Affinage

AGO3

Protein argonaute-3 · UniProt Q9H9G7

Round 2 corrected
Length
860 aa
Mass
97.4 kDa
Annotated
2026-04-28
50 papers in source corpus 21 papers cited in narrative 22 extracted findings

Mechanistic narrative

Synthesis pass · prose summary of the discoveries below

AGO3 (Argonaute-3) is a member of the Argonaute protein family that participates in small RNA-mediated gene silencing across multiple biological contexts. In mammals, AGO3 loads miRNAs in proportion to its cellular abundance, interacts with GW182/TNRC6 scaffold proteins and Importin 8 to effect miRNA-guided translational repression and mRNA decay, but lacks endonucleolytic (slicer) activity, unlike AGO2 (PMID:15260970, PMID:22474261, PMID:19383768, PMID:19167051). AGO3 also processes retinoic acid-induced Alu-derived small RNAs to direct degradation of stem-cell mRNAs such as Nanog, thereby regulating exit from the pluripotent state (PMID:23064648). In invertebrate germlines (Drosophila, Bombyx, mosquito), orthologous AGO3 retains slicer activity and functions as the sense-strand piRNA carrier in the ping-pong amplification cycle, where its endonuclease cleavage of transposon transcripts initiates phased production of antisense piRNAs loaded into Piwi, with its stability, nuage localization, and piRNA loading coordinated by PRMT5-mediated symmetric dimethylarginine modifications and Tudor-domain proteins Krimper, PAPI, and Vreteno (PMID:25049272, PMID:26340424, PMID:19377467, PMID:26295961, PMID:37984437).

Mechanistic history

Synthesis pass · year-by-year structured walk · 12 steps
  1. 2003 Medium

    Identification of AGO3 as a DICER-associated Argonaute family member placed it within the RNA silencing machinery and established its potential role in siRNA/miRNA pathways.

    Evidence Co-immunoprecipitation and affinity binding of FLAG-DICER with His-AGO family members in HEK293 cells; siRNA knockdown functional assays

    PMID:12526743 PMID:12906857

    Open questions at the time
    • Whether AGO3 possesses catalytic activity was not tested
    • Relative contribution of AGO3 versus other AGO family members to silencing was unknown
    • Endogenous small RNA cargo of AGO3 was uncharacterized
  2. 2004 High

    Demonstrating that purified human AGO3 complexes associate with miRNAs yet lack slicer activity resolved a key question about functional specialization within the mammalian AGO family.

    Evidence Affinity purification of FLAG/HA-tagged AGO1–4 from human cells followed by in vitro RNA cleavage assays

    PMID:15260970

    Open questions at the time
    • The mechanism by which AGO3 contributes to silencing without cleavage was not determined
    • Whether AGO3 has any unique target selectivity versus other non-slicer AGOs remained open
  3. 2009 High

    Multiple studies established the interaction network and regulatory framework for AGO3 in miRNA-mediated silencing: GW182/TNRC6 proteins recruit AGO3 for translational repression and mRNA decay, Importin 8 facilitates AGO-target engagement, and RISC loading proceeds with shared structural preferences across all four human AGOs.

    Evidence Co-immunoprecipitation and tethering assays for TNRC6-AGO interaction; Imp8 knockdown with AGO IP-microarray; in vitro RISC assembly with purified AGO proteins and systematic duplex variants

    PMID:19167051 PMID:19383768 PMID:19966796

    Open questions at the time
    • AGO3-specific contributions to target repression were not separated from those of other AGOs
    • Whether AGO3 has non-redundant targets in vivo was untested
  4. 2009 High

    Discovery that Drosophila Ago3 carries PRMT5-dependent symmetrical dimethylarginine modifications essential for its protein stability revealed a post-translational regulatory axis critical for piRNA pathway function.

    Evidence dPRMT5 genetic loss-of-function in Drosophila ovaries with western blotting for Ago3/Aub levels and sDMA detection

    PMID:19377467

    Open questions at the time
    • Identity of specific arginine residues modified was not mapped
    • Whether sDMA modifications regulate Ago3 slicer activity directly was unknown
  5. 2010 High

    Defining the Drosophila Ago3-Aub ping-pong cycle in testes revealed that Ago3 and Aub are mutually interdependent for piRNA accumulation, with a modified strand-bias at certain loci.

