{"gene":"CCDC120","run_date":"2026-06-09T22:57:17","timeline":{"discoveries":[{"year":2017,"finding":"CCDC120 is a novel subdistal appendage (SDA) component of the centriole. It is anchored to SDAs by ODF2 and recruits CEP170 and Ninein to the centrosome through different coiled-coil domains at its N terminus. CCDC68 is a CEP170-interacting protein that competes with CCDC120 in recruiting CEP170 to SDAs. Both CCDC120 and CCDC68 are required for centrosome microtubule anchoring in human interphase cells.","method":"siRNA knockdown, co-immunoprecipitation, immunofluorescence microscopy, domain mapping with deletion constructs in human cells","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — reciprocal Co-IP, domain-mapping mutagenesis, and clean KD with defined cellular phenotype (microtubule anchoring defect); multiple orthogonal methods in a single focused study","pmids":["28422092"],"is_preprint":false},{"year":2014,"finding":"CCDC120 binds to cytohesin-2 (a guanine nucleotide exchange factor for Arf6) via its CC1 coiled-coil domain. CCDC120 determines cytohesin-2 localization into vesicles in growing neurites; CCDC120 knockdown disperses cytohesin-2 into the cytoplasm, inhibits neurite growth, and reduces Arf6 activation. Re-introduction of wild-type CCDC120 rescues these defects, but a CC1-region-deficient CCDC120 construct does not, establishing the CC1 domain as necessary for cytohesin-2 interaction and neurite growth.","method":"Co-immunoprecipitation, siRNA knockdown, domain-deletion rescue experiments, live-cell vesicle transport imaging, Arf6 activation assay (GGA pulldown) in N1E-115 neuronal cells","journal":"The Journal of biological chemistry","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP, domain-deletion rescue, and functional assay (Arf6 activation, neurite growth) in single lab with multiple orthogonal methods","pmids":["25326380"],"is_preprint":false},{"year":2026,"finding":"CCDC120 localizes to desmosomes and is required for desmosomal integrity. CCDC120 undergoes liquid-liquid phase separation (LLPS) and co-condenses with the desmosomal component plakophilin-2 (PKP2) during desmosomal assembly, forming dynamic condensates that preserve desmosomal structure and junction stability. CCDC120 condensate behavior is modulated by PKCα-mediated phosphorylation. Loss of CCDC120 or altered CCDC120 phase-separation properties impairs intercalated disc structure and causes cardiac dysfunction in mice.","method":"Live-cell imaging of LLPS condensates, co-condensation assays with PKP2, PKCα phosphorylation assays, CCDC120 knockout mice with cardiac phenotype readout, immunofluorescence of intercalated disc structure","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal methods (LLPS reconstitution, co-condensation, phosphorylation assay, in vivo KO with cardiac phenotype) in a single focused study","pmids":["42098154"],"is_preprint":false},{"year":2026,"finding":"C-terminal truncations of CEP170 impair its centrosomal and microtubule localization via disrupted interactions with CCDC120, establishing CCDC120 as a centrosomal targeting mediator for CEP170.","method":"Co-immunoprecipitation, subcellular localization studies with CEP170 truncation constructs, microtubule regrowth assays in CRISPR/Cas9 CEP170-KO cells","journal":"Journal of biomedical science","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — Co-IP and localization with domain truncations in a single lab; CCDC120 interaction is a secondary finding within a CEP170-focused study","pmids":["41888776"],"is_preprint":false}],"current_model":"CCDC120 is a multi-compartment scaffold protein: at the centriole subdistal appendages it is anchored by ODF2 and hierarchically recruits CEP170 and Ninein (via distinct N-terminal coiled-coil domains) to mediate microtubule anchoring; in neurons its CC1 domain binds cytohesin-2 and directs anterograde vesicular transport of this Arf6-GEF to mediate neurite growth; and at cardiac desmosomes it undergoes PKCα-regulated liquid-liquid phase separation, co-condensing with plakophilin-2 to maintain desmosomal integrity and cardiac function."