{"gene":"DCAF10","run_date":"2026-04-28T17:28:53","timeline":{"discoveries":[{"year":2021,"finding":"OTUD1 stabilizes DCAF10 and recruits the CUL4A-DDB1-DCAF10 E3 ligase complex to promote polyubiquitination and proteasomal degradation of MCL1, thereby activating caspase-dependent apoptotic signaling. OTUD1 deubiquitinates and stabilizes DCAF10, linking the deubiquitinase to the CUL4A-based ubiquitin ligase machinery.","method":"Co-immunoprecipitation, deubiquitination assays, overexpression/knockdown with apoptosis readouts, MCL1 degradation assays","journal":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","confidence":"Medium","confidence_rationale":"Tier 2 — reciprocal Co-IP and functional knockdown with defined phenotype, single lab","pmids":["33898171"],"is_preprint":false},{"year":2023,"finding":"Adenovirus E1A binds DCAF10 to co-opt the CUL4-DDB1-DCAF10 E3 ligase complex, redirecting it to polyubiquitinate RUVBL1 and RUVBL2 AAA+ ATPases for proteasomal degradation. This degradation inhibits IRF3 activation and suppresses innate immune interferon-stimulated gene expression, enabling viral replication.","method":"Affinity purification-mass spectrometry, proteasomal degradation assays, siRNA knockdown of DCAF10, IRF3/ISG expression readouts","journal":"Journal of virology","confidence":"Medium","confidence_rationale":"Tier 2 — AP-MS identification plus functional knockdown with defined immune phenotype, single lab","pmids":["37962355"],"is_preprint":false},{"year":2025,"finding":"The CUL4/DDB1/DCAF10 E3 ligase complex mediates proteasome-dependent degradation of ALOX15B in KRAS-mutant pancreatic cancer. ABHD17C-mediated depalmitoylation and cytoplasmic translocation of ALOX15B facilitates its recognition and ubiquitination by CUL4/DDB1/DCAF10, enabling ferroptosis evasion.","method":"Co-immunoprecipitation, proteasomal degradation assays, KRAS/ERK pathway manipulation, in vitro and in vivo tumor models","journal":"Advanced science (Weinheim, Baden-Wurttemberg, Germany)","confidence":"Medium","confidence_rationale":"Tier 2 — Co-IP establishing complex interaction with functional degradation assays in vitro and in vivo, single lab","pmids":["40569151"],"is_preprint":false},{"year":2026,"finding":"DCAF10 is the substrate receptor within the CUL4A-DDB1-DCAF10 E3 ubiquitin ligase complex that specifically recognizes N-terminally acetylated Src-family kinases (SFKs). When SFKs lack N-terminal myristoylation and are instead N-terminally acetylated, DCAF10 recognizes the acetylated glycine residue as an N-degron, and the reconstituted CUL4A-DDB1-DCAF10 complex ubiquitinates these SFKs in vitro, defining a novel Ac/N-degron pathway that monitors myristoylation status.","method":"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, siRNA knockdown and CRISPR/Cas9 knockout of Lyn, inducible Lyn-GFP variants, in vitro ubiquitination reconstitution assay","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 1 — in vitro reconstitution of ubiquitination with mutagenesis (acetylated vs myristoylated N-terminus), structural predictions, and CRISPR KO validation with multiple orthogonal methods","pmids":["41484149"],"is_preprint":false}],"current_model":"DCAF10 functions as the substrate receptor subunit of the CUL4A-DDB1-DCAF10 E3 ubiquitin ligase complex, recognizing substrates including N-terminally acetylated Src-family kinases (via an Ac/N-degron mechanism), ALOX15B (upon depalmitoylation in KRAS-mutant cancer), and RUVBL1/2 (when co-opted by adenovirus E1A), and it can be stabilized by the deubiquitinase OTUD1 to promote MCL1 degradation and apoptosis."