{"gene":"CEP43","run_date":"2026-06-09T22:57:18","timeline":{"discoveries":[{"year":2006,"finding":"Crystal structure of the N-terminal domain of FOP/FGFR1OP was solved at 1.6 Å resolution, revealing an alpha-helical bundle of two antiparallel chains each with five alpha-helices. The LisH domain is embedded within this N-terminal segment, which was shown to be required (but not sufficient) for dimerization and centrosomal localization of FOP.","method":"X-ray crystallography at 1.6 Å resolution; functional validation by localization assays of truncation mutants","journal":"Journal of molecular biology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure with functional mutagenesis/truncation validation in a single rigorous study","pmids":["16690081"],"is_preprint":false},{"year":2017,"finding":"CEP19 is recruited to the mother centriole/ciliary base via its binding to the centrosomal protein FGFR1OP (FOP). CEP19 in turn captures GTP-bound RABL2B to initiate intraflagellar transport (IFT) complex entry into the cilium.","method":"Affinity-purification mass spectrometry; genetic disruption; localization assays","journal":"Developmental cell","confidence":"High","confidence_rationale":"Tier 2 / Strong — AP-MS identification replicated across two independent labs (PMID 28625565 and PMID 28428259) with consistent localization and functional data","pmids":["28625565","28428259"],"is_preprint":false},{"year":2017,"finding":"FGFR1OP (FOP) acts upstream of CEP19 in the centrosomal hierarchy: RABL2 is recruited to the mother centriole/basal body in a CEP19-dependent manner, and CEP19 is itself recruited via its binding to FGFR1OP. RABL2, in its GTP-bound state, interacts with the IFT-B complex via the IFT74-IFT81 heterodimer.","method":"Co-immunoprecipitation; live-cell and immunofluorescence localization; gene disruption in Chlamydomonas; dominant-negative mutant expression in human cells","journal":"Molecular biology of the cell","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP and localization data in single lab, consistent with independent parallel study","pmids":["28428259"],"is_preprint":false},{"year":2018,"finding":"Mouse Fop (FGFR1OP ortholog) mutation perturbs ciliogenesis in vivo, alters centriolar satellite (CS) movements and pericentriolar material composition, and disrupts Hedgehog signaling, leading to a short rib-polydactyly ciliopathy phenotype that recapitulates a human skeletal dysplasia syndrome.","method":"Mouse knockout/mutation model; in vivo ciliogenesis assay; Hedgehog pathway readout; immunofluorescence of centriolar satellites","journal":"Human molecular genetics","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — defined loss-of-function mouse model with multiple cellular and pathway readouts in a single study","pmids":["29982567"],"is_preprint":false},{"year":2024,"finding":"FGFR1OP deletion in mouse intestinal epithelial cells disrupted crypt architecture (crypt loss, inflammation, lethality) and impaired epithelial resilience during colitis. Mechanistically, FGFR1OP was shown to be required for non-muscle myosin II activity, thereby maintaining actomyosin cytoskeleton integrity and crypt cell adhesion.","method":"Conditional knockout in mouse intestinal epithelium; colitis challenge model; myosin II activity assay; immunofluorescence/cytoskeletal analysis","journal":"Developmental cell","confidence":"High","confidence_rationale":"Tier 2 / Moderate — conditional KO with defined cellular phenotype and direct myosin II activity measurement, multiple orthogonal readouts in a single study","pmids":["38942017"],"is_preprint":false},{"year":2013,"finding":"The FGFR1OP-RET fusion protein (generated by chromosomal translocation) displays constitutive tyrosine kinase activity, transforms NIH3T3 fibroblasts, induces IL3-independent growth and activates PI3K/STAT signaling in hematopoietic Ba/F3 cells, and causes myeloproliferative disorder in vivo in mice.","method":"Molecular cloning; in vitro transformation assay (NIH3T3); cytokine-independence assay (Ba/F3); signaling pathway analysis; murine bone marrow transplantation","journal":"Molecular oncology","confidence":"Medium","confidence_rationale":"Tier 1–2 / Moderate — functional reconstitution with in vitro kinase/transformation and in vivo models, single lab","pmids":["24315414"],"is_preprint":false},{"year":2025,"finding":"Network-based prioritization of candidate ciliopathy genes identified likely pathogenic variants in CEP43/FGFR1OP in three previously unsolved primary ciliopathy cases, suggesting CEP43 as a novel ciliopathy gene.","method":"Protein interaction network propagation; human genetics (variant identification in unsolved cases)","journal":"Genome biology","confidence":"Low","confidence_rationale":"Tier 4 / Weak — computational network prioritization with variant identification; no direct functional experiment performed on the protein in this study","pmids":["41715205"],"is_preprint":false}],"current_model":"CEP43/FGFR1OP encodes a centrosomal protein whose N-terminal LisH-containing domain mediates dimerization and centrosomal targeting; it anchors CEP19 at the centriolar base to enable RABL2-GTP capture and initiation of intraflagellar transport into primary cilia, regulates centriolar satellite dynamics and Hedgehog signaling required for skeletal development, and in intestinal epithelial cells sustains non-muscle myosin II activity to maintain actomyosin cytoskeleton integrity and epithelial renewal."