AGO1 is the principal Arabidopsis Argonaute effector of miRNA- and siRNA-guided post-transcriptional gene silencing. It binds small-RNA guides and complementary target RNAs, using its PIWI domain to cleave targets and also participating in translational repression. AGO1 acts in cytoplasmic and ER-associated silencing complexes and can enter nuclear and cytoplasmic condensate-associated pools. It participates in secondary-siRNA production and antiviral RNA interference, while its regulation of endogenous transcripts controls leaf and meristem development, auxin responses and immunity.
| GO Term | Evidence | Action | Reason |
|---|---|---|---|
| GO:0003676 nucleic acid binding | IEA GO_REF:0000002 | MODIFY | Summary: AGO1 is a guide-RNA-bound Argonaute, but nucleic acid binding is too broad for its curated role. Reason: The InterPro nucleic-acid/RNA-binding inference is sound, but AGO1 directly binds miRNA and siRNA guides (PMID:16081530). Refine the binding assertion to these ligand-specific functions; catalytic RNA cleavage is separately represented and should not be substituted for a binding activity. Proposed replacements: miRNA binding siRNA binding |
| GO:0003723 RNA binding | IEA GO_REF:0000002 | MODIFY | Summary: AGO1 binds RNA as a guide-loaded RISC effector, especially miRNAs and siRNAs. Reason: The InterPro nucleic-acid/RNA-binding inference is sound, but AGO1 directly binds miRNA and siRNA guides (PMID:16081530). Refine the binding assertion to these ligand-specific functions; catalytic RNA cleavage is separately represented and should not be substituted for a binding activity. Proposed replacements: miRNA binding siRNA binding |
| GO:0005737 cytoplasm | IEA GO_REF:0000044 | ACCEPT | Summary: AGO1 has documented cytoplasm localization in Arabidopsis. Reason: AGO1 localization is dynamic; both cytoplasmic PTGS and nuclear/nucleocytoplasmic contexts are supported. |
| GO:0010016 shoot system morphogenesis | IEA GO_REF:0000117 | KEEP AS NON CORE | Summary: AGO1 mutants or genetic interactions affect shoot system morphogenesis. Reason: The ARBA developmental inference agrees with experimentally observed defects in shoot architecture, axillary meristems and leaf organs (PMID:9427751). Retain as non-core developmental consequences of small-RNA-mediated regulation. |
| GO:0051607 defense response to virus | IEA GO_REF:0000117 | MODIFY | Summary: AGO1 executes antiviral RNA interference through viral-siRNA-guided silencing. Reason: The electronic defense annotation is supported by ago1 virus hypersensitivity and AGO1 loading of viral siRNAs in PMID:11910010 and PMID:17158744. The RNAi-specific antiviral term captures the demonstrated mechanism more precisely. Proposed replacements: RNAi-mediated antiviral immune response |
| GO:0005515 protein binding | IPI PMID:23622241 MicroRNAs inhibit the translation of target mRNAs on the end... | REMOVE | Summary: AGO1 associates with the ER, where miRNA-mediated translational repression occurs. Reason: The study reports AGO1-AMP1 co-immunoprecipitation at the ER, but explicitly allows shared membrane proximity rather than a common protein complex as an explanation. Remove generic protein binding as uninformative; retain the ER/translational-silencing evidence in the functional synthesis. Do not infer direct AMP1 binding or a new catalytic activity from co-IP. Supporting Evidence: PMID:23622241 AGO1 is a peripheral ER membrane protein that is also possibly associated with the rough ER. PMID:23622241 the observed co-IP between AMP1 and AGO1 (Fig 5A, B) could be attributable to the two proteins being in close proximity on the same membrane rather than being in the same protein complex. |