},"narrative":{"teleology":[{"year":2021,"claim":"Establishing that DCAF10 operates within the CUL4A–DDB1 E3 ligase axis to degrade MCL1 answered how this substrate receptor connects to apoptotic signaling, and revealed that DCAF10 itself is regulated by OTUD1-mediated deubiquitination.","evidence":"Co-immunoprecipitation, deubiquitination assays, and overexpression/knockdown studies with apoptosis readouts in cell lines","pmids":["33898171"],"confidence":"Medium","gaps":["Single-lab study; independent replication of the OTUD1–DCAF10–MCL1 axis is lacking","Direct binding interface between DCAF10 and MCL1 is undefined","In vivo physiological relevance of OTUD1 regulation of DCAF10 is unexplored"]},{"year":2023,"claim":"Demonstrating that adenovirus E1A hijacks CUL4–DDB1–DCAF10 to degrade RUVBL1/2 and suppress interferon signaling revealed that DCAF10 can be redirected to non-endogenous substrates by viral factors, expanding the functional scope of DCAF-based E3 ligases in host–pathogen interactions.","evidence":"Affinity purification–mass spectrometry identification of E1A–DCAF10 interaction, siRNA knockdown of DCAF10, and IRF3/ISG expression readouts during adenovirus infection","pmids":["37962355"],"confidence":"Medium","gaps":["Single-lab finding; mechanism of E1A-mediated substrate redirection to RUVBL1/2 is not structurally resolved","Whether RUVBL1/2 are endogenous DCAF10 substrates in uninfected cells is unknown","Generalizability to other adenovirus serotypes not tested"]},{"year":2025,"claim":"Identification of ALOX15B as a DCAF10-dependent substrate in KRAS-mutant cancer demonstrated that depalmitoylation-triggered cytoplasmic translocation is the recognition switch, linking lipid modification status to CUL4/DDB1/DCAF10-mediated degradation and ferroptosis evasion.","evidence":"Co-immunoprecipitation, proteasomal degradation assays, KRAS/ERK pathway manipulation, and in vitro/in vivo pancreatic tumor models","pmids":["40569151"],"confidence":"Medium","gaps":["Single-lab study; the direct degron motif on ALOX15B recognized by DCAF10 is not defined","Whether DCAF10 recognizes depalmitoylated ALOX15B via the same binding mode as acetylated substrates is unknown","Therapeutic relevance of targeting the DCAF10–ALOX15B axis is untested"]},{"year":2026,"claim":"Reconstitution of CUL4A–DDB1–DCAF10-mediated ubiquitination of N-terminally acetylated Src-family kinases in vitro defined the Ac/N-degron pathway, establishing that DCAF10 monitors myristoylation status by specifically recognizing Nt-acetylated glycine as a degradation signal.","evidence":"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, CRISPR/Cas9 knockout, inducible Lyn-GFP variants, and in vitro ubiquitination reconstitution","pmids":["41484149"],"confidence":"High","gaps":["No experimental high-resolution structure of DCAF10 bound to an Ac/N-degron peptide exists","Full physiological substrate repertoire of DCAF10 beyond SFKs remains undefined","Whether the Ac/N-degron pathway is conserved across species is not addressed"]},{"year":null,"claim":"The unifying principle governing DCAF10 substrate selection — whether all substrates share a lipid-modification-dependent degron or whether distinct recognition modes exist — remains an open mechanistic question.","evidence":"","pmids":[],"confidence":"Low","gaps":["No experimental crystal or cryo-EM structure of DCAF10 in complex with DDB1 or any substrate","No systematic proteomics-based identification of the full endogenous substrate repertoire","In vivo knockout phenotype in animal models has not been reported"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[0,1,2,3]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1,2,3]}],"localization":[{"term_id":"GO:0005829","term_label":"cytosol","supporting_discovery_ids":[2,3]}],"pathway":[{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[0,1,2,3]},{"term_id":"R-HSA-5357801","term_label":"Programmed Cell Death","supporting_discovery_ids":[0]},{"term_id":"R-HSA-168256","term_label":"Immune System","supporting_discovery_ids":[1]}],"complexes":["CUL4A–DDB1–DCAF10 E3 ubiquitin ligase"],"partners":["DDB1","CUL4A","OTUD1","MCL1","RUVBL1","RUVBL2","ALOX15B"],"other_free_text":[]},"mechanistic_narrative":"DCAF10 is the substrate receptor subunit of the CUL4A–DDB1–DCAF10 E3 ubiquitin ligase complex, directing polyubiquitination and