{"gene":"KLHL23","run_date":"2026-06-10T02:59:49","timeline":{"discoveries":[{"year":2025,"finding":"KLHL23 acts as the substrate-recognition adaptor of a CUL3-based E3 ubiquitin ligase complex that specifically polyubiquitylates the GTP-bound (active) form of CDC42, targeting it for proteasomal degradation. KLHL23 and RhoGDI compete for the CDC42 switch II region, with KLHL23 preferentially recognizing CDC42•GTP and RhoGDI preferentially sequestering CDC42•GDP, together achieving spatiotemporal co-inactivation of CDC42.","method":"Biochemical reconstitution of KLHL23-Cul3 E3 ligase activity toward CDC42•GTP; competitive binding assays between KLHL23 and RhoGDI for the CDC42 switch II region; FRET assays for spatiotemporal CDC42 inactivation in cells; loss-of-function depletion with membrane-protrusion and metastasis phenotypic readouts; germline CDC42-Y64C variant shown to escape KLHL23-mediated degradation","journal":"Nature chemical biology","confidence":"High","confidence_rationale":"Tier 1 / Strong — in vitro reconstitution of E3 ligase activity, mutagenesis/variant validation (Y64C), competitive binding assays, and FRET in live cells, all in a single rigorous study with multiple orthogonal methods","pmids":["40846997"],"is_preprint":false},{"year":2018,"finding":"KLHL23 directly binds to actin and suppresses actin polymerization; KLHL23 silencing induced filopodium and lamellipodium formation, and activated actin cytoskeleton remodeling, which augmented cellular hypoxic responses in a cell-density-dependent manner, activating HIF and Notch signaling to drive EMT in hepatocellular carcinoma cells.","method":"Subgenome-wide screen for invasion suppressors; KLHL23 silencing with morphological readouts (filopodia, lamellipodia); actin polymerization assays; HIF/Notch signaling measurements after KLHL23 KD; rescue with actin polymerization inhibitors or ATP supplementation; patient-derived xenograft validation","journal":"Hepatology (Baltimore, Md.)","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct binding to actin and suppression of polymerization demonstrated, multiple functional readouts, but binding mechanism not fully reconstituted in vitro; single lab","pmids":["29171033"],"is_preprint":false},{"year":2021,"finding":"KLHL23 localizes to actin stress fibers in invasive leading cells during migration and promotes focal adhesion complex formation; knockdown of KLHL23 abolishes actin stress fibers, translocates vinculin to the perimembrane, and enhances cancer cell mobility in urothelial carcinoma.","method":"Wound healing assay; KLHL23 knockdown with vinculin localization readout by fluorescence microscopy; co-localization of KLHL23 with actin fibers; focal adhesion formation assays","journal":"The Chinese journal of physiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization to actin fibers tied to functional consequence (vinculin translocation, altered migration); single lab with two orthogonal methods","pmids":["34169920"],"is_preprint":false},{"year":2016,"finding":"Overexpression of KLHL23 protein (derived from PHOSPHO2-KLHL23 read-through transcript) in gastric cancer cells increases cell proliferation, and silencing of KLHL23 expression decreases cyclin D1 levels.","method":"Overexpression and siRNA silencing of KLHL23 in gastric cancer cell lines; cell proliferation assays; Western blot for cyclin D1","journal":"FEBS open bio","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single expression system; mechanistic link between KLHL23 and cyclin D1 not directly established beyond correlation with knockdown","pmids":["27833855"],"is_preprint":false}],"current_model":"KLHL23 is the substrate-recognition subunit of a CUL3 RING E3 ubiquitin ligase that polyubiquitylates active (GTP-bound) CDC42 for proteasomal degradation; together with RhoGDI—which sequesters GDP-bound CDC42—KLHL23 spatiotemporally co-inactivates CDC42, restraining actin cytoskeleton remodeling, membrane protrusion, and EMT-driven metastasis."