},"narrative":{"mechanistic_narrative":"CEP43 (FGFR1OP/FOP) is a centrosomal protein that anchors a recruitment hierarchy at the mother centriole governing intraflagellar transport and ciliogenesis [PMID:28625565, PMID:28428259]. Its N-terminal segment, which embeds a LisH domain and folds into an antiparallel five-helix bundle, mediates dimerization and centrosomal targeting [PMID:16690081]. At the ciliary base CEP43 recruits CEP19, which in turn captures GTP-bound RABL2; RABL2-GTP engages the IFT-B complex through the IFT74-IFT81 heterodimer to initiate transport into the cilium [PMID:28625565, PMID:28428259]. Loss of function in mouse perturbs ciliogenesis, alters centriolar satellite movements and pericentriolar material composition, and disrupts Hedgehog signaling, producing a short rib-polydactyly ciliopathy phenotype that models a human skeletal dysplasia [PMID:29982567]. Beyond its centrosomal role, CEP43 is required in intestinal epithelial cells for non-muscle myosin II activity, maintaining actomyosin cytoskeleton integrity, crypt cell adhesion, and epithelial resilience [PMID:38942017]. A FGFR1OP-RET translocation fusion confers constitutive tyrosine kinase activity that transforms cells and drives myeloproliferative disease, a property of the chimeric kinase rather than wild-type CEP43 [PMID:24315414].","teleology":[{"year":2006,"claim":"Establishing the structural basis for CEP43 self-association answered how the protein achieves centrosomal targeting at the molecular level.","evidence":"X-ray crystallography of the N-terminal domain at 1.6 Å with truncation-mutant localization assays","pmids":["16690081"],"confidence":"High","gaps":["N-terminal domain is necessary but not sufficient for localization, leaving additional targeting determinants undefined","no structure of the full-length protein or of any partner complex"]},{"year":2017,"claim":"Identifying CEP43 as the centriolar anchor for CEP19 placed it at the top of a recruitment hierarchy that initiates IFT entry into cilia.","evidence":"AP-MS, reciprocal Co-IP, gene disruption, and localization assays across two independent labs, including Chlamydomonas and human cell systems","pmids":["28625565","28428259"],"confidence":"High","gaps":["binding interface between CEP43 and CEP19 not structurally mapped","regulation/timing of the CEP43–CEP19–RABL2 recruitment cascade unresolved"]},{"year":2018,"claim":"An in vivo loss-of-function model linked CEP43 to ciliogenesis, centriolar satellite dynamics, and Hedgehog-dependent skeletal development.","evidence":"Mouse Fop mutant with ciliogenesis, Hedgehog readouts, and centriolar satellite immunofluorescence","pmids":["29982567"],"confidence":"Medium","gaps":["mechanistic link between CEP43 and centriolar satellite movement not defined","whether the skeletal phenotype is solely IFT-dependent is unresolved"]},{"year":2024,"claim":"A tissue-specific knockout revealed a cilium-independent role for CEP43 in sustaining actomyosin integrity through non-muscle myosin II.","evidence":"Conditional knockout in mouse intestinal epithelium with colitis challenge and direct myosin II activity measurement","pmids":["38942017"],"confidence":"High","gaps":["molecular link between CEP43 and myosin II activation not defined","relationship of this role to the centrosomal function unknown"]},{"year":2013,"claim":"Characterization of the FGFR1OP-RET fusion showed how CEP43 sequences contribute to oncogenic kinase activation when fused to RET.","evidence":"Cloning, NIH3T3 transformation, Ba/F3 cytokine-independence, signaling analysis, and murine bone marrow transplantation","pmids":["24315414"],"confidence":"Medium","gaps":["contribution of CEP43 dimerization domain to fusion kinase activation not isolated","phenotype reflects the chimera, not endogenous CEP43"]},{"year":2025,"claim":"Network prioritization nominated CEP43 as a candidate human ciliopathy gene, extending its developmental relevance to patients.","evidence":"Protein interaction network propagation plus variant identification in unsolved ciliopathy cases","pmids":["41715205"],"confidence":"Low","gaps":["computational prioritization with no functional validation of the