DICER1

Summary: The transferred transcriptional repression claim is not resolved by the inspected mouse experiments.

Reason: The Q8R418 donor traces to mouse Schwann-cell Dicer deletion studies (PMIDs 20463238 and 20805985). They measure altered transcription-factor mRNA/protein abundance and differentiation after loss of miRNA processing. GO:0000122 specifically concerns the rate or extent of RNA polymerase II transcription; these readouts do not distinguish transcriptional change from RNA stability. The donor and orthology are genuine, but this term-level mechanism remains unresolved. This is not a claim that the mouse annotation or human transcriptional regulation is false.

Summary: The target binds double-stranded RNA substrates.

Reason: IPR011545 is a genuine target helicase-like domain match, but its nucleic-acid-binding mapping is broad. Direct human Dicer dsRNA-binding experiments establish a more informative target function. This refinement does not infer ATP hydrolysis or DNA binding from the fold.

Proposed replacements: double-stranded RNA binding

Summary: Conserved RNA binding can be specified as double-stranded RNA binding.

Reason: The target lies below the experimentally grounded PAINT node PTN000383725. Direct human binding assays and the conserved RNA-processing architecture support the narrower dsRNA-binding term. The target appearing among the descendant evidence is legitimate experimental grounding, not circularity.

Proposed replacements: double-stranded RNA binding

Summary: The PAZ/dsRNA-binding architecture supports specific RNA-substrate binding.

Reason: The official IPR003100 PAZ and IPR044441 dsRNA-binding-domain matches occur in the displayed human sequence. Purified human Dicer binds dsRNA and pre-miRNA substrates. Use the established dsRNA-binding function instead of the broad RNA-binding parent; no activity is assigned to every alternative product from domain presence alone.

Proposed replacements: double-stranded RNA binding

Summary: Dicer directly binds double-stranded RNA.

Reason: The original separates binding from cleavage using purified human Dicer and a C-terminal dsRNA-binding domain. The historical 1912-aa clone produced in Sf9 cells is target evidence but is not assumed to be an exact sequence match to the current 1922-aa product. Binding contributes to the integrated RNase III mechanism.

Summary: Double-stranded RNA recognition is consistent with Dicer-dependent RMRP-derived small-RNA production.

Reason: The original human-cell knockdowns reduce RMRP-derived siRNAs and distinguish Dicer processing from TERT-associated RNA synthesis. This perturbation is not itself a binding-affinity measurement; independent purified human Dicer dsRNA binding grounds the molecular function. The 2025 correction replaces duplicated/mislabeled Figure 5b material and reports unchanged conclusions; it is not a retraction.

Summary: The measured endonuclease reaction is RNase III processing.

Reason: Purified human Dicer processes pre-let-7 and edited pre-miR-151 substrates in the original cleavage experiments. Loop changes alter cleavage without corresponding affinity changes. RNase III activity identifies the established cleavage chemistry more precisely than generic RNA endonuclease activity.

Proposed replacements: ribonuclease III activity

Summary: The viral inhibition experiment concerns Dicer RNase III processing.

Reason: The accessible original abstract reports HCV-core association with Dicer and inhibition of Dicer-dependent small-RNA processing. Detailed full-text construct and assay conditions were not recovered. The broad endonuclease assertion is biologically established independently, so refine its gene-level function to RNase III without claiming a newly inspected HCV assay or assigning viral-core catalysis.

Proposed replacements: ribonuclease III activity

Summary: Dicer processes double-stranded RNA into small RNAs by its RNase III mechanism.

Reason: The human RMRP experiments support Dicer-dependent small-RNA formation, not RNA-dependent RNA synthesis by Dicer. Independent purified-enzyme work specifies the endonuclease activity as RNase III. The Figure 5b correction is recorded separately and does not erase this independent biochemical grounding.

Proposed replacements: ribonuclease III activity

Summary: The reconstituted complex contains the RNase III processing enzyme.

Reason: Purified human Dicer, AGO2 and TRBP form a processing/loading assembly. The observed Dicer precursor-cleavage role is more precisely RNase III activity; AGO2 performs target-RNA slicing. The reported concentration-dependent complex stability does not establish invariant cellular stoichiometry.

Proposed replacements: ribonuclease III activity

Summary: Recombinant human Dicer has RNase III activity.

Reason: The original directly assays cleavage of long dsRNA and pre-let-7, with mock-preparation controls. Historical 1912-aa construct identity and current natural-product identities are kept separate. This is the central RNA-processing activity.

Summary: Independent human Dicer preparations establish RNase III cleavage.

Reason: The original compares recombinant human Dicer with mammalian immunoprecipitates and measures dsRNA processing. ATP-depletion and K70A experiments demonstrate cleavage under ATP-independent assay conditions, not an autonomous Dicer ATPase or helicase activity.

Summary: The tandem RNase III architecture performs double-stranded RNA cleavage.

Reason: The accessible source describes a human RNase IIIb fragment forming a catalytic homodimer and cleaving dsRNA. This fragment result complements independent full-length human Dicer biochemistry; it does not imply that the intact protein is obligatorily a homodimer or that every natural short product is active.

Summary: RNase III activity is conserved in the Dicer clade.

Reason: The target is a descendant of PAINT node PTN000383725 and has direct experimental RNase III evidence itself. The family-tree placement, target domains and purified human assays agree. Neither the donor count nor target self-inclusion is a propagation defect.

Summary: Human Dicer directly cleaves RNA using a substrate-dependent counting mechanism.

Reason: The original purifies FLAG-tagged human Dicer from HEK293 cells and assays precursor processing and phosphate-pocket mutants. Human constructs also rescue mouse Dicer-deficient cells. These experiments support RNase III cleavage; their substrate-dependent counting results are not generalized to every RNA.

Summary: The combined domain and enzyme mapping matches the established human activity.

Reason: IPR000999 and IPR036389 match the two RNase III regions of the displayed sequence. EC 3.1.26.3 identifies the same reaction supported by purified human Dicer experiments. The mapping does not establish activity of all splice products independently.

Summary: Reactome assigns Dicer the cleavage of a tRNA–HIV RNA hybrid.

Reason: The typed catalyst path resolves to DICER1/Q9UPY3 entity 203820. PMID:19729508 uses recombinant Dicer and a PBS/tRNA hybrid to produce the small RNA, with Dicer-omission and cellular knockdown controls. This is a contextual substrate of the existing RNase III activity, not a separate catalytic core or evidence that all tRNA fragments require Dicer.