},"narrative":{"mechanistic_narrative":"KLHL23 is a substrate-recognition adaptor that couples a CUL3 RING E3 ubiquitin ligase to the control of actin cytoskeleton dynamics, restraining cell migration, membrane protrusion, and EMT-driven metastasis [PMID:40846997, PMID:29171033]. Mechanistically, KLHL23 selects the GTP-bound (active) form of CDC42 for polyubiquitylation and proteasomal degradation, engaging the CDC42 switch II region in competition with RhoGDI, which instead sequesters the GDP-bound form; together they achieve spatiotemporal co-inactivation of CDC42, and a germline CDC42-Y64C variant escapes this KLHL23-mediated turnover [PMID:40846997]. Consistent with negative regulation of CDC42-driven actin remodeling, KLHL23 directly binds actin and suppresses its polymerization, and its loss induces filopodia and lamellipodia and activates hypoxic HIF/Notch signaling to drive EMT in hepatocellular carcinoma [PMID:29171033]; KLHL23 also localizes to actin stress fibers in leading migratory cells and promotes focal adhesion formation, with its depletion abolishing stress fibers, redistributing vinculin, and enhancing cancer cell motility [PMID:34169920].","teleology":[{"year":2016,"claim":"An initial functional link tied KLHL23 expression to cancer cell growth, raising the question of whether the protein had a defined molecular role beyond a proliferation correlate.","evidence":"Overexpression and siRNA silencing in gastric cancer cell lines with proliferation assays and cyclin D1 Western blot","pmids":["27833855"],"confidence":"Low","gaps":["Mechanistic link to cyclin D1 is correlative, not direct","Single lab and single expression system","KLHL23 derived from a PHOSPHO2-KLHL23 read-through transcript, leaving the native gene product's role ambiguous"]},{"year":2018,"claim":"The question of KLHL23's biochemical action was addressed by showing it directly engages and restrains the actin cytoskeleton, establishing it as an invasion/EMT suppressor rather than a generic proliferation factor.","evidence":"Subgenome-wide invasion-suppressor screen, actin binding and polymerization assays, morphological readouts, HIF/Notch signaling measurements, and patient-derived xenograft validation in hepatocellular carcinoma","pmids":["29171033"],"confidence":"Medium","gaps":["Direct actin-binding mechanism not reconstituted in vitro","Did not connect actin suppression to KLHL23's adaptor function","Single lab"]},{"year":2021,"claim":"The cell-biological basis of migration control was refined by localizing KLHL23 to actin stress fibers and linking it to focal adhesion organization.","evidence":"Wound-healing assay, KLHL23 knockdown with vinculin localization imaging, and co-localization with actin fibers in urothelial carcinoma","pmids":["34169920"],"confidence":"Medium","gaps":["Molecular basis of stress-fiber localization unresolved","Relationship to actin-binding versus E3 adaptor activity not defined","Single lab"]},{"year":2025,"claim":"The unifying mechanism was established by showing KLHL23 is the CUL3 substrate adaptor that selectively ubiquitylates active CDC42 and co-inactivates it with RhoGDI, explaining how it restrains actin remodeling and metastasis.","evidence":"In vitro reconstitution of KLHL23-CUL3 E3 ligase activity toward CDC42•GTP, KLHL23/RhoGDI competitive binding assays at the switch II region, live-cell FRET, depletion with protrusion/metastasis readouts, and CDC42-Y64C escape variant","pmids":["40846997"],"confidence":"High","gaps":["Whether KLHL23 ubiquitylates Rho-family GTPases beyond CDC42 is undefined","Mechanistic relationship between direct actin binding (#1) and CUL3-dependent CDC42 degradation not integrated","Upstream signals controlling KLHL23 activity unknown"]},{"year":null,"claim":"How KLHL23's two reported biochemical activities—direct actin binding and CUL3-mediated CDC42 ubiquitylation—are mechanistically reconciled, and what regulates KLHL23 itself, remain open.","evidence":"","pmids":[],"confidence":"High","gaps":["No structural model of the KLHL23-CUL3-CDC42 complex","Substrate range beyond CDC42 unmapped","Regulation of KLHL23 abundance and recruitment unknown"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0140096","term_label":"catalytic activity, acting on a protein","supporting_discovery_ids":[0]},{"term_id":"GO:0016874","term_label":"ligase activity","supporting_discovery_ids":[0]},{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0]},{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[1,2]}],"localization":[{"term_id":"GO:0005856","term_label":"cytoskeleton","supporting_discovery_ids":[1,2]}],"pathway":[{"term_id":"R-HSA-392499","term_label":"Metabolism of proteins","supporting_discovery_ids":[0]},{"term_id":"R-HSA-162582","term_label":"Signal Transduction","supporting_discovery_ids":[0,1]}],"complexes":["CUL3-RING E3 ubiquitin ligase"],"partners":["CUL3","CDC42","ACTB"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q8NBE8","full_name":"Kelch-like protein 