variants","causality in patients not established"]},{"year":null,"claim":"How CEP43 mechanistically couples its centrosomal/ciliary anchoring role to non-muscle myosin II regulation in epithelial cells remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["no molecular bridge between CEP43 and myosin II identified","no structural model of CEP43 partner complexes","tissue-specificity of its two functional roles unexplained"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[1,2]}],"localization":[{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[0,1,2]},{"term_id":"GO:0005929","term_label":"cilium","supporting_discovery_ids":[1,2,3]}],"pathway":[{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[1,2,3]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[3]}],"complexes":[],"partners":["CEP19","RABL2","RET"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"O95684","full_name":"Centrosomal protein 43","aliases":["FGFR1 oncogene partner"],"length_aa":399,"mass_kda":43.1,"function":"Required for anchoring microtubules to the centrosomes (PubMed:16314388, PubMed:28659385). Required for ciliation (PubMed:28625565, PubMed:28659385)","subcellular_location":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome; Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole; Cytoplasm, cytoskeleton, cilium basal body","url":"https://www.uniprot.org/uniprotkb/O95684/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CEP43","classification":"Not Classified","n_dependent_lines":452,"n_total_lines":1208,"dependency_fraction":0.3741721854304636},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[{"gene":"CEP350","stoichiometry":0.2},{"gene":"CEP78","stoichiometry":0.2},{"gene":"DDB1","stoichiometry":0.2},{"gene":"PPP2CA","stoichiometry":0.2},{"gene":"PPP2CB","stoichiometry":0.2}],"url":"https://opencell.sf.czbiohub.org/search/CEP43","total_profiled":1310},"omim":[{"mim_id":"609062","title":"POU DOMAIN, CLASS 6, TRANSCRIPTION FACTOR 2; POU6F2","url":"https://www.omim.org/entry/609062"},{"mim_id":"601583","title":"WILMS TUMOR 5; WT5","url":"https://www.omim.org/entry/601583"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Supported","locations":[{"location":"Centrosome","reliability":"Supported"},{"location":"Basal body","reliability":"Supported"},{"location":"Centriolar satellite","reliability":"Additional"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in all","driving_tissues":[{"tissue":"testis","ntpm":43.6}],"url":"https://www.proteinatlas.org/search/CEP43"},"hgnc":{"alias_symbol":["FOP"],"prev_symbol":["FGFR1OP"]},"alphafold":{"accession":"O95684","domains":[{"cath_id":"-","chopping":"2-56","consensus_level":"medium","plddt":83.7785,"start":2,"end":56},{"cath_id":"1.20.960.40","chopping":"59-139","consensus_level":"medium","plddt":88.128,"start":59,"end":139}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/O95684","model_url":"https://alphafold.ebi.ac.uk/files/AF-O95684-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-O95684-F1-predicted_aligned_error_v6.png","plddt_mean":62.97},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CEP43","jax_strain_url":"https://www.jax.org/strain/search?query=CEP43"},"sequence":{"accession":"O95684","fasta_url":"https://rest.uniprot.org/uniprotkb/O95684.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/O95684/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/O95684"}},"corpus_meta":[{"pmid":"27245147","id":"PMC_27245147","title":"FGFR 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The LisH domain is embedded within this N-terminal segment, which was shown to be required (but not sufficient) for dimerization and centrosomal localization of FOP.\",\n      \"method\": \"X-ray crystallography at 1.6 Å resolution; functional validation by localization assays of truncation mutants\",\n      \"journal\": \"Journal of molecular biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure with functional mutagenesis/truncation validation in a single rigorous study\",\n      \"pmids\": [\"16690081\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"CEP19 is recruited to the mother centriole/ciliary base via its binding to the centrosomal protein FGFR1OP (FOP). CEP19 in turn captures GTP-bound RABL2B to initiate intraflagellar transport (IFT) complex entry into the cilium.\",\n      \"method\": \"Affinity-purification mass spectrometry; genetic disruption; localization assays\",\n      \"journal\": \"Developmental cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — AP-MS identification replicated across two independent labs (PMID 28625565 and PMID 28428259) with consistent localization and functional data\",\n      \"pmids\": [\"28625565\", \"28428259\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2017,\n      \"finding\": \"FGFR1OP (FOP) acts upstream of CEP19 in the centrosomal hierarchy: RABL2 is recruited to the mother centriole/basal body in a CEP19-dependent manner, and CEP19 is itself recruited via its binding to FGFR1OP. RABL2, in its GTP-bound state, interacts with the IFT-B complex via the IFT74-IFT81 heterodimer.