Summary: Retain the phylogenetically inherited DNase assertion as a contextual activity.

Reason: The target genuinely descends from PAINT node PTN001029377, whose IBD for GO:0004530 is grounded in worm DCR1 experiments. The original demonstrates CED3-dependent cleavage at worm D1472 and DNA cleavage by the resulting fragment, not by intact DCR1 under the tested conditions. No target-specific loss, cleavage-site difference or node-placement error was established. Lack of a human activation experiment alone does not overturn the curator's ancestral-function judgment. Retain the inherited activity outside the principal RNA-processing core, while leaving the human activation mechanism and product/fragment correspondence open.

Summary: Dicer associates with a catalytic Argonaute partner.

Reason: The accessible source explicitly reports human and mouse Dicer/eIF2C associations and a conserved PIWI-domain interaction. The imported Q8CJG0 partner is mouse AGO2, not human AGO1. Its established catalytic Argonaute class permits enzyme-binding refinement; detailed full-text construct conditions remain unavailable and no exact current human isoform or purified-contact claim is made.

Proposed replacements: enzyme binding

Summary: The Dicer–AGO1 association is retained as a loading-related interaction.

Reason: The accessible source supports Dicer/eIF2C association, and independent human AGO1-complex experiments corroborate the pair. AGO1 is not the AGO2 slicer, so enzyme binding is not inferred from the shared Argonaute family. No separately demonstrated adaptor mechanism is assigned to this pair.

Summary: Dicer binds the catalytic PIWI-family protein PIWIL1.

Reason: The recovered original tests human Hiwi/PIWIL1 and Dicer domains in yeast two-hybrid and biochemical interaction experiments, including nuclease-resistant association. The verified catalytic partner class supports enzyme binding. Interaction does not make Dicer a piRNA-target slicer or establish every physiological PIWIL1 complex.

Proposed replacements: enzyme binding

Summary: Dicer binds the nuclease AGO2.

Reason: The recovered original maps the human AGO2 PIWI/Dicer RNase III interaction and reports direct biochemical association. Enzyme binding specifies the partner class without transferring AGO2 target-RNA slicing to Dicer or assigning an inhibitory function to Dicer.

Proposed replacements: enzyme binding

Summary: Dicer directly associates with its RNA-binding cofactor TRBP.

Reason: The recovered original contains human-cell complexes and purified Dicer/TRBP experiments. TRBP promotes substrate recruitment and RISC loading, but its established RNA-binding/cofactor class does not make it an enzyme. The pair is retained; no invented RNA-binding-protein-binding or adaptor function is substituted.

Summary: The Dicer–TRBP interaction is directly supported.

Reason: The recovered original combines endogenous human coimmunoprecipitation, nuclease treatment, recombinant proteins and two-hybrid assays. Exact interaction records agree. Its differing depletion/stability results relative to PMID:15973356 are acknowledged rather than converted to a universal stability mechanism. Generic binding is retained as non-core under the project instruction.

Summary: Dicer associates with PACT/PRKRA.

Reason: Human-cell coimmunoprecipitation and domain experiments support the pair. PACT is an RNA-binding regulator, not a protein kinase despite its name. Purified PACT did not stimulate Dicer processing under the particular tested conditions; this does not invalidate association or establish a separate adaptor activity.

Summary: Dicer associates with TRBP in human processing complexes.

Reason: The original human-cell interaction and domain data support the TRBP pair. Its cofactor role is retained without assigning enzyme-binding, kinase-binding or a distinct adaptor mechanism. Coupled processing/slicer assays do not transfer AGO2 slicing to Dicer.

Summary: PACT association is consistent with a Dicer-containing processing assembly.

Reason: The accessible source explicitly describes human Dicer–TRBP–PACT association and small-RNA processing. The full experimental body was not recovered; independent PMID:16424907 supports the exact PACT pair. This retains association without inventing simultaneous direct occupancy or a PACT enzyme class.

Summary: TRBP association is supported in the processing assembly.

Reason: The accessible source describes a human Dicer/TRBP/PACT complex. Independent purified and endogenous Dicer–TRBP experiments corroborate this pair. The annotation does not establish invariant ternary stoichiometry or a new Dicer adaptor function.

Summary: The full set of five source-specific protein associations is not independently resolved.

Reason: The source row combines EIF6, RPL7A, TRBP, MOV10 and AGO2. The accessible abstract describes a larger silencing-associated assembly, but the complete DICER1-specific interaction and construct records were not recovered. Known loading partners do not validate every listed pair, and a single catalytic or translation-factor-binding replacement would silently narrow the multi-partner assertion. Retain uncertainty without claiming misattribution.

Summary: Dicer associates with the ATPase DHX9/RNA helicase A.

Reason: The accessible original explicitly reports RNA helicase A association with Dicer, AGO2 and TRBP and a role in loading. Official DHX9 function establishes ATP hydrolysis, permitting ATPase-binding refinement. Full assay details were unavailable; association is not represented as purified binary binding or a Dicer helicase reaction.

Proposed replacements: ATPase binding

Summary: Dicer associates with AGO2 in human RNA-processing complexes.

Reason: The recovered original identifies Dicer in affinity-purified human AGO2 complexes and assays precursor processing. AGO2 is a catalytic Argonaute, supporting enzyme binding. The source distinguishes complex populations and AGO2 target cleavage from Dicer precursor cleavage.

Proposed replacements: enzyme binding

Summary: Dicer is present in human AGO1-containing processing complexes.

Reason: The recovered original identifies Dicer in selected AGO1 complex fractions, with mass spectrometry and processing assays. AGO1 lacks the established AGO2 slicer activity, so a catalytic partner class is not inferred. Complex association does not imply purified direct contact or invariant RISC membership.

Summary: HCV core associates with and inhibits Dicer in the reported cellular context.

Reason: The source abstract explicitly describes Dicer interaction with HCV core and inhibited small-RNA processing. The imported partner is the mature viral core chain, not the enzymatic polyprotein. Full experimental details were not recovered; preserve the curated association without transferring another viral protein activity or asserting a receptor/adaptor mechanism.

Summary: Dicer binds the enzyme arachidonate 5-lipoxygenase.

Reason: The original uses human historical Dicer C-terminal fragments, purified interaction assays and cellular coimmunoprecipitation with ALOX5. The observed modulation of lipoxygenase activity does not make Dicer a lipoxygenase. Enzyme binding is the supported partner-class refinement, with the tested fragment scope retained.

