natl Acad. Sci. USA 112, 767–772 (2015). This paper reports the existence of different AGO2 complexes in vitro and in vivo.
Nazer, E., Gomez Acuna, L. & Kornblihtt, A. R. Seeking the truth behind the myth: Argonaute tales from “nuclearland”. Mol. Cell. 82, 503–513 (2022). A review article discussing nuclear roles for AGO proteins in different model organisms.
Stein, P. et al. Essential role for endogenous siRNAs during meiosis in mouse oocytes. PLoS Genet 11, e1005013 (2015). This paper reports the requirement of the catalytic domain of AGO2 to mouse female meiosis.
Flemr, M. et al. A retrotransposon-driven dicer isoform directs endogenous small interfering RNA production in mouse oocytes. Cell 155, 807–816 (2013). This paper reports the existence of a truncated DICER isoform in mouse oocytes.
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This is a summary of: Sala, L. et al. AGO2 silences mobile transposons in the nucleus of quiescent cells. Nat. Struct. Mol. Biol. https://doi.org/10.1038/s41594-023-01151-z (2023).
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AGO2 localizes to the nucleus in quiescence and represses transposon expression. Nat Struct Mol Biol 30, 1838–1839 (2023). https://doi.org/10.1038/s41594-023-01169-3
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DOI: https://doi.org/10.1038/s41594-023-01169-3