    Evidence Ago3 immunoprecipitation followed by deep sequencing in Drosophila testes, piRNA pathway mutant analysis

    PMID:20980675

    Open questions at the time
    • Whether the modified ping-pong mechanism at Su(Ste) loci reflects a testis-specific adaptation was not resolved
    • Direct demonstration of Ago3 slicer cleavage products in testes was lacking
  6. 2011 High

    Identification of PAPI as a Tudor-domain partner that anchors Ago3 to nuage via sDMA-dependent binding established the first molecular mechanism for Ago3 subcellular localization in the piRNA pathway.

    Evidence Co-IP, papi mutant immunofluorescence and western blot showing Ago3 delocalization and destabilization in Drosophila ovaries

    PMID:21447556

    Open questions at the time
    • Whether PAPI directly facilitates piRNA loading onto Ago3 or merely provides a localization platform was unclear
    • Relationship between PAPI and other Tudor-domain organizers (Krimper, Vreteno) was unresolved
  7. 2012 High

    Two studies in mammalian systems refined AGO3's functional scope: mouse Ago3 loads miRNAs in proportion to its low abundance with random sorting, while human AGO3 processes Alu-derived small RNAs to degrade Nanog mRNA and regulate stem-cell fate.

    Evidence Conditional Ago1/Ago2 knockout in mouse skin with quantitative proteomics and small RNA-seq; AGO3 knockdown in human embryonic stem cells with RNA-seq and Co-IP

    PMID:22474261 PMID:23064648

    Open questions at the time
    • Whether AGO3-dependent Alu RNA processing occurs in tissues beyond embryonic stem cells was untested
    • Structural basis for AGO3 recognition of Alu-derived duplexes was unknown
  8. 2014 High

    Active-site mutagenesis proved that Drosophila Ago3 slicer activity is essential for ping-pong piRNA amplification and revealed a slicer-independent role in suppressing aberrant Aub:Aub ping-pong and controlling Armitage localization between mitochondria and nuage.

    Evidence Ago3 catalytic-dead mutant expression, subcellular fractionation, immunoprecipitation, and genetic epistasis in Drosophila germline

    PMID:25049272

    Open questions at the time
    • Molecular mechanism by which Ago3 inhibits Aub:Aub homotypic ping-pong without slicing was unknown
    • How Ago3 coordinates Armitage trafficking with Zucchini at mitochondria was not biochemically defined
  9. 2015 High

    Three convergent studies defined the Tudor protein Krimper as the central scaffold of Ago3 nuage recruitment and ping-pong complex assembly: Krimper binds piRNA-free Ago3, promotes its sDMA modification and sense-piRNA loading, and coordinates Ago3-Aub pairing; meanwhile Ago3 cleavage was shown to initiate most Piwi-bound piRNA production via phased biogenesis.

    Evidence In vitro binding assays, Krimper-RNAi and krimp mutant analysis, FRAP dynamics, piRNA sequencing in ago3 slicer mutants and qin mutants in Drosophila ovaries

    PMID:26212455 PMID:26295961 PMID:26340424

    Open questions at the time
    • Structural details of the Krimper-Ago3 interface were unresolved
    • Whether Krimper-equivalent scaffolds exist in mammalian piRNA pathways was unknown
  10. 2020 High

    Work in Bombyx mori demonstrated that Ago3-piRISC bodies serve as the platform for secondary Siwi-piRISC production, with Tudor protein Vreteno bridging unloaded Siwi and Ago3-piRISC via sDMA contacts; upon Siwi depletion Ago3 undergoes protective phosphorylation and insolubilization, revealing a quality-control mechanism.

    Evidence Siwi depletion and re-expression experiments, phosphorylation analysis, Co-IP, immunofluorescence in Bombyx ovarian germ cells

    PMID:32914505

    Open questions at the time
    • Identity of the kinase phosphorylating Ago3 was unknown
    • Whether this aggregation mechanism is conserved in Drosophila was untested
  11. 2021 High

    Biochemical dissection of DDX43 showed it liberates cleaved RNA products from Bombyx Ago3-piRISC in an ATP hydrolysis-dependent manner, resolving how sense-strand cleavage intermediates are handed off for Siwi loading.