Proposed replacements: enzyme binding

Summary: Human Dicer associates with AGO2.

Reason: Human Myc-AGO2 affinity purification and mass spectrometry recover Dicer. The catalytic AGO2 partner permits enzyme-binding refinement; later mouse extract deadenylation experiments in this paper are not assigned to Dicer. This is a complex association, not a purified-contact measurement.

Proposed replacements: enzyme binding

Summary: Human Dicer associates with AGO1.

Reason: Human Myc-AGO1 HEK293 affinity-purification data recover Dicer. AGO1 association supports a processing-complex interaction but not enzyme binding, because the AGO2 nuclease class cannot be inferred from the family name. No Dicer deadenylase or adaptor activity is assigned.

Summary: TRBP phosphorylation modulates the Dicer-containing complex.

Reason: Human-cell interaction and perturbation experiments link TRBP phosphorylation to Dicer-complex stability and small-RNA processing. Dicer associates with TRBP; it is not shown to phosphorylate TRBP. Retain the pair without kinase-binding or an independently established adaptor classification.

Summary: Purified Dicer and TRBP form a processing/loading assembly.

Reason: The reconstituted human complex supports physical association. TRBP is a nonenzymatic RNA-binding cofactor, and the three-component assembly does not by itself establish a distinct Dicer molecular adaptor activity. Complex stability depends on concentration in these experiments.

Summary: Purified Dicer associates with the nuclease AGO2.

Reason: The human Dicer–TRBP–AGO2 reconstitution supports association with a catalytic partner. Refine to enzyme binding without asserting that every pair directly contacts in the same way, that native stoichiometry is invariant, or that Dicer performs AGO2 target slicing.

Proposed replacements: enzyme binding

Summary: The viral Rex association is retained with its inhibition context.

Reason: The accessible original reports HTLV-1 Rex–Dicer interaction and inhibition of shRNA-mediated silencing; exact interaction records support the pair. Rex is a viral RNA-export regulator, not an ATPase or nuclease. Full original assay details were not recovered, so no additional physiological receptor or adaptor mechanism is assigned.

Summary: Dicer associates with PACT in human cellular fractions.

Reason: The original human-cell coimmunoprecipitation identifies PACT with Dicer in the study of cytoplasmic and nuclear pools. PACT is not a kinase. Association supports a regulatory complex, without establishing a separate adaptor function or universal localization of all Dicer products.

Summary: Dicer associates with TRBP in the examined human cells.

Reason: The original coimmunoprecipitation and fractionation support TRBP–Dicer association. The findings include nuclear as well as cytoplasmic pools and do not justify restricting the interaction to one compartment or assigning a new cofactor-binding class absent a verified term.

Summary: Dicer associates with the catalytic partner AGO2.

Reason: AGO2 is recovered with Dicer in the human-cell complex analysis. Its established nuclease class supports enzyme binding, while the experiment remains a cellular association rather than purified contact. Nuclear localization of a Dicer pool does not imply every product or loading event is nuclear.

Proposed replacements: enzyme binding

Summary: Dicer associates with the protein kinase PKR.

Reason: The genuine original and exact nonexpanded human IntAct coimmunoprecipitation record EBI-6124533 support the PKR/P19525 pair in addition to spoke-expanded discovery records. PKR is a protein kinase, permitting the specific partner-class term. No purified binding or Dicer kinase activity is asserted; the substantive scope of the metadata-listed 2011 erratum was not recovered.

Proposed replacements: protein kinase binding

Summary: Dicer associates with the ATPase LGP2/DHX58.

Reason: The original and exact human nonexpanded coimmunoprecipitation record EBI-6125302 support DHX58/Q96C10 association. Official DHX58 ATP-hydrolysis activity supports ATPase binding. Neither FLAG purification nor coimmunoprecipitation establishes direct purified contact, affinity, or intrinsic Dicer helicase activity.

Proposed replacements: ATPase binding

Summary: Dicer associates with the RNA-editing enzyme ADAR1 p150.

Reason: The source tests ADAR1 p150 and Dicer with recombinant and cellular assays, including RNA-binding-defective constructs. The enzyme partner class is established even where editing catalysis is dispensable for stimulation of Dicer. This does not assign RNA editing to Dicer or imply that ADAR1 is catalytically active within every complex.

Proposed replacements: enzyme binding

Summary: Dicer associates with ADAR1 p110.

Reason: The source also tests the p110 ADAR1 product represented by the imported partner identifier. Association and stimulation of Dicer are separable from ADAR1 editing. Enzyme binding specifies the partner class, without claiming a new Dicer chemistry or replacing the source product identifier.

Proposed replacements: enzyme binding

Summary: The source includes Dicer-associated TRBP.

Reason: Interaction records and the original complex comparisons support the TRBP association. TRBP is an RNA-binding cofactor; the data do not establish a new catalytic partner class. Comparisons involving ADAR1 do not require all cofactors to occupy the same ternary complex simultaneously.

Summary: Dicer associates with AGO2 in the ADAR1-modulated processing system.

Reason: The original experiments support an AGO2/Dicer association and distinguish Dicer-mediated recruitment from ADAR1 effects. AGO2 is an enzyme, so enzyme binding is appropriate. No direct ADAR1–AGO2 contact or Dicer target-slicing activity is inferred.

Proposed replacements: enzyme binding

Summary: PACT associates with Dicer in reconstituted processing complexes.

Reason: Purified human Dicer and PACT support the association, while substrate-dependent processing differs from TRBP complexes. PACT can slow processing of a perfect pre-siRNA under the tested conditions. These findings do not turn PACT into an enzyme or establish a distinct Dicer adaptor core.

Summary: TRBP associates with Dicer in reconstituted processing complexes.

Reason: Purified human proteins and processing assays support the pair. TRBP alters substrate/product behavior as a cofactor. Generic binding is retained without assigning an unsupported partner enzyme or an independent adaptor mechanism.

Summary: Dicer associates with AGO2 in the purified loading system.

Reason: The human protein reconstitutions include Dicer, AGO2 and alternative dsRNA-binding partners. AGO2 is the catalytic partner, supporting enzyme binding. This refinement neither assigns target slicing to Dicer nor assumes invariant simultaneous occupancy by both TRBP and PACT.

Proposed replacements: enzyme binding

Summary: Dicer associates with AGO2 during small-RNA loading.

Reason: Human HeLa Myc-AGO2 coimmunoprecipitation recovers Dicer with nuclease-treatment controls. The interaction supports binding to the established AGO2 enzyme class; the chaperone-dependent loading experiments do not make Dicer a chaperone or prove purified pairwise contact.