},"narrative":{"mechanistic_narrative":"CCDC120 is a multi-compartment coiled-coil scaffold protein that organizes microtubule-anchoring and junctional machinery across distinct cellular contexts [PMID:28422092, PMID:25326380, PMID:42098154]. At the centriole subdistal appendages it is anchored by ODF2 and uses distinct N-terminal coiled-coil domains to hierarchically recruit CEP170 and Ninein, an activity required for centrosomal microtubule anchoring in interphase cells; its recruitment of CEP170 is antagonized by CCDC68, which competes for the same interaction [PMID:28422092]. CCDC120 serves as the centrosomal targeting mediator for CEP170, whose C-terminal truncations lose centrosomal and microtubule localization when the CCDC120 interaction is disrupted [PMID:41888776]. In neurons, the CC1 coiled-coil domain binds cytohesin-2, an Arf6 guanine-nucleotide exchange factor, and directs its anterograde vesicular transport into growing neurites; loss of CCDC120 disperses cytohesin-2, reduces Arf6 activation, and inhibits neurite growth [PMID:25326380]. At cardiac desmosomes CCDC120 undergoes liquid-liquid phase separation and co-condenses with plakophilin-2 to preserve desmosomal and intercalated disc integrity, a behavior tuned by PKCα-mediated phosphorylation; its loss causes cardiac dysfunction in mice [PMID:42098154].","teleology":[{"year":2014,"claim":"Established the first molecular function for CCDC120 by showing its CC1 domain couples the Arf6-GEF cytohesin-2 to vesicular transport driving neurite outgrowth, defining it as a transport scaffold rather than an inert structural protein.","evidence":"Co-IP, domain-deletion rescue, live-cell vesicle imaging, and Arf6 GGA-pulldown activation assay in N1E-115 neuronal cells","pmids":["25326380"],"confidence":"High","gaps":["Structural basis of the CC1-cytohesin-2 interaction unresolved","Whether the same domain mediates the centriolar functions later described was not tested","Identity of the motor/vesicle machinery transporting the complex not defined"]},{"year":2017,"claim":"Defined CCDC120 as a subdistal appendage component that uses ODF2 for anchoring and separate N-terminal coiled-coil domains to recruit CEP170 and Ninein, placing it within a hierarchical microtubule-anchoring module subject to CCDC68 competition.","evidence":"siRNA knockdown, reciprocal co-IP, domain-mapping deletion constructs, and immunofluorescence in human cells","pmids":["28422092"],"confidence":"High","gaps":["Structural architecture of the SDA scaffold not resolved","Regulation of the CCDC120/CCDC68 competition not defined","Relationship between centriolar and neuronal functions unaddressed"]},{"year":2026,"claim":"Extended CCDC120 into a third compartment, showing it phase-separates and co-condenses with plakophilin-2 under PKCα control to maintain desmosomal/intercalated-disc integrity, with knockout causing cardiac dysfunction in vivo.","evidence":"Live-cell LLPS imaging, PKP2 co-condensation assays, PKCα phosphorylation assays, and CCDC120 knockout mice with cardiac phenotyping","pmids":["42098154"],"confidence":"High","gaps":["Phosphosites controlling condensate behavior not mapped","Whether desmosomal LLPS and centriolar scaffolding share determinants is unknown","Composition of the condensates beyond PKP2 not defined"]},{"year":2026,"claim":"Reinforced CCDC120 as the centrosomal targeting mediator for CEP170 by showing CEP170 C-terminal truncations lose centrosomal/microtubule localization through disrupted CCDC120 binding.","evidence":"Co-IP, localization with CEP170 truncation constructs, and microtubule regrowth assays in CRISPR CEP170-KO cells","pmids":["41888776"],"confidence":"Medium","gaps":["CCDC120 interaction is a secondary finding within a CEP170-focused study","Binding interface on CCDC120 not mapped","Functional consequence for CCDC120 itself not directly tested"]},{"year":null,"claim":"How a single coiled-coil scaffold is partitioned among centrioles, neuronal vesicles, and cardiac desmosomes, and what regulates this compartment switching, remains unresolved.","evidence":"No integrative study addresses cross-compartment regulation in the available corpus","pmids":[],"confidence":"Low","gaps":["No structural model of CCDC120","No mechanism linking its distinct localizations","Tissue-specific expression and isoform usage not characterized"]}],"mechanism_profile":{"molecular_activity":[{"term_id":"GO:0060090","term_label":"molecular adaptor activity","supporting_discovery_ids":[0,1,2]},{"term_id":"GO:0008092","term_label":"cytoskeletal protein binding","supporting_discovery_ids":[0]}],"localization":[{"term_id":"GO:0005815","term_label":"microtubule