    Evidence Domain deletion and mutagenesis of DDX43, ATP hydrolysis assays, Co-IP with Ago3-piRISC in Bombyx cells

    PMID:33555135

    Open questions at the time
    • Whether a DDX43 ortholog performs the same function in Drosophila or mammals was unknown
    • Structural basis of DDX43-Ago3 interaction was not determined
  12. 2023 High

    Identification of BmGtsf1L as a co-factor that binds piRNA-loaded Ago3 and engages a second, distinct interface on the Vreteno eTudor domain established a dual-binding model for piRNA amplification complex assembly.

    Evidence AlphaFold modeling validated by in vitro binding assays with point mutations, Co-IP, and immunofluorescence in Bombyx

    PMID:37984437

    Open questions at the time
    • Functional consequence of disrupting the Gtsf1L-Vreteno interface on piRNA levels in vivo was not quantified
    • Whether the dual-interface model extends to Drosophila Vreteno was untested

Open questions

Synthesis pass · forward-looking unresolved questions
  • Key open questions include: the structural basis for human AGO3's catalytic inactivity versus invertebrate Ago3's slicer competence; whether mammalian AGO3 has non-redundant physiological roles distinct from AGO1/2/4 in somatic tissues; the identity of kinases and phosphatases regulating Ago3 aggregation; and the extent to which the mammalian germline AGO3-BRG1 axis of meiotic sex chromosome inactivation operates through piRNA or miRNA pathways.
  • No crystal or cryo-EM structure of human AGO3 is available
  • Mammalian somatic non-redundant functions of AGO3 are poorly defined
  • Mechanism linking AGO3 to BRG1 removal from sex chromatin is biochemically unresolved

Mechanism profile

Synthesis pass · controlled-vocabulary classification · explore literature graph →
Molecular activity
GO:0003723 RNA binding 4 GO:0140098 catalytic activity, acting on RNA 3 GO:0098772 molecular function regulator activity 2
Localization
GO:0005829 cytosol 2 GO:0005634 nucleus 1 GO:0005694 chromosome 1
Pathway
R-HSA-8953854 Metabolism of RNA 6 R-HSA-74160 Gene expression (Transcription) 2
Partners
DDX43DICER1IPO8PAPITDRKHTNRC6A
Complex memberships
RISCping-pong piRNA processing complex (4P complex)