Proposed replacements: enzyme binding

Summary: The exosomal Dicer–TRBP source is under an unresolved expression of concern.

Reason: The original reports Dicer immunoprecipitation with TRBP in cancer-exosome preparations, but PMID:40930611 questions the publication-wide original data, specifically including reused Dicer Figure 3A lanes. Figure 3J/K is not individually declared false, and no retraction is inferred. Independent loading-complex papers establish the ordinary pair, but they do not validate this disputed exosomal experiment. Preserve this source-specific row as unresolved.

Summary: The cancer-exosome Dicer–AGO2 experiment is not treated as reliable independent evidence.

Reason: The original reports AGO2 in Dicer immunoprecipitates; its IntAct record is a spoke-expanded complex. The later expression of concern describes broader data-integrity concerns and ongoing journal review, without individually falsifying this pair. Independent purified loading complexes establish Dicer–AGO2 association but do not resolve the exosomal experiment. Keep the original source and uncertainty.

Summary: The Dicer–TRBP binding interface is structurally established.

Reason: Human Dicer PBD and TRBP domains were crystallized and tested by binding assays, with full-length validation. PACT and TRBP use a mutually exclusive interface under these conditions. Engineered interface mutants and mouse-cell rescue are not natural human products, and the pair does not establish a separate adaptor function.

Summary: Dicer associates with AGO2 in the quantitative interaction screen.

Reason: The exact source interaction record supports the AGO2 pair in a human-cell affinity-purification screen. AGO2 is a catalytic Argonaute, so enzyme binding is more informative than generic binding. Screen association does not establish purified direct contact, native stoichiometry or a product-specific interaction.

Proposed replacements: enzyme binding

Summary: All three listed Dicer associations remain unverified from the accessible original material.

Reason: The source row lists SND1, TNRC6A and AGO2. The genuine original Figure 1A shows TSN/SND1 association with AGO2 and GW182, while Dicer is in a separate knockdown panel. Supplementary reciprocal FLAG-AGO2 experiments could contain relevant evidence, but the supplement was not recovered. Do not infer misattribution or absence from the inspected panels, and do not transfer TSN mature-miRNA decay to Dicer.

Summary: The Nipah matrix-protein association is supported in tagged-protein experiments.

Reason: The original reports TAP-MS and reciprocal Dicer coimmunoprecipitation with N-terminally tagged Nipah M; C-terminal tagging differed. No effect on miRNA processing was detected. Retain the association, without claiming a physiological antiviral sensing mechanism or using a foreign-protein-binding refinement whose annotation convention requires established physiological relevance.

Summary: TWEAK associates with a Dicer fragment and with cellular Dicer in the tested expression systems.

Reason: Retested yeast two-hybrid assays were positive for the human Dicer C-terminal fragment (residues 1772–1912), whereas full-length Dicer was negative in that assay. Flag-TWEAK coimmunoprecipitated cellular Dicer after RNase treatment, establishing an association that is not explained by an RNA bridge; other protein-mediated association remains possible. The negative full-length assay does not negate the positive observations, but fragment binding and overexpression-dependent cellular association do not resolve direct full-length binding or native access to transmembrane or soluble TWEAK. TWEAK is a cytokine, yet these combined limits make a whole-product cytokine-binding refinement insufficiently established here. Retain the positive association as non-core without assigning receptor activity or TWEAK signaling to Dicer.

Summary: Dicer associates with TRBP in a context-dependent nuclear complex.

Reason: Patient-derived glioblastoma stem-cell experiments recover Dicer/TRBP and show nuclear enrichment compared with neural progenitor cells. Circ2082 directly binds RBM3, with Dicer association depending on RBM3; that does not establish direct Dicer circular-RNA binding. Retain the TRBP pair without a new adaptor function or universal nuclear localization.

Summary: BioPlex supports a Dicer–PACT association.

Reason: Exact human interaction records and the BioPlex AP-MS design support the PRKRA pair. Gene-level aggregation and tagged bait purification do not resolve a natural Dicer product or purified direct contact. PACT is a nonenzymatic regulator, so neither its kinase-activator name nor AP-MS association justifies kinase binding or a separate adaptor activity.

Summary: BioPlex supports association with the enzyme AGO2.

Reason: The exact human AP-MS record supports the pair, independently consistent with purified loading-complex studies. AGO2 has established nuclease activity, allowing enzyme-binding refinement on a screen-level association. Gene-level protein aggregation does not resolve a natural isoform or establish affinity, direct contact or native stoichiometry.

Proposed replacements: enzyme binding

Summary: BioPlex supports the Dicer–AGO1 association.

Reason: The exact human AP-MS record supports this pair, with gene-level aggregation and tagged-bait limitations. AGO1 is not assigned AGO2 slicer activity. Retain the association without an unsupported enzyme-binding or adaptor replacement.

Summary: The primary 2025 AP-MS dataset contains the Dicer–AGO1 pair.

Reason: The paper-linked NDEx AP-MS graph contains AGO1 bait node 552592, DICER1 prey node 550352 and edge 610082. This is measured AP-MS association, not map proximity or inferred membership in a derived assembly. U2OS tagged-bait experiments do not establish purified contact or a current natural isoform; the graph metadata ambiguity is retained without calling the bait sequence ambiguous. The equation correction does not identify this pair, and AGO1 does not supply an established catalytic partner class.

Summary: ATP binding is not established solely by the conserved helicase-like fold.

Reason: The official IPR011545 match is genuine. Purified human Dicer experiments failed to detect ATP binding/hydrolysis under their tested conditions and show ATP-independent cleavage; this does not prove that every Dicer state lacks ATP binding. The domain mapping and target biochemistry leave this particular subactivity unresolved, without claiming the domain is absent or that an ATP-independent reaction alone excludes nucleotide binding.

Summary: Human Dicer has context-dependent nuclear pools.

Reason: The target is inside the PAINT clade assigned nuclear localization. Independent human fractionation and immunodetection in PMID:21858095, and patient-derived glioblastoma-stem-cell work in PMID:33328224, support nuclear pools. Nuclear localization is contextual rather than an exclusive location of the integrated processing core; neither tissue differences nor target self-grounding invalidates the phylogeny.

Summary: Dicer performs its principal processing/loading functions in the cytoplasm.