\",\n      \"method\": \"Co-immunoprecipitation; live-cell and immunofluorescence localization; gene disruption in Chlamydomonas; dominant-negative mutant expression in human cells\",\n      \"journal\": \"Molecular biology of the cell\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and localization data in single lab, consistent with independent parallel study\",\n      \"pmids\": [\"28428259\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Mouse Fop (FGFR1OP ortholog) mutation perturbs ciliogenesis in vivo, alters centriolar satellite (CS) movements and pericentriolar material composition, and disrupts Hedgehog signaling, leading to a short rib-polydactyly ciliopathy phenotype that recapitulates a human skeletal dysplasia syndrome.\",\n      \"method\": \"Mouse knockout/mutation model; in vivo ciliogenesis assay; Hedgehog pathway readout; immunofluorescence of centriolar satellites\",\n      \"journal\": \"Human molecular genetics\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — defined loss-of-function mouse model with multiple cellular and pathway readouts in a single study\",\n      \"pmids\": [\"29982567\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"FGFR1OP deletion in mouse intestinal epithelial cells disrupted crypt architecture (crypt loss, inflammation, lethality) and impaired epithelial resilience during colitis. Mechanistically, FGFR1OP was shown to be required for non-muscle myosin II activity, thereby maintaining actomyosin cytoskeleton integrity and crypt cell adhesion.\",\n      \"method\": \"Conditional knockout in mouse intestinal epithelium; colitis challenge model; myosin II activity assay; immunofluorescence/cytoskeletal analysis\",\n      \"journal\": \"Developmental cell\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — conditional KO with defined cellular phenotype and direct myosin II activity measurement, multiple orthogonal readouts in a single study\",\n      \"pmids\": [\"38942017\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"The FGFR1OP-RET fusion protein (generated by chromosomal translocation) displays constitutive tyrosine kinase activity, transforms NIH3T3 fibroblasts, induces IL3-independent growth and activates PI3K/STAT signaling in hematopoietic Ba/F3 cells, and causes myeloproliferative disorder in vivo in mice.\",\n      \"method\": \"Molecular cloning; in vitro transformation assay (NIH3T3); cytokine-independence assay (Ba/F3); signaling pathway analysis; murine bone marrow transplantation\",\n      \"journal\": \"Molecular oncology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1–2 / Moderate — functional reconstitution with in vitro kinase/transformation and in vivo models, single lab\",\n      \"pmids\": [\"24315414\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"Network-based prioritization of candidate ciliopathy genes identified likely pathogenic variants in CEP43/FGFR1OP in three previously unsolved primary ciliopathy cases, suggesting CEP43 as a novel ciliopathy gene.\",\n      \"method\": \"Protein interaction network propagation; human genetics (variant identification in unsolved cases)\",\n      \"journal\": \"Genome biology\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 4 / Weak — computational network prioritization with variant identification; no direct functional experiment performed on the protein in this study\",\n      \"pmids\": [\"41715205\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CEP43/FGFR1OP encodes a centrosomal protein whose N-terminal LisH-containing domain mediates dimerization and centrosomal targeting; it anchors CEP19 at the centriolar base to enable RABL2-GTP capture and initiation of intraflagellar transport into primary cilia, regulates centriolar satellite dynamics and Hedgehog signaling required for skeletal development, and in intestinal epithelial cells sustains non-muscle myosin II activity to maintain actomyosin cytoskeleton integrity and epithelial renewal.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"CEP43 (FGFR1OP/FOP) is a centrosomal protein that anchors a recruitment hierarchy at the mother centriole governing intraflagellar transport and ciliogenesis [#1, #2]. Its N-terminal segment, which embeds a LisH domain and folds into an antiparallel five-helix bundle, mediates dimerization and centrosomal targeting [#0]. At the ciliary base CEP43 recruits CEP19, which in turn captures GTP-bound RABL2; RABL2-GTP engages the IFT-B complex through the IFT74-IFT81 heterodimer to initiate transport into the cilium [#1, #2]. Loss of function in mouse perturbs ciliogenesis, alters centriolar satellite movements and pericentriolar material composition, and disrupts Hedgehog signaling, producing a short rib-polydactyly ciliopathy phenotype that models a human skeletal dysplasia [#3]. Beyond its centrosomal role, CEP43 is required in intestinal epithelial cells for non-muscle myosin II activity, maintaining actomyosin cytoskeleton integrity, crypt cell adhesion, and epithelial resilience [#4]. A FGFR1OP-RET translocation fusion confers constitutive tyrosine kinase activity that transforms cells and drives myeloproliferative disease, a property of the chimeric kinase rather than wild-type CEP43 [#5].