| GO:0005515 protein binding | IPI PMID:38446745 ARGONAUTE1-binding Tudor domain proteins function in small i... | REMOVE | Summary: AGO1 interacts with PDS5C/E in a pathway supporting 24-nt siRNA production for RdDM. Reason: Remove the uninformative generic protein-binding annotation, not the reported physical association. This interaction evidence does not by itself establish a distinct, more specific molecular function of AGO1; in particular, do not transfer the partner's catalytic or regulatory activity to AGO1. Supporting Evidence: PMID:38446745 Proteome and imaging analyses revealed that PDS5C/E interact with AGO1. |
| GO:0035278 miRNA-mediated gene silencing by inhibition of translation | IDA PMID:34192539 Ribosome stalling caused by the Argonaute-microRNA-SGS3 comp... | ACCEPT | Summary: An Argonaute-miRNA-SGS3 complex stalls ribosomes and couples translational regulation to secondary-siRNA production. Reason: The source reports miRNA-Argonaute-SGS3-mediated ribosome stalling rather than simple target-mRNA decay. This supports a core translational-silencing mechanism, corroborated by the independent AGO1/ER study PMID:23622241. The cache remains abstract-only for the specific stalling experiments. Supporting Evidence: PMID:34192539 ribosome stalling caused by the Argonaute-microRNA-SGS3 complex regulates production of secondary small interfering RNAs (siRNAs) in plants. PMID:23622241 AGO1 is a peripheral ER membrane protein that is also possibly associated with the rough ER. |
| GO:0036464 cytoplasmic ribonucleoprotein granule | IDA PMID:36640363 Phase separation of SGS3 drives siRNA body formation and pro... | ACCEPT | Summary: AGO1 is recruited into SGS3-containing cytoplasmic siRNA bodies. Reason: The full article for PMID:36640363 was obtained as a published PDF and Figure 6B/C directly shows AGO1 recruitment to SGS3 condensates and BiFC in Arabidopsis protoplasts. The prior rejection based on an SGS3-focused abstract was incorrect. Independent heat-stress experiments in PMID:38384836 corroborate AGO1 localization to cytoplasmic ribonucleoprotein condensates. Source-specific PDF evidence and retrieval provenance are recorded in AGO1-notes.md. Supporting Evidence: PMID:38384836 AGO1 protein accumulation in cytosolic condensates where it colocalizes with components of siRNA bodies and of stress granules. |
| GO:0010267 ta-siRNA processing | IMP PMID:15469823 Endogenous trans-acting siRNAs regulate the accumulation of ... | ACCEPT | Summary: AGO1 participates in the biogenesis of endogenous trans-acting siRNAs. Reason: The original experiments require AGO1 for endogenous trans-acting siRNA accumulation. Together with the Argonaute-miRNA-SGS3 mechanism in PMID:34192539, this places AGO1 directly in secondary-siRNA production upstream of RDR6/Dicer processing. It does not assign Dicer activity to AGO1. Supporting Evidence: PMID:15469823 they require components of the cosuppression pathway (RDR6 and SGS3) and also components of the microRNA (miRNA) pathway (AGO1, DCL1, HEN1, and HYL1) PMID:34192539 ribosome stalling caused by the Argonaute-microRNA-SGS3 complex regulates production of secondary small interfering RNAs (siRNAs) in plants. |
| GO:0035198 miRNA binding | IPI PMID:35137215 CONSTITUTIVE EXPRESSER OF PATHOGENESIS-RELATED GENES 5 is an... | ACCEPT | Summary: AGO1 miRNA binding is a well-established core function; the cached CPR5 abstract does not detail the AGO1 assays, but the curator had the full text. Reason: AGO1 miRNA binding is directly demonstrated by PMID:16081530 and PMID:30181559. The original reference's AGO1-specific assay is not exposed in its cached abstract; retain the independently established function and defer to the source curator without claiming an uninspected experiment was performed. Supporting Evidence: PMID:16081530 AGO1 is physically associated with miRNAs, transacting siRNAs, and transgene-derived siRNAs PMID:30181559 SDN1 interacts with the AGO1 PAZ domain in an RNA-independent manner in vitro, enabling it to act on AGO1-bound microRNAs. |