23","aliases":[],"length_aa":558,"mass_kda":63.9,"function":"","subcellular_location":"","url":"https://www.uniprot.org/uniprotkb/Q8NBE8/entry"},"depmap":{"release":"DepMap","has_data":false,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/KLHL23"},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/KLHL23","total_profiled":1310},"omim":[],"hpa":{"profiled":true,"resolved_as":"","reliability":"Approved","locations":[{"location":"Actin filaments","reliability":"Approved"},{"location":"Nucleoplasm","reliability":"Additional"}],"tissue_specificity":"Low tissue specificity","tissue_distribution":"Detected in all","driving_tissues":[],"url":"https://www.proteinatlas.org/search/KLHL23"},"hgnc":{"alias_symbol":["MGC2610","FLJ37812","MGC22679"],"prev_symbol":[]},"alphafold":{"accession":"Q8NBE8","domains":[{"cath_id":"3.30.710.10","chopping":"17-133","consensus_level":"high","plddt":93.0746,"start":17,"end":133},{"cath_id":"1.25.40","chopping":"164-257","consensus_level":"medium","plddt":84.1927,"start":164,"end":257},{"cath_id":"2.120.10.80","chopping":"273-554","consensus_level":"medium","plddt":94.2922,"start":273,"end":554}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8NBE8","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q8NBE8-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q8NBE8-F1-predicted_aligned_error_v6.png","plddt_mean":90.19},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=KLHL23","jax_strain_url":"https://www.jax.org/strain/search?query=KLHL23"},"sequence":{"accession":"Q8NBE8","fasta_url":"https://rest.uniprot.org/uniprotkb/Q8NBE8.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q8NBE8/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q8NBE8"}},"corpus_meta":[{"pmid":"29171033","id":"PMC_29171033","title":"Actin cytoskeleton remodeling drives epithelial-mesenchymal transition for hepatoma invasion and metastasis in mice.","date":"2018","source":"Hepatology (Baltimore, Md.)","url":"https://pubmed.ncbi.nlm.nih.gov/29171033","citation_count":121,"is_preprint":false},{"pmid":"34343486","id":"PMC_34343486","title":"Dysfunction of Cullin 3 RING E3 ubiquitin ligase causes vasoconstriction and increased sodium reabsorption in diabetes.","date":"2021","source":"Archives of biochemistry and biophysics","url":"https://pubmed.ncbi.nlm.nih.gov/34343486","citation_count":22,"is_preprint":false},{"pmid":"27833855","id":"PMC_27833855","title":"Overexpression of KLHL23 protein from read-through transcription of PHOSPHO2-KLHL23 in gastric cancer increases cell proliferation.","date":"2016","source":"FEBS open bio","url":"https://pubmed.ncbi.nlm.nih.gov/27833855","citation_count":19,"is_preprint":false},{"pmid":"21496248","id":"PMC_21496248","title":"A novel locus (CORD12) for autosomal dominant cone-rod dystrophy on chromosome 2q24.2-2q33.1.","date":"2011","source":"BMC medical genetics","url":"https://pubmed.ncbi.nlm.nih.gov/21496248","citation_count":5,"is_preprint":false},{"pmid":"34169920","id":"PMC_34169920","title":"Confirming whether KLHL23 deficiency potentiates migration in urothelial carcinoma.","date":"2021","source":"The Chinese journal of physiology","url":"https://pubmed.ncbi.nlm.nih.gov/34169920","citation_count":4,"is_preprint":false},{"pmid":"39636292","id":"PMC_39636292","title":"Unveiling KLHL23 as a key immune regulator in hepatocellular carcinoma through integrated analysis.","date":"2024","source":"Aging","url":"https://pubmed.ncbi.nlm.nih.gov/39636292","citation_count":2,"is_preprint":false},{"pmid":"40846997","id":"PMC_40846997","title":"KLHL23 and RhoGDI coordinate CDC42 inactivation ensuring membrane homeostasis.","date":"2025","source":"Nature chemical biology","url":"https://pubmed.ncbi.nlm.nih.gov/40846997","citation_count":1,"is_preprint":false},{"pmid":"41608197","id":"PMC_41608197","title":"PFAS Alter Thyroid Histology and Cellular Signaling In Vitro and In Vivo.","date":"2025","source":"Journal of the Endocrine Society","url":"https://pubmed.ncbi.nlm.nih.gov/41608197","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6197,"output_tokens":1279,"usd":0.018888,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7907,"output_tokens":2124,"usd":0.046317,"stage2_stop_reason":"end_turn"},"total_usd":0.065205,"stage1_batch_id":"msgbatch_01BbTCMyrRPyhtEq6b1MdwCN","stage2_batch_id":"msgbatch_011dEed5bbxYvTAaQWKJevxu","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2025,\n      \"finding\": \"KLHL23 acts as the substrate-recognition adaptor of a CUL3-based E3 ubiquitin ligase complex that specifically polyubiquitylates the GTP-bound (active) form of CDC42, targeting it for proteasomal degradation. KLHL23 and RhoGDI compete for the CDC42 switch II region, with KLHL23 preferentially recognizing CDC42•GTP and RhoGDI preferentially sequestering CDC42•GDP, together achieving spatiotemporal co-inactivation of CDC42.