Reason: The PAINT node PTN000383725 includes the target and experimentally characterized Dicers. Human purified/cellular processing studies and localization support a cytoplasmic pool. This is not an exclusion of nuclear, membrane-associated or extracellular pools.

Summary: The UniProt cytoplasmic-location mapping is supported.

Reason: The official subcellular-location mapping agrees with human-cell localization and the RNA-processing/loading mechanism. Cytoplasm is nonexclusive; no all-isoform localization is inferred from the gene-level mapping.

Summary: The Human Protein Atlas supports cytosolic DICER1.

Reason: The current official target record ENSG00000100697/Q9UPY3 assigns supported cytosolic localization by immunocytochemistry/immunofluorescence, including A431 and BJ fibroblast records. This review inspected the target XML metadata, not image pixels. The location agrees with processing/loading evidence but is not exclusive.

Summary: Reactome places the Dicer-containing pre-miRNA cleavage machinery in the cytosol.

Reason: The saved typed event and complex/member paths resolve to DICER1 entity 203820, Q9UPY3, in cytosol 70101. This supports location during pre-miRNA cleavage. It does not assign every reaction in the assembly to Dicer: Argonaute-mediated passenger/target cleavage is distinct from Dicer precursor processing.

Summary: Reactome places the Dicer-containing miRNA loading machinery in the cytosol.

Reason: The saved typed event and complex/member paths resolve to DICER1 entity 203820, Q9UPY3, in cytosol 70101. This supports location during miRNA loading. It does not assign every reaction in the assembly to Dicer: Argonaute-mediated passenger/target cleavage is distinct from Dicer precursor processing.

Summary: Reactome places the Dicer-containing siRNA passenger-strand removal machinery in the cytosol.

Reason: The saved typed event and complex/member paths resolve to DICER1 entity 203820, Q9UPY3, in cytosol 70101. This supports location during siRNA passenger-strand removal. It does not assign every reaction in the assembly to Dicer: Argonaute-mediated passenger/target cleavage is distinct from Dicer precursor processing.

Summary: Reactome places the Dicer-containing siRNA loading machinery in the cytosol.

Reason: The saved typed event and complex/member paths resolve to DICER1 entity 203820, Q9UPY3, in cytosol 70101. This supports location during siRNA loading. It does not assign every reaction in the assembly to Dicer: Argonaute-mediated passenger/target cleavage is distinct from Dicer precursor processing.

Summary: Reactome places the Dicer-containing miRNA passenger-strand removal machinery in the cytosol.

Reason: The saved typed event and complex/member paths resolve to DICER1 entity 203820, Q9UPY3, in cytosol 70101. This supports location during miRNA passenger-strand removal. It does not assign every reaction in the assembly to Dicer: Argonaute-mediated passenger/target cleavage is distinct from Dicer precursor processing.

Summary: Reactome places the Dicer-containing double-stranded RNA cleavage machinery in the cytosol.

Reason: The saved typed event and complex/member paths resolve to DICER1 entity 203820, Q9UPY3, in cytosol 70101. This supports location during double-stranded RNA cleavage. It does not assign every reaction in the assembly to Dicer: Argonaute-mediated passenger/target cleavage is distinct from Dicer precursor processing.

Summary: Reactome places the Dicer-containing tRNA–HIV RNA hybrid cleavage machinery in the cytosol.

Reason: The saved typed event and complex/member paths resolve to DICER1 entity 203820, Q9UPY3, in cytosol 70101. This supports location during tRNA–HIV RNA hybrid cleavage. It does not assign every reaction in the assembly to Dicer: Argonaute-mediated passenger/target cleavage is distinct from Dicer precursor processing.

Summary: The Dicer product in the expression event has a supported cytosolic location.

Reason: Reactome identifies the cytosolic DICER1 product in this MITF-dependent expression event. Independent human localization and processing/loading evidence support the gene-level cytosol annotation, consistently with the other cytosol rows. Dicer is the output of this event, not a transcriptional catalyst or a participant in its own synthesis.

Summary: Retain the inherited apoptotic-fragmentation role with its fragment-mediated source mechanism.

Reason: The PAINT IBD at PTN001029377/taxon 6072 places this function in a clade containing both human DICER1 and worm DCR1. The inspected worm source establishes performed DNA-cleavage work by a caspase-generated fragment, satisfying the participation distinction rather than relying only on cell-death necessity. No concrete evolutionary or target-specific contradiction was found. Retain the phylogenetic assertion as a non-core apoptotic context; the exact human cleavage and activation mechanism remains a question, not a reason to reject the inherited function.

Summary: The broad processing mapping can specify Dicer precursor cleavage.

Reason: The target RNase III domain matches and independent human biochemical experiments establish pre-miRNA and siRNA processing. These are more informative than generic RNA processing, and both are already represented in the imported annotations. This refinement adds no novel process assertion.

Proposed replacements: pre-miRNA processing siRNA processing

Summary: Dicer performs the pre-miRNA cleavage step of miRNA metabolism.

Reason: The curated pathway contains Dicer-mediated precursor cleavage through its typed catalyst path. Pre-miRNA processing identifies the work performed by Dicer rather than all synthesis, turnover and regulation of miRNAs. The more specific process is supported by direct human biochemical evidence.

Proposed replacements: pre-miRNA processing

Summary: Dicer limits proliferation in the studied Schwann-cell differentiation system.

Reason: The Q4G034 donor traces to primary rat Schwann-cell Dicer knockdown, where proliferation markers increased and differentiation/myelination declined (PMID:20648646). This is a conserved developmental regulatory context of miRNA processing, not a separate catalytic function. Timing matters: mouse studies show different early versus later proliferation outcomes.

Summary: The source-specific Dicer contribution to the reported repression is not resolved.

Reason: The accessible PMID:22105995 abstract emphasizes miR-19/TLR2 regulation in rheumatoid-arthritis fibroblast-like synoviocytes, without enough DICER1-specific assay detail to adjudicate this row. Full relevant experimental text was not recovered. The known general role of Dicer in small-RNA production does not substitute for the source-specific evidence, and no misattribution is claimed.

Summary: Dicer-dependent miRNA production regulates gene expression in endothelial cells.

Reason: The source reports human microvascular endothelial-cell Dicer knockdown/overexpression and a miR-210/Ephrin-A3 regulatory relationship. This supports a contextual gene-expression effect of miRNA production, not direct transcriptional repression or a new catalytic core. Detailed full-text assay conditions were not recovered; the accessible result and established processing role support retention.

Summary: The measured effect is reduced TNF production rather than demonstrated downstream TNF-receptor signaling.