| GO:0035197 siRNA binding | IDA PMID:16081530 Arabidopsis ARGONAUTE1 is an RNA Slicer that selectively rec... | ACCEPT | Summary: AGO1 directly associates with miRNAs and several siRNA classes. Reason: siRNA binding is a specific molecular-function annotation for AGO1 guide-RNA sorting and RISC function. Supporting Evidence: PMID:16081530 AGO1 is physically associated with miRNAs, transacting siRNAs, and transgene-derived siRNAs |
| GO:0035198 miRNA binding | IDA PMID:16081530 Arabidopsis ARGONAUTE1 is an RNA Slicer that selectively rec... | ACCEPT | Summary: AGO1 directly associates with miRNAs and several siRNA classes. Reason: miRNA binding is a specific molecular-function annotation for AGO1 guide-RNA sorting and RISC function. Supporting Evidence: PMID:16081530 AGO1 is physically associated with miRNAs, transacting siRNAs, and transgene-derived siRNAs |
| GO:0003729 mRNA binding | HDA PMID:27729395 In Planta Determination of the mRNA-Binding Proteome of Arab... | ACCEPT | Summary: AGO1 contacts target mRNAs as part of guide-directed RISC target recognition. Reason: Target-mRNA recognition is a direct step in AGO1 guide-directed silencing, not merely a downstream phenotype. Leaf interactome capture explicitly identifies AGO1 (PMID:32344669), and the target-cleavage assay in PMID:16081530 independently establishes engagement of target RNA. The seedling-proteome source table is not exposed in its abstract. Supporting Evidence: PMID:32344669 we identified the well-characterised RBPs AGO1 and AGO2, which are involved in RNAi PMID:16081530 It mediates the in vitro cleavage of a mir165 target RNA |
| GO:0003729 mRNA binding | IDA PMID:32344669 Discovering the RNA-Binding Proteome of Plant Leaves with an... | ACCEPT | Summary: RNA interactome capture directly detects AGO1 among leaf RNA-binding proteins. Reason: Target-mRNA recognition is a direct step in AGO1 guide-directed silencing, not merely a downstream phenotype. Leaf interactome capture explicitly identifies AGO1 (PMID:32344669), and the target-cleavage assay in PMID:16081530 independently establishes engagement of target RNA. The seedling-proteome source table is not exposed in its abstract. Supporting Evidence: PMID:32344669 we identified the well-characterised RBPs AGO1 and AGO2, which are involved in RNAi PMID:16081530 It mediates the in vitro cleavage of a mir165 target RNA |
| GO:0005634 nucleus | HDA PMID:28887381 Global Analysis of Membrane-associated Protein Oligomerizati... | ACCEPT | Summary: AGO1 has documented nucleus localization in Arabidopsis. Reason: Nuclear localization is supported in the AGO/viral-2b interaction study PMID:22247253. Retain this established compartment with source-curator deference where the original source-specific imaging or proteomic table is not exposed in the cache. Do not equate viral-induced redistribution with constitutive residence in the nucleolus. Supporting Evidence: PMID:22247253 the 2b-AGO interactions in vivo also required the nucleolar targeting of 2b and had the potential to redistribute both the 2b and AGO proteins in nucleus. |
| GO:0005515 protein binding | IPI PMID:28463111 RISC-interacting clearing 3'- 5' exoribonucleases (RICEs) de... | REMOVE | Summary: AGO1 associates with RICE cofactors that clear uridylated cleavage fragments. Reason: Remove the uninformative generic protein-binding annotation, not the reported physical association. This interaction evidence does not by itself establish a distinct, more specific molecular function of AGO1; in particular, do not transfer the partner's catalytic or regulatory activity to AGO1. Supporting Evidence: PMID:28463111 We showed that RICE1 and its genetic paralog, RICE2, interacted with both AGO10 and AGO1 |
| GO:0005737 cytoplasm | IDA PMID:28463111 RISC-interacting clearing 3'- 5' exoribonucleases (RICEs) de... | ACCEPT | Summary: AGO1 associates with RICE cofactors that clear uridylated cleavage fragments. Reason: Cytoplasmic AGO localization is directly visualized in the RICE cofactor study PMID:28463111 and is consistent with ER-associated AGO1 in PMID:23622241. Retain the established location and defer to original curators for source-specific experiments not exposed in individual abstracts. Supporting Evidence: PMID:28463111 co-localization of RICE1-CFP and YFP-AGOs was observed predominantly in cytoplasm. |