proteasomal degradation of specific substrates. It recognizes N-terminally acetylated Src-family kinases via an Ac/N-degron mechanism that monitors myristoylation status, defining a quality-control pathway for lipid-modified kinases [PMID:41484149]. The same complex is co-opted by adenovirus E1A to degrade the AAA+ ATPases RUVBL1 and RUVBL2, suppressing IRF3-dependent innate immune signaling [PMID:37962355], and mediates degradation of depalmitoylated ALOX15B in KRAS-mutant pancreatic cancer to enable ferroptosis evasion [PMID:40569151]. DCAF10 protein stability is itself regulated by the deubiquitinase OTUD1, which stabilizes DCAF10 to promote CUL4A–DDB1–DCAF10-dependent degradation of the anti-apoptotic protein MCL1 [PMID:33898171]."},"prefetch_data":{"uniprot":{"accession":"Q5QP82","full_name":"DDB1- and CUL4-associated factor 10","aliases":["WD repeat-containing protein 32"],"length_aa":559,"mass_kda":60.6,"function":"May function as a substrate receptor for CUL4-DDB1 E3 ubiquitin-protein ligase complex","subcellular_location":"","url":"https://www.uniprot.org/uniprotkb/Q5QP82/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/DCAF10","classification":"Not Classified","n_dependent_lines":19,"n_total_lines":1208,"dependency_fraction":0.015728476821192054},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"DDB1","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/DCAF10","total_profiled":1310},"omim":[{"mim_id":"620295","title":"DDB1- AND CUL4-ASSOCIATED FACTOR 10; DCAF10","url":"https://www.omim.org/entry/620295"},{"mim_id":"612022","title":"OTU DOMAIN-CONTAINING PROTEIN 1; OTUD1","url":"https://www.omim.org/entry/612022"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Nucleoli fibrillar center","reliability":"Approved"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/DCAF10"},"hgnc":{"alias_symbol":["MGC10765","FLJ23201"],"prev_symbol":["WDR32"]},"alphafold":{"accession":"Q5QP82","domains":[],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5QP82","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q5QP82-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q5QP82-F1-predicted_aligned_error_v6.png","plddt_mean":69.56},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=DCAF10","jax_strain_url":"https://www.jax.org/strain/search?query=DCAF10"},"sequence":{"accession":"Q5QP82","fasta_url":"https://rest.uniprot.org/uniprotkb/Q5QP82.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q5QP82/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q5QP82"}},"corpus_meta":[{"pmid":"33898171","id":"PMC_33898171","title":"OTUD1 Activates Caspase-Independent and Caspase-Dependent Apoptosis by Promoting AIF Nuclear Translocation and MCL1 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signaling.\",\n      \"method\": \"Co-immunoprecipitation, deubiquitination assays, functional cell-based assays\",\n      \"journal\": \"Advanced Science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — Co-IP and functional assays in a single study; MCL1 degradation linked to CUL4A-DDB1-DCAF10 complex recruitment\",\n      \"pmids\": [\"33898171\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Adenovirus E1A binds DCAF10 to assemble a CUL4-based ubiquitin ligase complex that polyubiquitinates RUVBL1 and RUVBL2, inducing their proteasomal degradation and thereby inhibiting IRF3 activation and interferon-stimulated gene expression.\",\n      \"method\": \"Mass spectrometry, proteasomal degradation assays, gene expression analysis of ISGs\",\n      \"journal\": \"Journal of Virology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — MS-based identification of complex and functional readout (IRF3/ISG suppression) in a single study\",\n      \"pmids\": [\"37962355\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"DCAF10 functions as the substrate receptor (N-recognin) of the CUL4A-DDB1-DCAF10 E3 ubiquitin ligase complex, recognizing an N-terminally acetylated glycine residue on alternatively processed Src-family kinases (SFKs) and promoting their ubiquitination and degradation, defining a novel Ac/N-degron pathway that monitors loss of N-terminal myristoylation.