Reason: The original human hepatocyte experiments link Dicer-dependent miR-125b/miR-130a processing to lower TNF production after LPS. NF-kappaB activation was not altered in the tested comparison. GO:0010804 concerns signals following TNF receptor binding; GO:0032720 describes the measured ligand-production outcome more precisely. This is a context-specific regulatory effect, not Dicer cytokine or receptor activity.

Proposed replacements: negative regulation of tumor necrosis factor production

Summary: Dicer promotes Schwann-cell differentiation through regulatory RNAs.

Reason: The actual rat donor work uses Dicer knockdown in primary Schwann cells and rat neuron cocultures, measuring reduced mature miRNAs, differentiation markers and myelination. Human cells used for viral packaging are not the donor experiment. The conserved role is contextual and does not imply Dicer is a transcription factor.

Summary: Mouse Dicer evidence supports a conserved Schwann-cell differentiation role.

Reason: The donor studies delete Dicer in the mouse Schwann-cell lineage, producing a promyelinating arrest and altered regulatory-RNA/marker expression. The lineage-restricted experiment supports this regulatory process, not a human cell assay or an independent Dicer structural component of myelin.

Summary: Dicer participates in selected tRNA-fragment-producing reactions.

Reason: The Reactome pathway includes direct Dicer cleavage of a tRNA–HIV RNA hybrid and other tRNA-fragment routes. PMID:19729508 directly assays the hybrid substrate; the pathway itself notes that many tRNA-derived fragments persist without Dicer. Retain the contextual tRNA-decay assertion without treating all tRNA turnover as a Dicer core.

Summary: Dicer contributes to post-transcriptional silencing through guide-RNA production and loading.

Reason: The ARBA rule is a genuine current source with multiple alternative conditions; an exact target FunFam match was not independently rerun. Direct human processing/loading experiments support the biological pathway claim. The broad silencing outcome is retained as context for the core cleavage/assembly steps, not as autonomous target-RNA slicing by Dicer.

Summary: The negated RISC assertion is retained in the source-specific release context.

Reason: The original demonstrates active AGO2–miRNA release from Dicer, particularly with pre-miR-30a, supporting a mature minimal effector that does not require stable Dicer membership. The same paper reports active AGO2 retained on Dicer beads with PML-GL3 and permits a fraction of loading complexes to remain associated. Thus this NOT row is not a universal absence claim for every dynamic RISC. Its negated flag is preserved exactly, and loading-complex membership remains a separate positive assertion.

Summary: Dicer can associate with RISC-related assemblies during loading.

Reason: The accessible source explicitly reports RNA helicase A interaction with Dicer, AGO2 and TRBP and involvement in loading. Detailed full text was not recovered. Independent human complexes show dynamic association and release, so retain the curated RISC membership as contextual rather than asserting that Dicer is an invariant component of the mature minimal effector.

Summary: The mapped hydrolytic RNA endonuclease activity is specifically RNase III.

Reason: IPR005034 is a real Dicer dimerization-domain match; that domain alone is not the catalytic center. Independent human biochemistry and the tandem RNase III domains establish the target reaction, allowing the more informative RNase III replacement without inferring catalysis merely from dimerization.

Proposed replacements: ribonuclease III activity

Summary: The AGO1 PIWI-domain interaction is retained as a domain-specific association.

Reason: The source abstract explicitly describes the conserved PIWI-domain/Dicer interaction and supports the imported AGO1 partner. Detailed full original conditions were unavailable, so no purified-contact or exact isoform claim is added. Domain-specific binding is more descriptive than generic binding but is not a separate Dicer catalytic or adaptor core.

Summary: Dicer has a developmental role in peripheral nerve formation.

Reason: The inspected mouse donor studies remove Dicer in Schwann cells and disrupt differentiation and myelination. This supports a nerve-development context mediated by regulatory-RNA production. It does not establish a neuron-intrinsic Dicer structural activity or a new independent core.

Summary: Conserved Dicer activity directly produces siRNAs.

Reason: The PAINT node PTN000383725 is experimentally grounded across Dicer lineages and includes human target experiments. Human recombinant and reconstituted-complex studies directly process double-stranded RNA into siRNAs. Differences among fly Dicer paralogs do not invalidate the target placement or direct evidence.

Summary: The Dicer–TRBP system processes double-stranded RNA into siRNAs.

Reason: The recovered original assays Dicer-containing human complexes and purified Dicer/TRBP with RNA substrates. Processing and loading are distinguished from target-RNA cleavage by AGO2. This is direct work in the integrated core.

Summary: Dicer participates in siRNA production in the reported processing complex.

Reason: The accessible source explicitly describes human Dicer/TRBP/PACT-mediated small-RNA processing. Full experimental detail was not recovered, but the process is directly established by independent purified human Dicer studies, so the curated assertion is retained without inventing unseen assay conditions.

Summary: Purified human Dicer processes siRNA precursors.

Reason: The original compares Dicer with TRBP or PACT on defined substrates. PACT can reduce processing of a perfect pre-siRNA under tested conditions, whereas different substrates behave differently. These quantitative effects support, rather than replace, the basic processing role.

Summary: The combined rule/domain mapping agrees with direct siRNA processing.

Reason: The official IPR044441 target match and current ARBA00087137 rule were inspected. Exact target FunFam assignments were not independently recomputed, so rule execution is not claimed. Independent human biochemistry establishes the process and grounds retention of this inferred row.

Summary: Dicer is required for the measured RMRP-derived siRNAs.

Reason: Two human-cell Dicer knockdowns reduce the RMRP-derived small RNAs and distinguish their processing from TERT-dependent RNA synthesis. The later Figure 5b correction is recorded; the core Dicer processing role is independently established and no Dicer RNA-dependent RNA polymerase activity is inferred.

Summary: Reactome assigns Dicer the siRNA precursor-cleavage step.

Reason: The curated pathway resolves through the dsRNA-cleavage reaction and Dicer-containing catalyst complexes to Q9UPY3. It is supported by independent human Dicer assays. Downstream Argonaute slicing and passenger-strand removal are not transferred wholesale to Dicer.

Summary: Pre-miRNA processing is conserved and directly grounded in human Dicer.

Reason: The target descends from PTN001029377 and carries direct experimental evidence used in the PAINT inference. Purified and cellular human studies directly establish precursor cleavage. The target appearing among descendant evidence is not circular.

Summary: Dicer cleaves pre-miRNA within the TRBP-containing system.