| GO:0030154 cell differentiation | IGI PMID:18653559 Vascular signalling mediated by ZWILLE potentiates WUSCHEL f... | KEEP AS NON CORE | Summary: AGO1 contributes to embryonic stem-cell signaling in a sequence distinct from ZLL/AGO10. Reason: Retain this experimentally supported developmental or physiological process as non-core context for AGO1-mediated small-RNA regulation. Supporting Evidence: PMID:18653559 WUS-dependent OC signalling to the stem cells is promoted by AGO1 and subsequently maintained by a provascular ZLL-dependent signalling pathway. |
| GO:0035198 miRNA binding | IPI PMID:30181559 Structural and biochemical insights into small RNA 3' end tr... | ACCEPT | Summary: AGO1-bound miRNAs are accessible to SDN1-mediated trimming. Reason: miRNA binding is a specific molecular-function annotation for AGO1 guide-RNA sorting and RISC function. Supporting Evidence: PMID:30181559 SDN1 interacts with the AGO1 PAZ domain in an RNA-independent manner in vitro, enabling it to act on AGO1-bound microRNAs. |
| GO:0005737 cytoplasm | ISM GO_REF:0000122 | ACCEPT | Summary: AGO1 has documented cytoplasm localization in Arabidopsis. Reason: AGO1 localization is dynamic; both cytoplasmic PTGS and nuclear/nucleocytoplasmic contexts are supported. |
| GO:0005515 protein binding | IPI PMID:29941559 Degradation of unmethylated miRNA/miRNA*s by a DEDDy-type 3'... | REMOVE | Summary: AGO1 interacts with ATRM2 in small-RNA surveillance. Reason: Remove the uninformative generic protein-binding annotation, not the reported physical association. This interaction evidence does not by itself establish a distinct, more specific molecular function of AGO1; in particular, do not transfer the partner's catalytic or regulatory activity to AGO1. Supporting Evidence: PMID:29941559 Finally, we show that ATRM2 colocalizes and physically interacts with Argonaute 1 (AGO1). |
| GO:0035198 miRNA binding | IDA PMID:16998468 Distinct catalytic and non-catalytic roles of ARGONAUTE4 in ... | ACCEPT | Summary: AGO1 miRNA binding is a well-established core function; the AGO4-titled paper likely also assayed AGO1-bound small RNAs, and the curator had the full text. Reason: AGO1 miRNA binding is directly demonstrated by PMID:16081530 and PMID:30181559. The original reference's AGO1-specific assay is not exposed in its cached abstract; retain the independently established function and defer to the source curator without claiming an uninspected experiment was performed. Supporting Evidence: PMID:16081530 AGO1 is physically associated with miRNAs, transacting siRNAs, and transgene-derived siRNAs PMID:30181559 SDN1 interacts with the AGO1 PAZ domain in an RNA-independent manner in vitro, enabling it to act on AGO1-bound microRNAs. |
| GO:0051607 defense response to virus | IDA PMID:26023161 Functional and Genetic Analysis Identify a Role for Arabidop... | KEEP AS NON CORE | Summary: AGO1 antiviral capacity against suppressor-deficient PVX does not imply that it restricts wild-type PVX like AGO2/5. Reason: The source supports an antiviral RNA-silencing capacity for AGO1, but AGO2/AGO5 are emphasized for wild-type PVX restriction; treat this as a non-core pathway output of AGO1 small-RNA effector activity. Supporting Evidence: PMID:26023161 all Arabidopsis AGO proteins have the potential to target PVX lacking its viral suppressor of RNA silencing (VSR), P25, but that only AGO2 and AGO5 are able to target wild-type PVX. |