\",\n      \"method\": \"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, siRNA knockdown, CRISPR/Cas9 knockout, inducible Lyn-GFP variants, in vitro ubiquitination reconstitution assay\",\n      \"journal\": \"Nature Communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — in vitro reconstitution of ubiquitination, mutagenesis/variant analysis, CRISPR KO, and structural modeling in a single study with multiple orthogonal methods\",\n      \"pmids\": [\"41484149\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"The CUL4/DDB1/DCAF10 E3 ligase complex mediates proteasome-dependent degradation of ALOX15B after ABHD17C-driven depalmitoylation and cytoplasmic translocation of ALOX15B in KRAS-mutant pancreatic cancer cells.\",\n      \"method\": \"Co-immunoprecipitation, proteasome inhibitor experiments, palmitoylation assays, in vivo and organoid functional studies\",\n      \"journal\": \"Advanced Science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — Co-IP demonstrating complex interaction with ALOX15B and functional degradation assays, single study\",\n      \"pmids\": [\"40569151\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"DCAF10 is a substrate receptor (N-recognin) of the CUL4A-DDB1 E3 ubiquitin ligase complex that recognizes N-terminally acetylated substrates — including Src-family kinases (via an Ac/N-degron pathway) and ALOX15B — promoting their polyubiquitination and proteasomal degradation; the complex is also co-opted by adenovirus E1A to degrade RUVBL1/2 and suppress innate immunity, and is stabilized by the deubiquitinase OTUD1 to drive MCL1 degradation and apoptosis.\"\n}\n```\n\n--- ROUND 2 (R2/R3, augmented corpus) ---\n\nI'll classify each paper first, then extract discoveries only from KEPT papers.\n\n**Classification:**\n\n1. PMID:33898171 — KEEP: Describes OTUD1 stabilizing DCAF10 and recruiting CUL4A-DDB1-DCAF10 complex to degrade MCL1.\n2. PMID:28336923 — EXCLUDE: Expression/omics analysis only, no mechanistic experiments on DCAF10.\n3. PMID:40569151 — KEEP: Describes CUL4/DDB1/DCAF10 E3 ligase complex mediating ALOX15B degradation.\n4. PMID:35968900 — EXCLUDE: Bioinformatics/network analysis only, no mechanistic experiments.\n5. PMID:37962355 — KEEP: Describes adenovirus E1A binding DCAF10 to target RUVBL1/2 for proteasomal degradation.\n6. PMID:41484149 — KEEP: Defines DCAF10 as E3 ligase substrate receptor for N-terminally acetylated SFKs.\n7. PMID:16169070 — EXCLUDE: General PPI screen, not mechanistically focused on DCAF10.\n8. PMID:12477932 — EXCLUDE: cDNA sequencing project.\n9. PMID:26186194 — EXCLUDE: General interactome mapping.\n10. PMID:28514442 — EXCLUDE: General interactome mapping.\n11. PMID:26496610 — EXCLUDE: General interactome mapping.\n12. PMID:32296183 — EXCLUDE: General interactome mapping.\n13. PMID:14702039 — EXCLUDE: cDNA sequencing project.\n14. PMID:33961781 — EXCLUDE: General interactome mapping.\n15. PMID:21873635 — EXCLUDE: GO annotation methodology.\n16. PMID:16964240 — EXCLUDE: About DDB1-CUL4A machinery generally, DCAF10 not specifically studied.\n17. PMID:33060197 — EXCLUDE: Coronavirus-host interactions, not DCAF10-specific.\n18. PMID:16949367 — EXCLUDE: About DCAFs generally, DCAF10 not specifically studied mechanistically.\n19. PMID:31257023 — EXCLUDE: About Bach1/Fbxo22, not DCAF10.\n20. PMID:35271311 — EXCLUDE: General proteome cartography.\n21. PMID:20360068 — EXCLUDE: General complex analysis.\n22. PMID:26331536 — EXCLUDE: About p53 mutants/chromatin.\n23. PMID:19596235 — EXCLUDE: About SLX4/BTBD12.\n24. PMID:21145461 — EXCLUDE: General CRL network analysis.\n25. PMID:25544563 — EXCLUDE: About herpesvirus-host interactions.\n26. PMID:32814053 — EXCLUDE: Neurodegenerative disease interactome.\n27. PMID:26972000 — EXCLUDE: About PHD3/FIH hydroxylases.\n28. PMID:35652658 — EXCLUDE: About SARS-CoV-2 N protein.