\",\n      \"method\": \"Biochemical reconstitution of KLHL23-Cul3 E3 ligase activity toward CDC42•GTP; competitive binding assays between KLHL23 and RhoGDI for the CDC42 switch II region; FRET assays for spatiotemporal CDC42 inactivation in cells; loss-of-function depletion with membrane-protrusion and metastasis phenotypic readouts; germline CDC42-Y64C variant shown to escape KLHL23-mediated degradation\",\n      \"journal\": \"Nature chemical biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — in vitro reconstitution of E3 ligase activity, mutagenesis/variant validation (Y64C), competitive binding assays, and FRET in live cells, all in a single rigorous study with multiple orthogonal methods\",\n      \"pmids\": [\"40846997\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"KLHL23 directly binds to actin and suppresses actin polymerization; KLHL23 silencing induced filopodium and lamellipodium formation, and activated actin cytoskeleton remodeling, which augmented cellular hypoxic responses in a cell-density-dependent manner, activating HIF and Notch signaling to drive EMT in hepatocellular carcinoma cells.\",\n      \"method\": \"Subgenome-wide screen for invasion suppressors; KLHL23 silencing with morphological readouts (filopodia, lamellipodia); actin polymerization assays; HIF/Notch signaling measurements after KLHL23 KD; rescue with actin polymerization inhibitors or ATP supplementation; patient-derived xenograft validation\",\n      \"journal\": \"Hepatology (Baltimore, Md.)\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct binding to actin and suppression of polymerization demonstrated, multiple functional readouts, but binding mechanism not fully reconstituted in vitro; single lab\",\n      \"pmids\": [\"29171033\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"KLHL23 localizes to actin stress fibers in invasive leading cells during migration and promotes focal adhesion complex formation; knockdown of KLHL23 abolishes actin stress fibers, translocates vinculin to the perimembrane, and enhances cancer cell mobility in urothelial carcinoma.\",\n      \"method\": \"Wound healing assay; KLHL23 knockdown with vinculin localization readout by fluorescence microscopy; co-localization of KLHL23 with actin fibers; focal adhesion formation assays\",\n      \"journal\": \"The Chinese journal of physiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization to actin fibers tied to functional consequence (vinculin translocation, altered migration); single lab with two orthogonal methods\",\n      \"pmids\": [\"34169920\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Overexpression of KLHL23 protein (derived from PHOSPHO2-KLHL23 read-through transcript) in gastric cancer cells increases cell proliferation, and silencing of KLHL23 expression decreases cyclin D1 levels.\",\n      \"method\": \"Overexpression and siRNA silencing of KLHL23 in gastric cancer cell lines; cell proliferation assays; Western blot for cyclin D1\",\n      \"journal\": \"FEBS open bio\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single expression system; mechanistic link between KLHL23 and cyclin D1 not directly established beyond correlation with knockdown\",\n      \"pmids\": [\"27833855\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"KLHL23 is the substrate-recognition subunit of a CUL3 RING E3 ubiquitin ligase that polyubiquitylates active (GTP-bound) CDC42 for proteasomal degradation; together with RhoGDI—which sequesters GDP-bound CDC42—KLHL23 spatiotemporally co-inactivates CDC42, restraining actin cytoskeleton remodeling, membrane protrusion, and EMT-driven metastasis.