| GO:0005634 nucleus | IDA PMID:22247253 Suppression of Arabidopsis ARGONAUTE1-mediated slicing, tran... | ACCEPT | Summary: The viral 2b-AGO interaction can alter nuclear distribution of AGO proteins. Reason: Nuclear localization is supported in the AGO/viral-2b interaction study PMID:22247253. Retain this established compartment with source-curator deference where the original source-specific imaging or proteomic table is not exposed in the cache. Do not equate viral-induced redistribution with constitutive residence in the nucleolus. Supporting Evidence: PMID:22247253 the 2b-AGO interactions in vivo also required the nucleolar targeting of 2b and had the potential to redistribute both the 2b and AGO proteins in nucleus. |
| GO:0005737 cytoplasm | IDA PMID:22247253 Suppression of Arabidopsis ARGONAUTE1-mediated slicing, tran... | ACCEPT | Summary: The viral 2b-AGO interaction can alter nuclear distribution of AGO proteins. Reason: Cytoplasmic AGO localization is directly visualized in the RICE cofactor study PMID:28463111 and is consistent with ER-associated AGO1 in PMID:23622241. Retain the established location and defer to original curators for source-specific experiments not exposed in individual abstracts. Supporting Evidence: PMID:28463111 co-localization of RICE1-CFP and YFP-AGOs was observed predominantly in cytoplasm. |
| GO:0009955 adaxial/abaxial pattern specification | IMP PMID:22623415 The microRNA pathway genes AGO1, HEN1 and HYL1 participate i... | KEEP AS NON CORE | Summary: ago1 and other miRNA-pathway mutants reveal roles in leaf polarity and patterning. Reason: Retain this experimentally supported developmental or physiological process as non-core context for AGO1-mediated small-RNA regulation. Supporting Evidence: PMID:22623415 The morphological and histological characterization of these mutants and of dicer-like1-9 indicates that small RNAs participate in the proximal-distal and adaxial-abaxial patterning of leaves |
| GO:0010305 leaf vascular tissue pattern formation | IMP PMID:22623415 The microRNA pathway genes AGO1, HEN1 and HYL1 participate i... | KEEP AS NON CORE | Summary: ago1 leaf vasculature is abnormal. Reason: The original mutant study explicitly identifies abnormal ago1 leaf vasculature, supporting non-core venation patterning. Supporting Evidence: PMID:22623415 The abnormal vasculature of ago1 and hyl1 leaves also suggests a role for AGO1 and HYL1 in venation patterning. |
| GO:0010589 leaf proximal/distal pattern formation | IMP PMID:22623415 The microRNA pathway genes AGO1, HEN1 and HYL1 participate i... | KEEP AS NON CORE | Summary: ago1 and other miRNA-pathway mutants reveal roles in leaf polarity and patterning. Reason: Retain this experimentally supported developmental or physiological process as non-core context for AGO1-mediated small-RNA regulation. Supporting Evidence: PMID:22623415 The morphological and histological characterization of these mutants and of dicer-like1-9 indicates that small RNAs participate in the proximal-distal and adaxial-abaxial patterning of leaves |
| GO:0005515 protein binding | IPI PMID:22940249 Ago hook and RNA helicase motifs underpin dual roles for SDE... | REMOVE | Summary: AGO1 associates with the GW-repeat-containing helicase SDE3 in silencing complexes. Reason: Remove the uninformative generic protein-binding annotation, not the reported physical association. This interaction evidence does not by itself establish a distinct, more specific molecular function of AGO1; in particular, do not transfer the partner's catalytic or regulatory activity to AGO1. Supporting Evidence: PMID:22940249 SDE3 is present with the PTGS effectors AGO1 and AGO2 in higher-order protein complexes owing to a specialized GW-repeat-containing C-terminal domain. |
| GO:0005515 protein binding | IPI PMID:17869109 The Polerovirus F box protein P0 targets ARGONAUTE1 to suppr... | REMOVE | Summary: The viral suppressor P0 associates with AGO1 and promotes its destabilization. Reason: Remove the uninformative generic protein-binding annotation, not the reported physical association. This interaction evidence does not by itself establish a distinct, more specific molecular function of AGO1; in particular, do not transfer the partner's catalytic or regulatory activity to AGO1. Supporting Evidence: PMID:17869109 Finally, we provide evidence that P0 physically interacts with AGO1. |