\n29. PMID:19295130 — EXCLUDE: About COP9 signalosome/Dda1.\n30. PMID:24778252 — EXCLUDE: About TRIM65/TNRC6.\n31. PMID:31973889 — EXCLUDE: General CRL4 network analysis.\n32. PMID:28298427 — EXCLUDE: GPCR interactome.\n33. PMID:36950384 — EXCLUDE: ASD protein interactions.\n34. PMID:26167880 — EXCLUDE: About SR protein kinases in yeast.\n\n```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"OTUD1 stabilizes DCAF10 and recruits the CUL4A-DDB1-DCAF10 E3 ligase complex to promote polyubiquitination and proteasomal degradation of MCL1, thereby activating caspase-dependent apoptotic signaling. OTUD1 deubiquitinates and stabilizes DCAF10, linking the deubiquitinase to the CUL4A-based ubiquitin ligase machinery.\",\n      \"method\": \"Co-immunoprecipitation, deubiquitination assays, overexpression/knockdown with apoptosis readouts, MCL1 degradation assays\",\n      \"journal\": \"Advanced science (Weinheim, Baden-Wurttemberg, Germany)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — reciprocal Co-IP and functional knockdown with defined phenotype, single lab\",\n      \"pmids\": [\"33898171\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"Adenovirus E1A binds DCAF10 to co-opt the CUL4-DDB1-DCAF10 E3 ligase complex, redirecting it to polyubiquitinate RUVBL1 and RUVBL2 AAA+ ATPases for proteasomal degradation. This degradation inhibits IRF3 activation and suppresses innate immune interferon-stimulated gene expression, enabling viral replication.\",\n      \"method\": \"Affinity purification-mass spectrometry, proteasomal degradation assays, siRNA knockdown of DCAF10, IRF3/ISG expression readouts\",\n      \"journal\": \"Journal of virology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — AP-MS identification plus functional knockdown with defined immune phenotype, single lab\",\n      \"pmids\": [\"37962355\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"The CUL4/DDB1/DCAF10 E3 ligase complex mediates proteasome-dependent degradation of ALOX15B in KRAS-mutant pancreatic cancer. ABHD17C-mediated depalmitoylation and cytoplasmic translocation of ALOX15B facilitates its recognition and ubiquitination by CUL4/DDB1/DCAF10, enabling ferroptosis evasion.\",\n      \"method\": \"Co-immunoprecipitation, proteasomal degradation assays, KRAS/ERK pathway manipulation, in vitro and in vivo tumor models\",\n      \"journal\": \"Advanced science (Weinheim, Baden-Wurttemberg, Germany)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 — Co-IP establishing complex interaction with functional degradation assays in vitro and in vivo, single lab\",\n      \"pmids\": [\"40569151\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"DCAF10 is the substrate receptor within the CUL4A-DDB1-DCAF10 E3 ubiquitin ligase complex that specifically recognizes N-terminally acetylated Src-family kinases (SFKs). When SFKs lack N-terminal myristoylation and are instead N-terminally acetylated, DCAF10 recognizes the acetylated glycine residue as an N-degron, and the reconstituted CUL4A-DDB1-DCAF10 complex ubiquitinates these SFKs in vitro, defining a novel Ac/N-degron pathway that monitors myristoylation status.\",\n      \"method\": \"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, siRNA knockdown and CRISPR/Cas9 knockout of Lyn, inducible Lyn-GFP variants, in vitro ubiquitination reconstitution assay\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 — in vitro reconstitution of ubiquitination with mutagenesis (acetylated vs myristoylated N-terminus), structural predictions, and CRISPR KO validation with multiple orthogonal methods\",\n      \"pmids\": [\"41484149\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"DCAF10 functions as the substrate receptor subunit of the CUL4A-DDB1-DCAF10 E3 ubiquitin ligase complex, recognizing substrates including N-terminally acetylated Src-family kinases (via an Ac/N-degron mechanism), ALOX15B (upon depalmitoylation in KRAS-mutant cancer), and RUVBL1/2 (when co-opted by adenovirus E1A), and it can be stabilized by the deubiquitinase OTUD1 to promote MCL1 degradation and apoptosis.