Evidence

Reading pass · 22 per-paper findings extracted from the source corpus
Year Finding Method Journal Conf PMIDs
2003 Human AGO3 (EIF2C3) was identified as a member of the eIF2C/AGO subfamily of Argonaute proteins. Immunoprecipitation and affinity binding experiments in HEK293 cells demonstrated that AGO3 protein associates with DICER, placing it within the RNA-mediated gene-silencing machinery. Immunoprecipitation and affinity binding assays in HEK293 cells co-transfected with FLAG-tagged DICER and His-tagged AGO family members Genomics Medium 12906857
2003 AGO3 (eIF2C3) and other eIF2C family members were shown to play an essential role in mammalian siRNA-mediated post-transcriptional gene silencing (PTGS), likely through synergistic interactions with Dicer. Immunoprecipitation experiments indicated complex formation between Dicer and eIF2C members. siRNA-based knockdown functional assay combined with immunoprecipitation in human and mouse cells Current biology : CB Medium 12526743
2004 Human AGO3 associates with miRNAs and is incorporated into microRNPs (miRNPs), but unlike AGO2, purified FLAG/HA-tagged AGO3 complexes lack endonuclease (slicer) activity. Exogenously introduced siRNAs also fail to recruit AGO3 for target RNA cleavage, establishing AGO3 as a catalytically inactive Argonaute in the miRNA/siRNA pathway. Affinity purification of FLAG/HA-tagged AGO1-4 from human cell lines, RNA cleavage assays, siRNA-based depletion of individual AGO members with reporter assay Molecular cell High 15260970
2009 Drosophila Ago3 contains symmetrical dimethylarginine (sDMA) modifications catalyzed by dPRMT5 (csul/dart5). Loss of dPRMT5 activity leads to a reduction in Ago3 and Aub protein levels and decreased piRNA levels with accumulation of retrotransposons in the ovary, demonstrating that arginine methylation is required for Ago3 stability in vivo. In vivo genetic loss-of-function of dPRMT5, western blotting for protein levels, immunofluorescence, biochemical detection of sDMA modifications Nature cell biology High 19377467
2009 Importin 8 (Imp8) interacts with AGO proteins including AGO3 and localizes to cytoplasmic processing bodies (P bodies). Imp8 is required for the recruitment of AGO protein complexes to a large set of target mRNAs, enabling efficient miRNA-guided gene silencing. Co-immunoprecipitation, immunofluorescence localization, knockdown of Imp8 followed by Ago2 immunoprecipitation-microarray analysis Cell Medium 19167051
2009 All four human AGO proteins (Ago1-4), including AGO3, show remarkably similar structural preferences for small-RNA duplexes during ATP-facilitated RISC loading: central mismatches promote loading and seed or 3'-mid mismatches facilitate strand unwinding. Human RISC assembly and dicing are uncoupled and ATP-dependent. In vitro RISC assembly assays with purified human AGO proteins, systematic duplex variant analysis, ATP dependency experiments Nature structural & molecular biology High 19966796
2009 GW182 family proteins TNRC6A, TNRC6B, and TNRC6C interact with all four human Argonaute proteins (AGO1-AGO4), including AGO3, through their N-terminal GW-repeat-containing regions. This interaction recruits TNRC6s to miRNA targets; the C-terminal silencing domain then mediates translational repression and mRNA degradation independently of AGO proteins. Co-immunoprecipitation, tethering assays, mutational analysis of GW repeats in human cells RNA (New York, N.Y.) Medium 19383768
2010 In Drosophila testes, AGO3 functions in the ping-pong amplification cycle together with Aubergine (Aub) for piRNA production from transposon transcripts. Unlike in ovaries, most AGO3-associated piRNAs corresponding to Su(Ste) and AT-chX loci are antisense-oriented and also found among Aub-associated piRNAs, suggesting a modified ping-pong mechanism at these loci. Genetic analysis showed AGO3 and Aub are mutually interdependent for piRNA accumulation. AGO3 immunoprecipitation followed by deep sequencing, piRNA pathway mutant analysis in Drosophila testes RNA (New York, N.Y.) High 20980675