| GO:0045087 innate immune response | IMP PMID:20164210 Identification of microRNAs involved in pathogen-associated ... | KEEP AS NON CORE | Summary: AGO1 contributes to PAMP-triggered immunity through miRNA pathways. Reason: Retain this experimentally supported developmental or physiological process as non-core context for AGO1-mediated small-RNA regulation. Supporting Evidence: PMID:20164210 the Arabidopsis (Arabidopsis thaliana) miRNA effector protein, Argonaute1 (AGO1), is required for a number of PTI responses including PAMP-induced callose deposition, gene expression, and seedling growth inhibition. |
| GO:0009733 response to auxin | IGI PMID:15829601 Auxin and light control of adventitious rooting in Arabidops... | KEEP AS NON CORE | Summary: AGO1-dependent root development is linked to auxin homeostasis and light responses. Reason: Retain this experimentally supported developmental or physiological process as non-core context for AGO1-mediated small-RNA regulation. Supporting Evidence: PMID:15829601 The defect in adventitious rooting observed in ago1 correlated with light hypersensitivity and the deregulation of auxin homeostasis specifically in the apical part of the seedlings. |
| GO:0009850 auxin metabolic process | IGI PMID:15829601 Auxin and light control of adventitious rooting in Arabidops... | KEEP AS NON CORE | Summary: ago1 alters auxin homeostasis. Reason: The original study measured reduced free IAA and IAA conjugates and altered GH3 expression in ago1. Retain a non-core auxin-metabolic effect; this does not imply AGO1 directly catalyzes auxin metabolism. Supporting Evidence: PMID:15829601 a clear reduction in endogenous levels of free indoleacetic acid (IAA) and IAA conjugates was shown. |
| GO:0010218 response to far red light | IGI PMID:15829601 Auxin and light control of adventitious rooting in Arabidops... | KEEP AS NON CORE | Summary: AGO1 contributes to phyA-dependent far-red responses. Reason: The indexed primary article reports phyA epistasis to ago1 in far-red light. This source-specific genetic observation supports KEEP_AS_NON_CORE. The local full-text extraction omits that result, so the accessible abstract snippet supports general light/auxin context only; retrieval details are in AGO1-notes.md. Supporting Evidence: PMID:15829601 The defect in adventitious rooting observed in ago1 correlated with light hypersensitivity and the deregulation of auxin homeostasis specifically in the apical part of the seedlings. |
| GO:0005634 nucleus | IDA PMID:17442570 Identification of nuclear dicing bodies containing proteins ... | ACCEPT | Summary: AGO1 nuclear localization is well established and consistent with the accepted sibling rows; the abstract-only cache does not show the specific localization data, but the curator had the full text. Reason: Nuclear localization is supported in the AGO/viral-2b interaction study PMID:22247253. Retain this established compartment with source-curator deference where the original source-specific imaging or proteomic table is not exposed in the cache. Do not equate viral-induced redistribution with constitutive residence in the nucleolus. Supporting Evidence: PMID:22247253 the 2b-AGO interactions in vivo also required the nucleolar targeting of 2b and had the potential to redistribute both the 2b and AGO proteins in nucleus. |
| GO:0005737 cytoplasm | IDA PMID:17442570 Identification of nuclear dicing bodies containing proteins ... | ACCEPT | Summary: AGO1 cytoplasmic localization is well established and consistent with the accepted sibling rows; the abstract-only cache does not show the specific localization data, but the curator had the full text. Reason: Cytoplasmic AGO localization is directly visualized in the RICE cofactor study PMID:28463111 and is consistent with ER-associated AGO1 in PMID:23622241. Retain the established location and defer to original curators for source-specific experiments not exposed in individual abstracts. Supporting Evidence: PMID:28463111 co-localization of RICE1-CFP and YFP-AGOs was observed predominantly in cytoplasm. |