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"KLHL23 is a substrate-recognition adaptor that couples a CUL3 RING E3 ubiquitin ligase to the control of actin cytoskeleton dynamics, restraining cell migration, membrane protrusion, and EMT-driven metastasis [#0, #1]. Mechanistically, KLHL23 selects the GTP-bound (active) form of CDC42 for polyubiquitylation and proteasomal degradation, engaging the CDC42 switch II region in competition with RhoGDI, which instead sequesters the GDP-bound form; together they achieve spatiotemporal co-inactivation of CDC42, and a germline CDC42-Y64C variant escapes this KLHL23-mediated turnover [#0]. Consistent with negative regulation of CDC42-driven actin remodeling, KLHL23 directly binds actin and suppresses its polymerization, and its loss induces filopodia and lamellipodia and activates hypoxic HIF/Notch signaling to drive EMT in hepatocellular carcinoma [#1]; KLHL23 also localizes to actin stress fibers in leading migratory cells and promotes focal adhesion formation, with its depletion abolishing stress fibers, redistributing vinculin, and enhancing cancer cell motility [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2016,\n      \"claim\": \"An initial functional link tied KLHL23 expression to cancer cell growth, raising the question of whether the protein had a defined molecular role beyond a proliferation correlate.\",\n      \"evidence\": \"Overexpression and siRNA silencing in gastric cancer cell lines with proliferation assays and cyclin D1 Western blot\",\n      \"pmids\": [\"27833855\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Mechanistic link to cyclin D1 is correlative, not direct\", \"Single lab and single expression system\", \"KLHL23 derived from a PHOSPHO2-KLHL23 read-through transcript, leaving the native gene product's role ambiguous\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"The question of KLHL23's biochemical action was addressed by showing it directly engages and restrains the actin cytoskeleton, establishing it as an invasion/EMT suppressor rather than a generic proliferation factor.\",\n      \"evidence\": \"Subgenome-wide invasion-suppressor screen, actin binding and polymerization assays, morphological readouts, HIF/Notch signaling measurements, and patient-derived xenograft validation in hepatocellular carcinoma\",\n      \"pmids\": [\"29171033\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Direct actin-binding mechanism not reconstituted in vitro\", \"Did not connect actin suppression to KLHL23's adaptor function\", \"Single lab\"]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The cell-biological basis of migration control was refined by localizing KLHL23 to actin stress fibers and linking it to focal adhesion organization.\",\n      \"evidence\": \"Wound-healing assay, KLHL23 knockdown with vinculin localization imaging, and co-localization with actin fibers in urothelial carcinoma\",\n      \"pmids\": [\"34169920\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular basis of stress-fiber localization unresolved\", \"Relationship to actin-binding versus E3 adaptor activity not defined\", \"Single lab\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"The unifying mechanism was established by showing KLHL23 is the CUL3 substrate adaptor that selectively ubiquitylates active CDC42 and co-inactivates it with RhoGDI, explaining how it restrains actin remodeling and metastasis.\",\n      \"evidence\": \"In vitro reconstitution of KLHL23-CUL3 E3 ligase activity toward CDC42\\u2022GTP, KLHL23/RhoGDI competitive binding assays at the switch II region, live-cell FRET, depletion with protrusion/metastasis readouts, and CDC42-Y64C escape variant\",\n      \"pmids\": [\"40846997\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Whether KLHL23 ubiquitylates Rho-family GTPases beyond CDC42 is undefined\", \"Mechanistic relationship between direct actin binding (#1) and CUL3-dependent CDC42 degradation not integrated\", \"Upstream signals controlling KLHL23 activity unknown\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How KLHL23's two reported biochemical activities\\u2014direct actin binding and CUL3-mediated CDC42 ubiquitylation\\u2014are mechanistically reconciled, and what regulates KLHL23 itself, remain open.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No structural model of the KLHL23-CUL3-CDC42 complex\", \"Substrate range beyond CDC42 unmapped\", \"Regulation of KLHL23 abundance and recruitment unknown\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0140096\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0016874\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005856\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-392499\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-162582\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\"CUL3-RING E3 ubiquitin ligase\"],\n    \"partners\": [\"CUL3\", \"CDC42\", \"ACTB\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"faith_supported":3,"faith_total":3,"faith_pct":100.0}}