Mouse Protein argonaute-2(EIF2C2) ELISA kit

Required for RNA-mediated gene silencing (RNAi) by the RNA-induced silencing complex (RISC). The 'minimal RISC' appears to include AGO2 bound to a short guide RNA such as a microRNA (miRNA) or short interfering RNA (siRNA). These guide RNAs direct RISC to complementary mRNAs that are targets for RISC-mediated gene silencing. The precise mechanism of gene silencing depends on the degree of complementarity between the miRNA or siRNA and its target. Binding of RISC to a perfectly complementary mRNA generally results in silencing due to endonucleolytic cleavage of the mRNA specifically by AGO2. Binding of RISC to a partially complementary mRNA results in silencing through inhibition of translation, and this is independent of endonuclease activity. May inhibit translation initiation by binding to the 7-methylguanosine cap, thereby preventing the recruitment of the translation initiation factor eIF4-E. May also inhibit translation initiation via interaction with EIF6, which itself binds to the 60S ribosomal subunit and prevents its association with the 40S ribosomal subunit. The inhibition of translational initiation leads to the accumulation of the affected mRNA in cytoplasmic processing bodies (P-bodies), where mRNA degradation may subsequently occur. In some cases RISC-mediated translational repression is also observed for miRNAs that perfectly match the 3' untranslated region (3'-UTR). Can also up-regulate the translation of specific mRNAs under certain growth conditions. Binds to the AU element of the 3'-UTR of the TNF (TNF-alpha) mRNA and up-regulates translation under conditions of serum starvation. Also required for transcriptional gene silencing (TGS), in which short RNAs known as antigene RNAs or agRNAs direct the transcriptional repression of complementary promoter regions. Regulates lymphoid and erythroid development and function, and this is independent of endonuclease activity.

1. 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. PMID: 29031931
2. This identified Ago2 as a key determinant of quiescence exit in Hematopoietic stem cells. PMID: 26850790
3. 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. PMID: 27783951
4. 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 PMID: 27154007
5. 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. PMID: 26332312
6. Roquin also directly binds Argonaute2, a central component of the RNA-induced silencing complex, and miR-146a, a microRNA that targets Icos mRNA. PMID: 25697406
7. mRNA Targeting to Endoplasmic Reticulum Precedes Ago Protein Interaction and MicroRNA (miRNA)-mediated Translation Repression PMID: 26304123
8. Target mRNAs induce tailing and trimming on Ago2-loaded miRNAs. PMID: 25724380
9. 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. PMID: 26140592
10. 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. PMID: 20386665
11. 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. PMID: 24361012
12. study identifies Fkbp4 and Fkbp5 as novel components of the Ago2 RISC loading complex PMID: 24049110
13. Insights into the role of Ago2 in the systemic release of proteins from beta-cells. PMID: 23358505
14. In mouse cells, Ago2 stability declined in Dicer-knockout cells & was rescued by proteasome blockade or introduction of either Dicer plasmid or Dicer-independent miRNA constructs. PMID: 23708604
15. Our results illuminate a novel feedback mechanism that post-transcriptionally couples Ago2 protein levels with small RNA abundance with implications for RNA-interference (RNAi) and miRNA function. PMID: 23485552
16. Altering Ago2 expression in T cells revealed that Ago proteins are limiting factors that determine miRNA abundance. Naive T cells with reduced Ago2 and miRNA expression differentiated more readily into cytokine-producing helper T cells. PMID: 23382546
17. Stable Argonaute protein-associated small RNAs are capable of repressing mitogen-induced transcripts. PMID: 23248281
18. Highlighting its role in antiviral defense, fly Ago2 dissociates so slowly from extensively complementary target RNAs that essentially every fully paired target is cleaved. Conversely, mouse AGO2, which mainly mediates miRNA-directed repression, dissociates rapidly and with similar rates for fully paired and seed-matched targets. PMID: 23178124
19. Decreased miRNA stability in cells lacking Ago2. PMID: 21941127
20. Ago2 is essential for normal self-renewal and differentiation. PMID: 21857111
21. Isolated were RNAs photo-cross-linked to mAgo2, of which hundreds contained a seed match to the mouse embryonic stem cells -enriched miRNA cluster miR-290-295, and, unexpectedly, the majority also contained a G-rich motif. PMID: 21258322
22. Dicer knockout cells can generate mature miR-451 but not other miRNAs, whereas Ago2 knockout cells reconstituted with wild-type Ago2, but not Slicer-deficient Ago2, can process miR-451. PMID: 20699384
23. findings link the conservation of Argonaute catalysis to a conserved mechanism of microRNA biogenesis that is important for vertebrate development PMID: 20424607
24. Results suggest that Ago2 and Dicer1 regulate QW182 protein expression in mouse embryos, which is linked to microRNA biosynthesis. PMID: 20353723
25. AGO2 downregulation impaired both short-term and long-term contextual fear memories. PMID: 20109527
26. mouse Ago2 binds efficiently to miRNAs forming active RNA-induced silencing complexes PMID: 19808937
27. essential for mouse development and cells lacking Argonaute2 are unable to mount an experimental response to siRNAs PMID: 15284456
28. disruption of Eif2c2 leads to embryonic lethality early in development after the implantation stage PMID: 17418524
29. Ago2 controls early development of lymphoid and erythroid cells PMID: 17626790
30. loss of eIF2C2 (Argonaute2 or Ago2) results in gastrulation arrest, ectopic expression of Brachyury (T), and mesoderm expansion PMID: 18166081
31. maternal expression of Ago2 is essential for the earliest stages of mouse embryogenesis PMID: 18701707
32. show that mLin41 acts as an E3 ubiquitin ligase in an auto-ubiquitylation assay and that mLin41 mediates ubiquitylation of Ago2 in vitro and in vivo PMID: 19898466
33. High-throughput sequencing of Ago bound RNAs isolated by crosslinking immunoprecipitation (HITS-CLIP) identifies functional protein-RNA interaction sites in brain; validated miR-124 sites are also identified in HeLa cells. PMID: 19536157

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Cytoplasm, P-body. Nucleus.

Argonaute family, Ago subfamily

Ubiquitous expression in 9.5 day embryos with highest levels in forebrain, heart, limb buds, and branchial arches.

KEGG: mmu:239528

STRING: 10090.ENSMUSP00000042207

UniGene: Mm.23095