2011 Drosophila AGO3 complexes with PAPI (Partner of PIWIs), a Tudor-domain protein, in the nuage. PAPI interacts with AGO3 via symmetrically dimethylated arginine residues on AGO3's N-terminal domain. In the absence of PAPI or dPRMT5, AGO3 is delocalized from the nuage and destabilized. AGO3 and PAPI also associate with the P-body components TRAL/ME31B complex in the nuage. Co-immunoprecipitation, immunofluorescence, genetic loss-of-function (papi mutants), western blotting in Drosophila ovaries Development (Cambridge, England) High 21447556
2012 Human AGO3 is required for the processing of retinoic acid-induced DR2 Alu transcripts into small RNAs (~28-65 nt) and for the subsequent degradation of target stem-cell mRNAs including Nanog mRNA, thereby regulating exit from the proliferative stem-cell state. AGO3-associated decapping complexes are recruited to target mRNAs in this pathway. AGO3 knockdown in human embryonic stem cells, RNA-seq, DICER inhibition, co-immunoprecipitation of AGO3-associated complexes Nature structural & molecular biology High 23064648
2012 Mouse AGO3 can load microRNAs efficiently in the absence of Ago1 and Ago2, demonstrating functional redundancy in miRNA loading. However, AGO3 interacts with a minority of microRNAs (<10%) in skin cells, proportional to its low abundance relative to Ago1 and Ago2. MicroRNAs are randomly sorted to individual Argonautes independently of slicer activity. Conditional knockout of Ago1 and Ago2 in mouse skin, shotgun proteomics quantification of Argonaute abundance, small RNA sequencing from individual AGO immunoprecipitates Genes & development High 22474261
2014 Drosophila AGO3 Slicer (endonuclease) activity is essential for piRNA amplification via the ping-pong cycle. AGO3 also inhibits homotypic Aub:Aub ping-pong in a Slicer-independent manner. Expression of an AGO3 Slicer mutant causes ectopic accumulation of Armitage (a primary piRNA pathway component) in nuage. AGO3 co-exists and interacts with Armitage in the mitochondrial fraction and acts with Zucchini to control dynamic Armitage localization between mitochondria and nuage in a Slicer-dependent fashion. Active-site mutagenesis (Slicer mutant), immunoprecipitation, subcellular fractionation, immunofluorescence, genetic epistasis in Drosophila germline The Journal of cell biology High 25049272
2015 Drosophila Krimper (Krimp), a Tudor-domain protein, directly interacts with piRNA-free AGO3 and promotes symmetrical dimethylarginine (sDMA) modification of AGO3, ensuring sense piRNA loading onto sDMA-modified AGO3. Krimp sequesters AGO3 within Krimp bodies in somatic cells (OSCs) where only primary piRNA pathway operates, preventing AGO3 from loading primary piRNAs and enforcing an antisense bias on the piRNA pool. Co-immunoprecipitation, aub mutant analysis, krimp-RNAi in ovarian somatic cells, immunofluorescence, piRNA sequencing Molecular cell High 26212455
2015 Drosophila Ago3 is recruited to perinuclear nuage through a piRNA-independent mechanism that relies on interaction with Krimper, a stable nuage component. Krimper interacts directly with both Aub and Ago3 to coordinate assembly of the ping-pong piRNA processing (4P) complex. sDMA modifications on Aub are required for Aub-Krimper interaction, but are dispensable for Ago3-Krimper binding. Genetic analysis of piRNA-free Ago3 mutants, in vitro binding assays, co-immunoprecipitation, FRAP, immunofluorescence in Drosophila ovaries Molecular cell High 26295961
2015 RNA cleavage by Drosophila Argonaute3 (AGO3) initiates production of most Piwi-bound piRNAs via phased piRNA biogenesis. The cardinal function of AGO3 (whose piRNA guides are predominantly sense transposon sequences) is to produce antisense piRNAs that direct transcriptional silencing by Piwi, rather than to make piRNAs guiding post-transcriptional silencing by Aubergine. Tudor protein Qin prevents Aubergine's cleavage products from becoming Piwi-bound piRNAs. An alternative slicing-independent pathway can also generate a subset of Piwi-bound piRNAs. piRNA sequencing, genetic epistasis (qin mutants, ago3 slicer mutants), biochemical analysis of piRNA populations in Drosophila ovarian germ cells Molecular cell High 26340424
