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Deletion of Ago2 in liver resulted in decreased fasting glucose levels in addition to reducing hepatic glucose production. Ago2 mediates the suppression of AMPKalpha1 by miR-148a.
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The microRNA effector protein AGO2 is predominantly expressed as an alternative isoform that encodes a truncated protein lacking all of the known essential domains. Full-length Ago2 was lowly expressed in maturing mouse oocytes. Reintroduction of full-length AGO2 together with an exogenous microRNA in either mouse or frog oocytes restored translational repression of a target reporter.
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We proved that this defect is cell autonomous and can be rescued by both a catalytically active and an inactive Ago2, but not by Ago2 deprived of its RNA binding capacity or by Ago1 overexpression. Overall, our results suggest a role for AGO2 in stem cell differentiation
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hepatic Ago2-mediated RNA silencing has a role in regulating energy metabolism linked to AMPK activation and obesity-associated pathophysiology
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AGO2-mediated cleavage of targets is more common than previously thought. This may explain the vital role of endonuclease activity in controlling miRNA-mediated gene regulation.
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Here, we show that partial loss of either APOBEC1 complementation factor (A1CF), the RNA-binding cofactor of APOBEC1 in RNA editing, or Argonaute 2 (AGO2), a key factor in the biogenesis of certain noncoding RNAs, modulates risk for TGCTs and testicular abnormalities in both parent-of-origin and conventional genetic manners.
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This identified Ago2 as a key determinant of quiescence exit in Hematopoietic stem cells.
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miR-9, along with Argonaute proteins (Agos), is localized to the nucleus of quiescent neural stem cells, and manipulating their nuclear/cytoplasmic ratio impacts quiescence.
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We propose that RISC-mediated inhibition of specific sets of chromatin regulators is a primary mechanism for preserving embryonic stem cell pluripotency while inhibiting the onset of embryonic developmental programs
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Increased AGO2 was detected in autophagy-deficient ATG5-/- and ATG16-/- mouse embryonic fibroblast cells. Chemical agents and VacA toxin, which disrupt autophagy, increased AGO2 expression in MEFs, epithelial cells lines, and human monocytes.
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DIS3L2 interacts with Ago2 and governs target RNA-directed miRNA degradation.
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Results from the liver show that, siRNA targets 3'UTR and the coding sequence (CDs) of endogenous genes in the presence Ago2 but in its absence, only 3'UTR-targeted siRNA-mediated knockdown are active with the help of Ago1 and Ago3.
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Roquin also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR-146a, a microRNA that targets Icos mRNA.
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mRNA Targeting to Endoplasmic Reticulum Precedes Ago Protein Interaction and MicroRNA (miRNA)-mediated Translation Repression
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Target mRNAs induce tailing and trimming on Ago2-loaded miRNAs.
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Mouse AGO2 binds tighter to miRNA targets than its RNAi cleavage product, even though the cleaved product contains more base pairs. By re-writing the rules for nucleic acid hybridization, Argonautes allow oligonucleotides to serve as specificity determinants with thermodynamic and kinetic properties more typical of RNA-binding proteins than of RNA or DNA.
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Mouse Ago2 can be expressed as a fusion protein with the maltose binding protein in a soluble and enzymatically active form, without requiring coexpression with chaperones and cleave the complementary RNA in absence of other cellular factors.
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This study identifies the targeting of Ago2 by miR-184 as an essential component of the compensatory response to regulate proliferation according to insulin sensitivity.
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study identifies Fkbp4 and Fkbp5 as novel components of the Ago2 RISC loading complex
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Insights into the role of Ago2 in the systemic release of proteins from beta-cells.