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"DCAF10 is a substrate receptor (DCAF/WDR protein) of the CUL4A–DDB1 E3 ubiquitin ligase complex that targets diverse substrates for polyubiquitination and proteasomal degradation. DCAF10 functions as an N-recognin that recognizes N-terminally acetylated glycine residues on alternatively processed Src-family kinases, defining an Ac/N-degron quality-control pathway that monitors loss of N-terminal myristoylation [PMID:41484149]. Additional substrates of the CUL4A–DDB1–DCAF10 complex include the anti-apoptotic protein MCL1, whose degradation is promoted when the deubiquitinase OTUD1 stabilizes DCAF10 to activate caspase-dependent apoptosis [PMID:33898171], and ALOX15B, which is targeted for degradation following depalmitoylation-driven cytoplasmic translocation in KRAS-mutant pancreatic cancer cells [PMID:40569151]. The complex is co-opted by adenovirus E1A, which binds DCAF10 to redirect ubiquitination toward RUVBL1 and RUVBL2, resulting in their degradation and suppression of IRF3-dependent innate immune signaling [PMID:37962355].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Establishing that DCAF10 operates within a CUL4A–DDB1 E3 ligase complex with biological consequence: OTUD1-mediated stabilization of DCAF10 recruits the complex to MCL1, promoting MCL1 degradation and caspase-dependent apoptosis — the first demonstration that DCAF10 functions as a substrate receptor with a defined physiological output.\",\n      \"evidence\": \"Co-immunoprecipitation, deubiquitination assays, and functional cell-based apoptosis assays\",\n      \"pmids\": [\"33898171\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"MCL1 as a direct substrate of DCAF10 has not been confirmed by in vitro reconstitution of ubiquitination\",\n        \"Whether OTUD1 stabilization of DCAF10 is a general regulatory mechanism or context-specific is unknown\",\n        \"The degron on MCL1 recognized by DCAF10 has not been mapped\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Revealing that viral pathogens exploit DCAF10: adenovirus E1A hijacks the CUL4–DDB1–DCAF10 complex to polyubiquitinate RUVBL1/2, leading to their proteasomal degradation and suppression of IRF3 activation and interferon-stimulated gene expression — establishing DCAF10 as a node in innate immune evasion.\",\n      \"evidence\": \"Mass spectrometry identification of the E1A–DCAF10 complex, proteasomal degradation assays, and ISG expression analysis\",\n      \"pmids\": [\"37962355\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The interface between E1A and DCAF10 has not been structurally resolved\",\n        \"Whether DCAF10 normally regulates RUVBL1/2 in uninfected cells is unknown\",\n        \"Single study without independent replication\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Expanding the substrate repertoire beyond signaling proteins: CUL4–DDB1–DCAF10 degrades ALOX15B after ABHD17C-mediated depalmitoylation causes its cytoplasmic translocation in KRAS-mutant pancreatic cancer, linking DCAF10 to lipid metabolism and tumor biology.\",\n      \"evidence\": \"Co-immunoprecipitation, proteasome inhibitor experiments, palmitoylation assays, in vivo and organoid functional studies\",\n      \"pmids\": [\"40569151\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The degron or recognition motif on ALOX15B that DCAF10 reads has not been identified\",\n        \"In vitro reconstitution of DCAF10-dependent ALOX15B ubiquitination is lacking\",\n        \"Single study in KRAS-mutant context; generality to other tissues unknown\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Defining the molecular recognition mechanism: DCAF10 is an N-recognin that binds N-terminally acetylated glycine residues exposed when Src-family kinases lose their myristoyl modification, establishing a bona fide Ac/N-degron pathway — the first mechanistic explanation for how DCAF10 selects its substrates.