| GO:0009616 RNAi-mediated antiviral immune response | IDA PMID:17158744 Cucumber mosaic virus-encoded 2b suppressor inhibits Arabido... | ACCEPT | Summary: AGO1 loads viral siRNAs during the antiviral response to CMV. Reason: RNAi-mediated antiviral immune response is the specific immune process that matches AGO1 mechanism. Supporting Evidence: PMID:17158744 AGO1 recruits virus-derived small interfering RNAs (siRNAs) in vivo |
| GO:0048830 adventitious root development | IMP PMID:15829601 Auxin and light control of adventitious rooting in Arabidops... | KEEP AS NON CORE | Summary: AGO1-dependent root development is linked to auxin homeostasis and light responses. Reason: Retain this experimentally supported developmental or physiological process as non-core context for AGO1-mediated small-RNA regulation. Supporting Evidence: PMID:15829601 The defect in adventitious rooting observed in ago1 correlated with light hypersensitivity and the deregulation of auxin homeostasis specifically in the apical part of the seedlings. |
| GO:0004521 RNA endonuclease activity | IDA PMID:16081530 Arabidopsis ARGONAUTE1 is an RNA Slicer that selectively rec... | MODIFY | Summary: AGO1 has PIWI-dependent target-RNA slicer activity. Reason: The term is correct but more general than the evidence. The paper shows that immunopurified AGO1 loaded with endogenous miR165 cleaves the paired PHV target mRNA at the predicted site, which is GO:0090624 endoribonuclease activity, cleaving miRNA-paired mRNA, an is_a descendant of RNA endonuclease activity. The same term is used for the AGO1 annoton in the plant miRNA biogenesis module. Proposed replacements: endoribonuclease activity, cleaving miRNA-paired mRNA Supporting Evidence: PMID:16081530 We also show that AGO1 has Slicer activity. PMID:16081530 the WT protein was correctly programmed by endogenous miR165 as it cleaved the PHV RNA in vitro |
| GO:0035195 miRNA-mediated post-transcriptional gene silencing | IEP PMID:15131082 The action of ARGONAUTE1 in the miRNA pathway and its regula... | ACCEPT | Summary: AGO1 is required for efficient repression of miRNA-target mRNAs. Reason: The original ago1 mutant study shows overaccumulation of miRNA cleavage targets, directly supporting the core miRNA-mediated post-transcriptional silencing process. Supporting Evidence: PMID:15131082 Arabidopsis ago1 mutants have increased accumulation of mRNAs known to be targeted for cleavage by miRNAs. |
| GO:0035195 miRNA-mediated post-transcriptional gene silencing | IMP PMID:15131082 The action of ARGONAUTE1 in the miRNA pathway and its regula... | ACCEPT | Summary: AGO1 is required for efficient repression of miRNA-target mRNAs. Reason: The original ago1 mutant study shows overaccumulation of miRNA cleavage targets, directly supporting the core miRNA-mediated post-transcriptional silencing process. Supporting Evidence: PMID:15131082 Arabidopsis ago1 mutants have increased accumulation of mRNAs known to be targeted for cleavage by miRNAs. |
| GO:0005737 cytoplasm | TAS PMID:9427751 AGO1 defines a novel locus of Arabidopsis controlling leaf d... | ACCEPT | Summary: ago1 mutants have severe leaf-blade and organ-development defects. Reason: Cytoplasmic AGO localization is directly visualized in the RICE cofactor study PMID:28463111 and is consistent with ER-associated AGO1 in PMID:23622241. Retain the established location and defer to original curators for source-specific experiments not exposed in individual abstracts. Supporting Evidence: PMID:28463111 co-localization of RICE1-CFP and YFP-AGOs was observed predominantly in cytoplasm. |