\",\n  \"teleology\": [\n    {\n      \"year\": 2006,\n      \"claim\": \"Establishing the structural basis for CEP43 self-association answered how the protein achieves centrosomal targeting at the molecular level.\",\n      \"evidence\": \"X-ray crystallography of the N-terminal domain at 1.6 Å with truncation-mutant localization assays\",\n      \"pmids\": [\"16690081\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"N-terminal domain is necessary but not sufficient for localization, leaving additional targeting determinants undefined\", \"no structure of the full-length protein or of any partner complex\"]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Identifying CEP43 as the centriolar anchor for CEP19 placed it at the top of a recruitment hierarchy that initiates IFT entry into cilia.\",\n      \"evidence\": \"AP-MS, reciprocal Co-IP, gene disruption, and localization assays across two independent labs, including Chlamydomonas and human cell systems\",\n      \"pmids\": [\"28625565\", \"28428259\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"binding interface between CEP43 and CEP19 not structurally mapped\", \"regulation/timing of the CEP43–CEP19–RABL2 recruitment cascade unresolved\"]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"An in vivo loss-of-function model linked CEP43 to ciliogenesis, centriolar satellite dynamics, and Hedgehog-dependent skeletal development.\",\n      \"evidence\": \"Mouse Fop mutant with ciliogenesis, Hedgehog readouts, and centriolar satellite immunofluorescence\",\n      \"pmids\": [\"29982567\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"mechanistic link between CEP43 and centriolar satellite movement not defined\", \"whether the skeletal phenotype is solely IFT-dependent is unresolved\"]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"A tissue-specific knockout revealed a cilium-independent role for CEP43 in sustaining actomyosin integrity through non-muscle myosin II.\",\n      \"evidence\": \"Conditional knockout in mouse intestinal epithelium with colitis challenge and direct myosin II activity measurement\",\n      \"pmids\": [\"38942017\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"molecular link between CEP43 and myosin II activation not defined\", \"relationship of this role to the centrosomal function unknown\"]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"Characterization of the FGFR1OP-RET fusion showed how CEP43 sequences contribute to oncogenic kinase activation when fused to RET.\",\n      \"evidence\": \"Cloning, NIH3T3 transformation, Ba/F3 cytokine-independence, signaling analysis, and murine bone marrow transplantation\",\n      \"pmids\": [\"24315414\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"contribution of CEP43 dimerization domain to fusion kinase activation not isolated\", \"phenotype reflects the chimera, not endogenous CEP43\"]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Network prioritization nominated CEP43 as a candidate human ciliopathy gene, extending its developmental relevance to patients.\",\n      \"evidence\": \"Protein interaction network propagation plus variant identification in unsolved ciliopathy cases\",\n      \"pmids\": [\"41715205\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"computational prioritization with no functional validation of the variants\", \"causality in patients not established\"]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How CEP43 mechanistically couples its centrosomal/ciliary anchoring role to non-muscle myosin II regulation in epithelial cells remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"no molecular bridge between CEP43 and myosin II identified\", \"no structural model of CEP43 partner complexes\", \"tissue-specificity of its two functional roles unexplained\"]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [1, 2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0005929\", \"supporting_discovery_ids\": [1, 2, 3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [1, 2, 3]},\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\"CEP19\", \"RABL2\", \"RET\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":6,"faith_total":6,"faith_pct":100.0}}