\",\n      \"evidence\": \"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, siRNA/CRISPR knockout, inducible Lyn-GFP variants, and in vitro ubiquitination reconstitution\",\n      \"pmids\": [\"41484149\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"A high-resolution experimental structure of DCAF10 bound to an Ac/N-degron peptide is not yet available (modeling relied on AlphaFold 3)\",\n        \"Whether all DCAF10 substrates (MCL1, ALOX15B, RUVBL1/2) are recognized through the same Ac/N-degron mechanism is unknown\",\n        \"The physiological contexts in which Src-family kinase myristoylation is lost, triggering this pathway in vivo, remain to be mapped\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"Open question: whether all known DCAF10 substrates share a common Ac/N-degron recognition mode or whether DCAF10 uses distinct binding surfaces for different substrates remains unresolved, and no experimental atomic-resolution structure of DCAF10 exists.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No crystal or cryo-EM structure of the DDB1–DCAF10 complex or DCAF10 alone\",\n        \"Unified versus multi-modal substrate recognition by DCAF10 untested\",\n        \"Tissue-specific roles and regulation of DCAF10 protein levels beyond OTUD1 are unexplored\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\n        \"term_id\": \"GO:0098772\",\n        \"supporting_discovery_ids\": [0, 1, 2, 3]\n      }\n    ],\n    \"localization\": [\n      {\n        \"term_id\": \"GO:0005829\",\n        \"supporting_discovery_ids\": [2, 3]\n      }\n    ],\n    \"pathway\": [\n      {\n        \"term_id\": \"R-HSA-392499\",\n        \"supporting_discovery_ids\": [0, 1, 2, 3]\n      },\n      {\n        \"term_id\": \"R-HSA-5357801\",\n        \"supporting_discovery_ids\": [0]\n      },\n      {\n        \"term_id\": \"R-HSA-168256\",\n        \"supporting_discovery_ids\": [1]\n      }\n    ],\n    \"complexes\": [\n      \"CUL4A-DDB1-DCAF10 E3 ubiquitin ligase\"\n    ],\n    \"partners\": [\n      \"DDB1\",\n      \"CUL4A\",\n      \"OTUD1\",\n      \"MCL1\",\n      \"RUVBL1\",\n      \"RUVBL2\",\n      \"ALOX15B\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```\n\n--- ROUND 2 (R2/R3, augmented corpus) ---\n\n```json\n{\n  \"mechanistic_narrative\": \"DCAF10 is the substrate receptor subunit of the CUL4A–DDB1–DCAF10 E3 ubiquitin ligase complex, directing polyubiquitination and proteasomal degradation of specific substrates. It recognizes N-terminally acetylated Src-family kinases via an Ac/N-degron mechanism that monitors myristoylation status, defining a quality-control pathway for lipid-modified kinases [PMID:41484149]. The same complex is co-opted by adenovirus E1A to degrade the AAA+ ATPases RUVBL1 and RUVBL2, suppressing IRF3-dependent innate immune signaling [PMID:37962355], and mediates degradation of depalmitoylated ALOX15B in KRAS-mutant pancreatic cancer to enable ferroptosis evasion [PMID:40569151]. DCAF10 protein stability is itself regulated by the deubiquitinase OTUD1, which stabilizes DCAF10 to promote CUL4A–DDB1–DCAF10-dependent degradation of the anti-apoptotic protein MCL1 [PMID:33898171].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Establishing that DCAF10 operates within the CUL4A–DDB1 E3 ligase axis to degrade MCL1 answered how this substrate receptor connects to apoptotic signaling, and revealed that DCAF10 itself is regulated by OTUD1-mediated deubiquitination.\",\n      \"evidence\": \"Co-immunoprecipitation, deubiquitination assays, and overexpression/knockdown studies with apoptosis readouts in cell lines\",\n      \"pmids\": [\"33898171\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single-lab study; independent replication of the OTUD1–DCAF10–MCL1 axis is lacking\",\n        \"Direct binding interface between DCAF10 and MCL1 is undefined\",\n        \"In vivo physiological relevance of OTUD1 regulation of DCAF10 is unexplored\"\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Demonstrating that adenovirus E1A hijacks CUL4–DDB1–DCAF10 to degrade RUVBL1/2 and suppress interferon signaling revealed that DCAF10 can be redirected to non-endogenous substrates by viral factors, expanding the functional scope of DCAF-based E3 ligases in host–pathogen interactions.