Reason: The recovered original directly tests precursor processing and assembly. This identifies the Dicer step rather than simply a knockdown consequence. The cofactor contribution does not require a new molecular function beyond the integrated RNase III mechanism.

Summary: Dicer performs pre-miRNA cleavage in the human-cell loading system.

Reason: The original separates Dicer precursor processing from AGO2 target slicing, including later human AGO2 and catalytic-mutant experiments. Initial mouse FLAG-AGO2 constructs in human cells are distinguished from human Dicer. Release of the final effector does not remove Dicer from the preceding processing step.

Summary: Reconstituted human Dicer directly processes a pre-miRNA substrate.

Reason: Purified human proteins process Drosophila pre-let-7 within the RISC-loading system. The substrate species does not change the human identity of the enzyme. The measured complex affinity is not reassigned to isolated Dicer.

Summary: Purified human Dicer processes pre-miRNAs with substrate-dependent cofactor effects.

Reason: The original compares pre-miRNA substrates with TRBP and PACT and measures cleavage/product differences. This is direct precursor-processing evidence, without assuming uniform cofactor effects or simultaneous direct occupancy.

Summary: Human Dicer recognizes and cleaves pre-miRNA stem-loop substrates.

Reason: The original uses purified human protein, cleavage assays and mobility-shift binding measurements. Edited bases and terminal-loop changes affect processing; the binding and cleavage readouts are kept distinct. This supports the core precursor-processing activity.

Summary: The Dicer-specific rule and dsRNA-binding-domain mapping agree with direct precursor processing.

Reason: ARBA00027506 includes a conjunction of IPR000999, IPR001650 and IPR044441, which occur in the target architecture. The official IPR044441 mapping and human biochemical evidence support retention. This does not prove that all natural products retain the full architecture or activity.

Summary: Dicer promotes myelination in the rat Schwann-cell system.

Reason: Primary rat Schwann-cell knockdown and rat neuron coculture show defective differentiation and myelination after reduced Dicer. The outcome is mediated through regulatory-RNA programs, not evidence that Dicer synthesizes myelin lipids or provides myelin structure.

Summary: Mouse donor experiments support a regulatory role in myelination.

Reason: Schwann-lineage Dicer deletion impairs myelination and alters differentiation programs. The phenotype supports conserved pathway regulation, with developmental timing and cell type explicit; it does not establish a separate human myelin-forming enzyme activity.

Summary: Dicer-dependent regulatory RNAs contribute to peripheral myelin formation.

Reason: The inspected mouse Schwann-cell deletion studies demonstrate failure of normal peripheral myelin formation. Dicer performs miRNA-processing work upstream of this developmental program. The existing process annotation is retained as contextual, without manufacturing an extra core or transferring a structural myelin role.

Summary: Dicer-dependent miRNAs restrain TNF production in the tested hepatocyte context.

Reason: The original connects Dicer loss, reduced mature miR-125b/miR-130a and increased TNF production after LPS in human hepatocyte experiments, with mouse experiments separately described. The result is cell-context-specific and does not establish Dicer as a cytokine, receptor or transcription factor.

Summary: The directly measured miRNA-processing step is pre-miRNA cleavage.

Reason: The recovered original assays precursor cleavage by Dicer-containing complexes and purified proteins. GO:0031054 identifies this step more precisely than the broader miRNA-processing parent, without proposing a new annotation.

Proposed replacements: pre-miRNA processing

Summary: The source directly measures Dicer pre-miRNA processing.

Reason: Purified Dicer/cofactor experiments process defined precursors and compare product profiles. The narrower pre-miRNA-processing term captures the demonstrated step, without assigning every aspect of miRNA maturation to Dicer.

Proposed replacements: pre-miRNA processing

Summary: Dicer-dependent mature-miRNA formation is consistent with its established precursor-cleavage step.

Reason: The source reports endothelial-cell Dicer perturbation and miR-210 effects. Detailed full text was not recovered, so no unseen intermediate assay is asserted. Independent direct human biochemistry defines the Dicer step as pre-miRNA processing; this provides the specific gene-level refinement while preserving the original evidence identity.

Proposed replacements: pre-miRNA processing

Summary: Dicer performs the precursor-processing step underlying the hepatocyte miRNA changes.

Reason: The original measures Dicer-dependent mature-miRNA levels and TNF regulation in human hepatocytes. Independent precursor-cleavage experiments specify the molecular step as pre-miRNA processing; downstream TNF effects are kept separate and non-core.

Proposed replacements: pre-miRNA processing

Summary: The rat donor phenotype concerns conserved Dicer-dependent precursor processing.

Reason: The actual primary rat Schwann-cell study measures reduced mature miRNAs after Dicer knockdown. It does not directly reconstitute precursor cleavage, but independent human Dicer experiments establish that specific step. Refine the broad processing term while retaining donor identity and distinguishing source phenotype from target biochemistry.

Proposed replacements: pre-miRNA processing

Summary: The source siRNA-binding signal belongs to a Dicer–TRBP complex rather than clearly isolated Dicer.

Reason: The recovered original mobility-shift experiment reports siRNA binding by TRBP and the Dicer/TRBP complex, while Dicer alone is negative under those conditions. The imported row asserts Dicer siRNA binding without the weaker contributes-to scope used by the separate pre-miRNA complex row. Direct Dicer contact with the siRNA in this assay remains unresolved; the source fields are preserved, and no universal inability to bind a short RNA is asserted.

Summary: Dicer has a perinuclear cytoplasmic pool in the 5-lipoxygenase study.

Reason: The original reports localization in the human-cell interaction context. This supports a nonexclusive perinuclear pool alongside cytosolic and nuclear observations, rather than restricting all Dicer activity or products to this compartment.

Summary: The UniProt perinuclear mapping is compatible with direct human localization evidence.

Reason: The official location mapping agrees with the human-cell observations in PMID:19022417. Perinuclear cytoplasm is a contextual pool and is not treated as an exclusive catalytic location or an isoform-wide property.

Summary: Dicer-dependent Schwann-cell programs affect neuronal projections in the mouse donor context.

Reason: The inspected donor experiments delete Dicer in Schwann cells, not neurons, and show altered nerve maturation and later axonal abnormalities. The existing broad morphogenesis annotation is retained as a contextual developmental consequence, without assigning a neuron-intrinsic structural mechanism or treating axonal degeneration alone as a new Dicer core.

Summary: Supported specific regulatory roles encompass Schwann-cell maturation and myelination, and restraint of TNF production.