organizing center","supporting_discovery_ids":[0,3]},{"term_id":"GO:0031410","term_label":"cytoplasmic vesicle","supporting_discovery_ids":[1]},{"term_id":"GO:0005886","term_label":"plasma membrane","supporting_discovery_ids":[2]}],"pathway":[{"term_id":"R-HSA-1852241","term_label":"Organelle biogenesis and maintenance","supporting_discovery_ids":[0]},{"term_id":"R-HSA-1266738","term_label":"Developmental Biology","supporting_discovery_ids":[1]}],"complexes":["centriole subdistal appendage","desmosome"],"partners":["ODF2","CEP170","NINEIN","CCDC68","CYTOHESIN-2","PKP2","PKCALPHA"],"other_free_text":[]}},"prefetch_data":{"uniprot":{"accession":"Q96HB5","full_name":"Coiled-coil domain-containing protein 120","aliases":[],"length_aa":630,"mass_kda":67.6,"function":"Centriolar protein required for centriole subdistal appendage assembly and microtubule anchoring in interphase cells (PubMed:28422092). Together with CCDC68, cooperate with subdistal appendage components ODF2, NIN and CEP170 for hierarchical subdistal appendage assembly (PubMed:28422092). Recruits NIN and CEP170 to centrosomes (PubMed:28422092). Also required for neurite growth. Localizes CYTH2 to vesicles to allow its transport along neurites, and subsequent ARF6 activation and neurite growth","subcellular_location":"Cytoplasm, cytoskeleton, microtubule organizing center, centrosome, centriole; Cytoplasm; Cell projection, neuron projection; Cell projection, growth cone; Endosome","url":"https://www.uniprot.org/uniprotkb/Q96HB5/entry"},"depmap":{"release":"DepMap","has_data":true,"is_common_essential":false,"resolved_as":"","url":"https://depmap.org/portal/gene/CCDC120","classification":"Not Classified","n_dependent_lines":1,"n_total_lines":1208,"dependency_fraction":0.0008278145695364238},"opencell":{"profiled":false,"resolved_as":"","ensg_id":"","cell_line_id":"","localizations":[],"interactors":[],"url":"https://opencell.sf.czbiohub.org/search/CCDC120","total_profiled":1310},"omim":[{"mim_id":"602488","title":"CYTOHESIN 2; CYTH2","url":"https://www.omim.org/entry/602488"},{"mim_id":"600464","title":"ADP-RIBOSYLATION FACTOR 6; ARF6","url":"https://www.omim.org/entry/600464"},{"mim_id":"300947","title":"COILED-COIL DOMAIN-CONTAINING PROTEIN 120; CCDC120","url":"https://www.omim.org/entry/300947"}],"hpa":{"profiled":true,"resolved_as":"","reliability":"Uncertain","locations":[{"location":"Mitochondria","reliability":"Uncertain"}],"tissue_specificity":"Tissue enhanced","tissue_distribution":"Detected in many","driving_tissues":[{"tissue":"esophagus","ntpm":34.6},{"tissue":"skin 1","ntpm":28.0}],"url":"https://www.proteinatlas.org/search/CCDC120"},"hgnc":{"alias_symbol":["JM11"],"prev_symbol":[]},"alphafold":{"accession":"Q96HB5","domains":[{"cath_id":"1.10.287","chopping":"107-172","consensus_level":"medium","plddt":94.2188,"start":107,"end":172}],"viewer_url":"https://alphafold.ebi.ac.uk/entry/Q96HB5","model_url":"https://alphafold.ebi.ac.uk/files/AF-Q96HB5-F1-model_v6.cif","pae_url":"https://alphafold.ebi.ac.uk/files/AF-Q96HB5-F1-predicted_aligned_error_v6.png","plddt_mean":55.5},"mouse_models":{"mgi_url":"https://www.informatics.jax.org/marker/summary?nomen=CCDC120","jax_strain_url":"https://www.jax.org/strain/search?query=CCDC120"},"sequence":{"accession":"Q96HB5","fasta_url":"https://rest.uniprot.org/uniprotkb/Q96HB5.fasta","uniprot_url":"https://www.uniprot.org/uniprotkb/Q96HB5/entry","alphafold_viewer_url":"https://alphafold.ebi.ac.uk/entry/Q96HB5"}},"corpus_meta":[{"pmid":"28422092","id":"PMC_28422092","title":"Hierarchical assembly of centriole subdistal appendages via centrosome binding proteins CCDC120 and CCDC68.","date":"2017","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/28422092","citation_count":67,"is_preprint":false},{"pmid":"25326380","id":"PMC_25326380","title":"Arf6 guanine nucleotide exchange factor cytohesin-2 binds to CCDC120 and is transported along neurites to mediate neurite growth.","date":"2014","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/25326380","citation_count":16,"is_preprint":false},{"pmid":"24781706","id":"PMC_24781706","title":"Molecular mapping and validation of a major QTL conferring resistance to a defoliating isolate of verticillium wilt in cotton (Gossypium hirsutum L.).","date":"2014","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/24781706","citation_count":16,"is_preprint":false},{"pmid":"22814699","id":"PMC_22814699","title":"Biology