2016 RNA helicase Spindle-E (Spn-E) is required to maintain AGO3 and Aub protein levels in Drosophila germline. Loss-of-function spn-E mutations cause a significant drop in AGO3 protein levels without suppressing ago3 transcription, indicating post-transcriptional regulation of AGO3 by Spn-E. spn-E mutants also show reduced ping-pong piRNA pairs from Su(Ste) transcripts in testes. Genetic loss-of-function (spn-E mutants), western blotting, small RNA sequencing, RT-PCR for transcript levels in Drosophila germline European journal of cell biology Medium 27320195
2017 In Aedes aegypti Aag2 cells, Ago3 and Piwi5 function as ping-pong partners for histone gene-derived piRNA biogenesis. Replication-dependent histone genes produce piRNAs from coding sequences in an Ago3- and Piwi5-dependent fashion, with these piRNAs dynamically expressed throughout the cell cycle. PIWI protein knockdown (Ago3 and Piwi5 RNAi), small RNA sequencing, cell cycle analysis in Aedes aegypti Aag2 cells Nucleic acids research Medium 28115625
2020 In Bombyx mori, secondary Siwi-piRISC production occurs at Ago3-positive nuage (Ago3 bodies) in an Ago3-dependent manner. Tudor protein Vreteno (Vret) interconnects unloaded Siwi and Ago3-piRISC through their sDMAs to facilitate secondary piRISC production. Upon Siwi depletion, Ago3 becomes phosphorylated and insolubilized in its piRISC form with cleaved RNAs and Vret, and Ago3 bodies enlarge; re-expression of Siwi restores normal morphology without new Ago3-piRISC supply, revealing a protective aggregation mechanism. Siwi depletion and re-expression experiments, co-immunoprecipitation, phosphorylation analysis, immunofluorescence, western blotting in Bombyx ovarian germ cells The EMBO journal High 32914505
2021 DEAD-box protein DDX43 facilitates Siwi-piRISC production by liberating cleaved RNAs from Bombyx Ago3-piRISC in an ATP hydrolysis-dependent manner. The helicase core of DDX43 mediates interaction with Ago3-piRISC and ATP hydrolysis, while its K-homology (KH) domain enhances ATPase activity independently of RNA binding. Both domains together are required for maximal RNA-binding activity. Biochemical interaction assays, ATP hydrolysis assays, domain deletion and mutational analysis, co-immunoprecipitation in Bombyx cells EMBO reports High 33555135
2021 Human AGO3 knockdown in cervical cancer cells inhibits cell proliferation and mobility, and exerts suppressive effects on cellular behaviors via inactivation of the Wnt/β-catenin signaling pathway, establishing AGO3 as a functional regulator of this pathway in cancer cells. AGO3 siRNA knockdown, cell proliferation assay, transwell migration/invasion assay, Wnt/β-catenin pathway reporter and western blotting Reproductive biology Low 33444963
2023 In Bombyx mori, the Gtsf1 homolog BmGtsf1L binds to piRNA-loaded BmAgo3 and co-localizes with BmAgo3 and BmVreteno in granules. The unstructured tail of BmGtsf1L directly interacts with a novel binding interface on the BmVreteno extended Tudor (eTudor) domain, distinct from its sDMA-binding interface. A single BmVreteno eTudor domain thereby provides two binding interfaces, interconnecting piRNA-loaded BmAgo3 and BmGtsf1L to facilitate piRNA amplification. Biochemical pull-down assays, AlphaFold structural modeling, atomistic molecular dynamics simulations, in vitro binding assays with mutational validation, co-immunoprecipitation, immunofluorescence The EMBO journal High 37984437
2025 Mouse AGO3 and AGO4, but not AGO2, localize to the sex chromatin of pachytene spermatocytes and are required for transcriptional silencing of XY-linked genes during Meiotic Sex Chromosome Inactivation (MSCI). Loss of AGO3 and AGO4 in Ago4^13-/- mice causes premature overexpression of spermiogenesis genes during prophase I, subfertility, and altered sperm morphology. AGO3 interacts with BRG1, a BAF complex subunit, and loss of AGO3/AGO4 results in increased BRG1 in spermatocytes, suggesting AGO3 aids in removing BRG1 from XY chromatin to achieve MSCI. Ago4^13-/- mouse genetic model, immunofluorescence localization to sex chromatin, co-immunoprecipitation of AGO3-BRG1, RNA-seq of meiotic transcriptomes, fertility and sperm morphology phenotyping bioRxivpreprint Medium