Reason: ARBA00028859 has alternative conditions whose exact target FunFam execution was not independently reconstructed. The broad assertion is biologically sound but is refined to all four supported descendants already represented in this review: negative regulation of Schwann cell proliferation, positive regulation of Schwann cell differentiation, positive regulation of myelination, and negative regulation of tumor necrosis factor production. Rodent Schwann-cell experiments support the first three, with age-dependent proliferation effects; human Huh7 DICER knockdown and miRNA rescue support the TNF-regulatory role. Current is_a/part_of ancestry places all four under GO:0051239. Peripheral nervous system myelin formation (GO:0032290) is not a descendant and is not used as its replacement. These refinements preserve the distinct experimental contexts and do not reconstruct ARBA execution or add new biological coverage.

Proposed replacements: negative regulation of Schwann cell proliferation positive regulation of Schwann cell differentiation positive regulation of myelination negative regulation of tumor necrosis factor production

Summary: Direct pre-miRNA binding is more informative than generic regulatory-RNA binding.

Reason: The current ARBA rule was inspected but its exact target FunFam execution was not independently rerun. Purified human Dicer directly binds precursor hairpins in independent experiments, supporting pre-miRNA binding. This does not generalize to every mature regulatory RNA or reassign a complex-only affinity to isolated Dicer.

Proposed replacements: pre-miRNA binding

Summary: DICER protein is detected as protected cargo in human extracellular-vesicle preparations.

Reason: The original uses surgical pericardial fluid, filtration and ExoQuick enrichment, DICER immunoblotting and proteinase/RNase protection lost upon sonication. These independent experiments support the existing exosome localization, with precipitation/purity limitations. They do not demonstrate extracellular Dicer catalysis or a Dicer-specific angiogenic mechanism, and are distinct from the disputed cancer-exosome source.

Summary: Dicer is a conserved RISC-loading-complex component.

Reason: The target is below PAINT node PTN000383726. Human purified and cellular experiments establish processing/loading-complex membership. Mature effector release and dynamic RISC association are distinct questions and do not negate this loading-complex annotation.

Summary: Dicer and TRBP participate in RISC loading.

Reason: The recovered original shows Dicer-containing processing complexes, purified association and loading-related assays. This is active precursor-processing/assembly work, not membership inferred solely from a downstream knockout phenotype.

Summary: Dicer is part of the precursor-processing loading machinery.

Reason: Human-cell experiments directly separate precursor processing from subsequent AGO2 target slicing and demonstrate partial effector release. The loading-complex annotation remains supported regardless of whether a particular mature effector retains Dicer.

Summary: Dicer participates in the RHA-associated loading assembly.

Reason: The accessible original explicitly places Dicer, AGO2, TRBP and RNA helicase A in the loading system. Full assay details were unavailable, but independent purified human Dicer loading-complex experiments support the exact general membership. No extra RHA-dependent catalytic activity is assigned to Dicer.

Summary: Purified human Dicer, AGO2 and TRBP form a loading complex.

Reason: The original reconstitutes a 1:1:1 complex and assays precursor processing and guide loading. This is a tested biochemical assembly; it is not assumed to represent invariant stoichiometry or composition in every cell.

Summary: The reconstituted human complex contains Dicer.

Reason: Purified human Dicer, AGO2 and TRBP form a stable complex at the examined higher concentration, with dissociation on dilution. Its structural RNA-handoff interpretation is distinguished from directly observed processing and complex formation.

Summary: Dicer forms loading complexes with alternative dsRNA-binding cofactors.

Reason: The original reconstitutes human Dicer/AGO2 complexes with TRBP or PACT and measures substrate-dependent loading/processing behavior. Alternative cofactors do not imply simultaneous direct occupancy or a separate core activity for each assembly.

Summary: The rule-based loading-complex assertion agrees with direct human experiments.

Reason: ARBA00085164 contains primate-lineage and FunFam conditions; exact target FunFam membership was not independently recomputed. Independent purified human loading complexes establish the biological claim, so the inferred assertion is retained without pretending a new rule execution was performed.

Summary: Physical association supports Dicer membership in the tested loading complexes.

Reason: The source protein-association experiments accompany human purified-complex reconstitution. Dicer performs the precursor-cleavage component; AGO2 performs the downstream target-slicing reaction. The IPI and IDA rows retain their distinct source identities.

Summary: Dicer contributes to pre-miRNA binding by the reconstituted loading complex.

Reason: The source filter-binding measurement is for the intact human RISC-loading complex with a Drosophila precursor substrate. The imported contributes_to qualifier is preserved and matches this weaker complex-level claim. The numerical affinity is not represented as a Dicer-only measurement.

Summary: Purified human Dicer directly binds pre-miRNA.

Reason: The original separates substrate binding from cleavage in full-length and engineered-domain variants. These experiments establish binding by Dicer itself; engineered helicase deletions are not natural alternative products. ATPase activity is not inferred from the domain name.

Summary: Purified human Dicer binds precursor hairpins.

Reason: Mobility-shift experiments directly test human Dicer binding to pre-miRNA substrates. Terminal-loop changes can alter cleavage without substantially changing affinity, demonstrating why binding and processing evidence should be kept distinct.

Summary: Dicer contributes performed processing work to RISC assembly.

Reason: The recovered original links Dicer/TRBP precursor cleavage and loading-complex formation to active silencing complexes. Dicer does work in the assembly pathway; AGO2 target-RNA slicing remains a distinct catalytic event.

Summary: Dicer participates in biochemical assembly of an active guide-loaded effector.

Reason: Purified human components process a precursor, select a guide and produce active AGO2-RISC. This directly grounds participation, rather than merely showing that loss of Dicer prevents an outcome. It does not require Dicer to remain in every mature minimal effector.

Summary: Human Dicer complexes participate in guide loading and RISC assembly.

Reason: The original reconstitutes complexes with AGO2 and alternative dsRNA-binding cofactors and measures substrate-dependent products and loading. These results support the integrated assembly process without inventing a distinct adaptor MF or assuming invariant complex composition.

Summary: Dicer supplies small RNAs to a silencing pathway that includes mRNA cleavage.

Reason: The accessible original describes human Dicer/TRBP/PACT-dependent small-RNA processing and silencing. Dicer performs precursor processing upstream of AGO2-mediated mRNA cleavage. Retain this existing pathway-level assertion as non-core context, without assigning mRNA slicing to Dicer or manufacturing a new process annotation.