| GO:0009965 leaf morphogenesis | IMP PMID:9427751 AGO1 defines a novel locus of Arabidopsis controlling leaf d... | KEEP AS NON CORE | Summary: ago1 mutants have severe leaf-blade and organ-development defects. Reason: Retain this experimentally supported developmental or physiological process as non-core context for AGO1-mediated small-RNA regulation. Supporting Evidence: PMID:9427751 Rosette leaves lack a leaf blade but still show adaxial/abaxial differentiation. |
| GO:0016441 post-transcriptional gene silencing | IEP PMID:11910010 Fertile hypomorphic ARGONAUTE (ago1) mutants impaired in pos... | ACCEPT | Summary: Hypomorphic ago1 mutations impair post-transcriptional gene silencing. Reason: Hypomorphic ago1 mutants are defective in PTGS even when fertile, separating the silencing defect from severe developmental abnormalities. Retain core post-transcriptional silencing. Supporting Evidence: PMID:11910010 We show that these hypomorphic ago1 mutants are defective for PTGS, like null sgs2, sgs3, and ago1 mutants |
| GO:0005783 endoplasmic reticulum | IDA PMID:23622241 MicroRNAs inhibit the translation of target mRNAs on the end... | NEW | Summary: AGO1 is a peripheral ER-associated protein. Reason: The cited study directly visualizes AGO1 colocalization with ER markers and tests membrane association by fractionation. This directly supported compartment is absent from the seeded annotations. Supporting Evidence: PMID:23622241 AGO1 is a peripheral ER membrane protein that is also possibly associated with the rough ER. |
| GO:0030371 translation repressor activity | IC PMID:34192539 Ribosome stalling caused by the Argonaute-microRNA-SGS3 comp... | NEW | Summary: AGO1-guide complexes mediate target-dependent translational repression. Reason: Infer translation repressor activity from the Argonaute-miRNA-SGS3 ribosome-stalling process and ER-associated miRNA repression. Target specificity is supplied by the bound small-RNA guide; this assignment does not require AGO1 to recognize an mRNA cis-regulatory element independently of that guide. Guide-mediated targeting and the ER context are separately captured by the process and localization annotations. Supporting Evidence: PMID:23622241 AGO1 is a peripheral ER membrane protein that is also possibly associated with the rough ER. PMID:34192539 ribosome stalling caused by the Argonaute-microRNA-SGS3 complex regulates production of secondary small interfering RNAs (siRNAs) in plants. PMID:23622241 miRNAs inhibit the translation of target RNAs on the ER. |
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Download this section (compressed HTML)Q: How do AGO1 target cleavage, translational repression and secondary-siRNA production partition between ER-associated and siRNA-body pools?
Q: Which viral contexts allow AGO1 to restrict infection despite viral suppressors, given the distinction between CMV and suppressor-competent PVX?
Q: Can the source-specific AGO1 RNA-binding and localization experiments in PMID:35137215, PMID:16998468, PMID:17442570 and the proteomics source tables be made available for direct inspection?
Experiment: Measure guide loading, cleavage and translation of defined targets in matched cytosolic, ER-associated and heat-induced condensate fractions, with localization and fraction-purity controls.
Hypothesis: AGO1 condensate recruitment alters spatial organization more strongly than its immediate catalytic activity.
Type: AGO1 compartment-specific activity measurements
Experiment: Compare defined AGO1-guide-target complexes in cleavage and translation assays with and without SGS3, separating target slicing from effects on secondary-siRNA production.
Hypothesis: Guide and target configuration distinguishes direct cleavage from SGS3-dependent ribosome stalling and secondary-siRNA initiation.
Type: AGO1 guide and target reconstitution
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