Source papers

Stage 0 corpus · 50 papers · ranked by NIH iCite citations
Year Title Journal Citations PMID
2012 Insights into RNA biology from an atlas of mammalian mRNA-binding proteins. Cell 1718 22658674
2004 Human Argonaute2 mediates RNA cleavage targeted by miRNAs and siRNAs. Molecular cell 1506 15260970
2002 Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. Proceedings of the National Academy of Sciences of the United States of America 1479 12477932
2011 Systematic and quantitative assessment of the ubiquitin-modified proteome. Molecular cell 1334 21906983
2008 Identification of host proteins required for HIV infection through a functional genomic screen. Science (New York, N.Y.) 1165 18187620
2015 The BioPlex Network: A Systematic Exploration of the Human Interactome. Cell 1118 26186194
2017 Architecture of the human interactome defines protein communities and disease networks. Nature 1085 28514442
2015 A human interactome in three quantitative dimensions organized by stoichiometries and abundances. Cell 1015 26496610
2012 The mRNA-bound proteome and its global occupancy profile on protein-coding transcripts. Molecular cell 973 22681889
2018 VIRMA mediates preferential m6A mRNA methylation in 3'UTR and near stop codon and associates with alternative polyadenylation. Cell discovery 829 29507755
2003 Complete sequencing and characterization of 21,243 full-length human cDNAs. Nature genetics 754 14702039
2021 Dual proteome-scale networks reveal cell-specific remodeling of the human interactome. Cell 705 33961781
2011 Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Briefings in bioinformatics 656 21873635
2002 The Argonaute family: tentacles that reach into RNAi, developmental control, stem cell maintenance, and tumorigenesis. Genes & development 650 12414724
2018 High-Density Proximity Mapping Reveals the Subcellular Organization of mRNA-Associated Granules and Bodies. Molecular cell 580 29395067
2021 Multilevel proteomics reveals host perturbations by SARS-CoV-2 and SARS-CoV. Nature 532 33845483
2022 OpenCell: Endogenous tagging for the cartography of human cellular organization. Science (New York, N.Y.) 432 35271311
2011 Global identification of modular cullin-RING ligase substrates. Cell 354 21963094
2003 Identification of eight members of the Argonaute family in the human genome. Genomics 330 12906857
2010 Dynamics of cullin-RING ubiquitin ligase network revealed by systematic quantitative proteomics. Cell 318 21145461
2009 ATP-dependent human RISC assembly pathways. Nature structural & molecular biology 295 19966796
2009 Importin 8 is a gene silencing factor that targets argonaute proteins to distinct mRNAs. Cell 281 19167051
2011 Toward an understanding of the protein interaction network of the human liver. Molecular systems biology 207 21988832
2018 An AP-MS- and BioID-compatible MAC-tag enables comprehensive mapping of protein interactions and subcellular localizations. Nature communications 201 29568061
2009 Arginine methylation of Piwi proteins catalysed by dPRMT5 is required for Ago3 and Aub stability. Nature cell biology 201 19377467
2015 A deep proteomics perspective on CRM1-mediated nuclear export and nucleocytoplasmic partitioning. eLife 198 26673895
2003 Short-interfering-RNA-mediated gene silencing in mammalian cells requires Dicer and eIF2C translation initiation factors. Current biology : CB 167 12526743
2005 Large-scale analysis of the human ubiquitin-related proteome. Proteomics 154 16196087
2012 Quantitative functions of Argonaute proteins in mammalian development. Genes & development 142 22474261
2022 Human transcription factor protein interaction networks. Nature communications 123 35140242
2009 The C-terminal domains of human TNRC6A, TNRC6B, and TNRC6C silence bound transcripts independently of Argonaute proteins. RNA (New York, N.Y.) 119 19383768
2015 Slicing and Binding by Ago3 or Aub Trigger Piwi-Bound piRNA Production by Distinct Mechanisms. Molecular cell 111 26340424
2015 Aub and Ago3 Are Recruited to Nuage through Two Mechanisms to Form a Ping-Pong Complex Assembled by Krimper. Molecular cell 97 26295961
2010 Biogenesis pathways of piRNAs loaded onto AGO3 in the Drosophila testis. RNA (New York, N.Y.) 97 20980675
2011 PAPI, a novel TUDOR-domain protein, complexes with AGO3, ME31B and TRAL in the nuage to silence transposition. Development (Cambridge, England) 84 21447556
2012 DICER- and AGO3-dependent generation of retinoic acid-induced DR2 Alu RNAs regulates human stem cell proliferation. Nature structural & molecular biology 70 23064648
2016 Arabidopsis AGO3 predominantly recruits 24-nt small RNAs to regulate epigenetic silencing. Nature plants 63 27243648
2015 Krimper Enforces an Antisense Bias on piRNA Pools by Binding AGO3 in the Drosophila Germline. Molecular cell 61 26212455
2014 AGO3 Slicer activity regulates mitochondria-nuage localization of Armitage and piRNA amplification. The Journal of cell biology 45 25049272
2017 Histone-derived piRNA biogenesis depends on the ping-pong partners Piwi5 and Ago3 in Aedes aegypti. Nucleic acids research 35 28115625
2014 Five children with deletions of 1p34.3 encompassing AGO1 and AGO3. European journal of human genetics : EJHG 26 25271087
2015 Identification of AGO3-associated miRNAs and computational prediction of their targets in the green alga Chlamydomonas reinhardtii. Genetics 25 25769981
2016 RNA helicase Spn-E is required to maintain Aub and AGO3 protein levels for piRNA silencing in the germline of Drosophila. European journal of cell biology 15 27320195
2020 Siwi levels reversibly regulate secondary piRISC biogenesis by affecting Ago3 body morphology in Bombyx mori. The EMBO journal 14 32914505
2021 DEAD-box polypeptide 43 facilitates piRNA amplification by actively liberating RNA from Ago3-piRISC. EMBO reports 13 33555135
2023 An extended Tudor domain within Vreteno interconnects Gtsf1L and Ago3 for piRNA biogenesis in Bombyx mori. The EMBO journal 8 37984437
2021 Argonaute 3 (AGO3) promotes malignancy potential of cervical cancer via regulation of Wnt/β-catenin signaling pathway. Reproductive biology 6 33444963
2011 [The nucleotide sequence features of the mature microRNA seem to be responsible for the affinity to human Ago2 AND Ago3 proteins]. Molekuliarnaia biologiia 4 21634124
2017 Dicer1, AGO3, and AGO4 microRNA machinery genes are differentially expressed in developing female reproductive organs and overexpressed in cancerous ovaries of chickens. Journal of animal science 3 29293730
2025 Global identification of AGO3-RNA interactions reveals targets of small RNA-mediated gene regulation in Chlamydomonas reinhardtii. Plant & cell physiology 0 40244707