\",\n      \"evidence\": \"Affinity purification–mass spectrometry identification of E1A–DCAF10 interaction, siRNA knockdown of DCAF10, and IRF3/ISG expression readouts during adenovirus infection\",\n      \"pmids\": [\"37962355\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single-lab finding; mechanism of E1A-mediated substrate redirection to RUVBL1/2 is not structurally resolved\",\n        \"Whether RUVBL1/2 are endogenous DCAF10 substrates in uninfected cells is unknown\",\n        \"Generalizability to other adenovirus serotypes not tested\"\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Identification of ALOX15B as a DCAF10-dependent substrate in KRAS-mutant cancer demonstrated that depalmitoylation-triggered cytoplasmic translocation is the recognition switch, linking lipid modification status to CUL4/DDB1/DCAF10-mediated degradation and ferroptosis evasion.\",\n      \"evidence\": \"Co-immunoprecipitation, proteasomal degradation assays, KRAS/ERK pathway manipulation, and in vitro/in vivo pancreatic tumor models\",\n      \"pmids\": [\"40569151\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Single-lab study; the direct degron motif on ALOX15B recognized by DCAF10 is not defined\",\n        \"Whether DCAF10 recognizes depalmitoylated ALOX15B via the same binding mode as acetylated substrates is unknown\",\n        \"Therapeutic relevance of targeting the DCAF10–ALOX15B axis is untested\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Reconstitution of CUL4A–DDB1–DCAF10-mediated ubiquitination of N-terminally acetylated Src-family kinases in vitro defined the Ac/N-degron pathway, establishing that DCAF10 monitors myristoylation status by specifically recognizing Nt-acetylated glycine as a degradation signal.\",\n      \"evidence\": \"Peptide pull-downs, mass spectrometry, AlphaFold 3 structural predictions, CRISPR/Cas9 knockout, inducible Lyn-GFP variants, and in vitro ubiquitination reconstitution\",\n      \"pmids\": [\"41484149\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"No experimental high-resolution structure of DCAF10 bound to an Ac/N-degron peptide exists\",\n        \"Full physiological substrate repertoire of DCAF10 beyond SFKs remains undefined\",\n        \"Whether the Ac/N-degron pathway is conserved across species is not addressed\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The unifying principle governing DCAF10 substrate selection — whether all substrates share a lipid-modification-dependent degron or whether distinct recognition modes exist — remains an open mechanistic question.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No experimental crystal or cryo-EM structure of DCAF10 in complex with DDB1 or any substrate\",\n        \"No systematic proteomics-based identification of the full endogenous substrate repertoire\",\n        \"In vivo knockout phenotype in animal models has not been reported\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [0, 1, 2, 3]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 1, 2, 3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005829\", \"supporting_discovery_ids\": [2, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [0, 1, 2, 3]},\n      {\"term_id\": \"R-HSA-5357801\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-168256\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\n      \"CUL4A–DDB1–DCAF10 E3 ubiquitin ligase\"\n    ],\n    \"partners\": [\n      \"DDB1\",\n      \"CUL4A\",\n      \"OTUD1\",\n      \"MCL1\",\n      \"RUVBL1\",\n      \"RUVBL2\",\n      \"ALOX15B\"\n    ],\n    \"other_free_text\": []\n  }\n}\n```"}