of fowl adenovirus type 1 infection of heterologous cells.","date":"2012","source":"Archives of virology","url":"https://pubmed.ncbi.nlm.nih.gov/22814699","citation_count":5,"is_preprint":false},{"pmid":"37704070","id":"PMC_37704070","title":"The molecular spectrum of Turkish osteopetrosis and related osteoclast disorders with natural history, including a candidate gene, CCDC120.","date":"2023","source":"Bone","url":"https://pubmed.ncbi.nlm.nih.gov/37704070","citation_count":4,"is_preprint":false},{"pmid":"40035858","id":"PMC_40035858","title":"Bacillus velezensis JM11 and Bacillus pumilus CPCF54 ameliorate Cadmium-Induced Oxidative Stress in Gladiolus grandiflorus Cut Flower.","date":"2025","source":"Current microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/40035858","citation_count":3,"is_preprint":false},{"pmid":"42098154","id":"PMC_42098154","title":"CCDC120 phase separation contributes to desmosomal integrity and cardiac function.","date":"2026","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/42098154","citation_count":0,"is_preprint":false},{"pmid":"41666234","id":"PMC_41666234","title":"Resistant cotton maintains vascular health via an integrative defense network against Verticillium dahliae.","date":"2026","source":"Annals of botany","url":"https://pubmed.ncbi.nlm.nih.gov/41666234","citation_count":0,"is_preprint":false},{"pmid":"41888776","id":"PMC_41888776","title":"CEP170 as a novel molecular link between centrosomal function and cerebral cortical development.","date":"2026","source":"Journal of biomedical science","url":"https://pubmed.ncbi.nlm.nih.gov/41888776","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6823,"output_tokens":1355,"usd":0.020397,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7995,"output_tokens":2247,"usd":0.048075,"stage2_stop_reason":"end_turn"},"total_usd":0.068472,"stage1_batch_id":"msgbatch_01ACAxJQabDsht39JXeWG22d","stage2_batch_id":"msgbatch_01QEU22A9U5sbPTgsMzTmvSf","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2017,\n      \"finding\": \"CCDC120 is a novel subdistal appendage (SDA) component of the centriole. It is anchored to SDAs by ODF2 and recruits CEP170 and Ninein to the centrosome through different coiled-coil domains at its N terminus. CCDC68 is a CEP170-interacting protein that competes with CCDC120 in recruiting CEP170 to SDAs. Both CCDC120 and CCDC68 are required for centrosome microtubule anchoring in human interphase cells.\",\n      \"method\": \"siRNA knockdown, co-immunoprecipitation, immunofluorescence microscopy, domain mapping with deletion constructs in human cells\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — reciprocal Co-IP, domain-mapping mutagenesis, and clean KD with defined cellular phenotype (microtubule anchoring defect); multiple orthogonal methods in a single focused study\",\n      \"pmids\": [\"28422092\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"CCDC120 binds to cytohesin-2 (a guanine nucleotide exchange factor for Arf6) via its CC1 coiled-coil domain. CCDC120 determines cytohesin-2 localization into vesicles in growing neurites; CCDC120 knockdown disperses cytohesin-2 into the cytoplasm, inhibits neurite growth, and reduces Arf6 activation. Re-introduction of wild-type CCDC120 rescues these defects, but a CC1-region-deficient CCDC120 construct does not, establishing the CC1 domain as necessary for cytohesin-2 interaction and neurite growth.\",\n      \"method\": \"Co-immunoprecipitation, siRNA knockdown, domain-deletion rescue experiments, live-cell vesicle transport imaging, Arf6 activation assay (GGA pulldown) in N1E-115 neuronal cells\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP, domain-deletion rescue, and functional assay (Arf6 activation, neurite growth) in single lab with multiple orthogonal methods\",\n      \"pmids\": [\"25326380\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"CCDC120 localizes to desmosomes and is required for desmosomal integrity. CCDC120 undergoes liquid-liquid phase separation (LLPS) and co-condenses with the desmosomal component plakophilin-2 (PKP2) during desmosomal assembly, forming dynamic condensates that preserve desmosomal structure and junction stability. CCDC120 condensate behavior is modulated by PKCα-mediated phosphorylation. Loss of CCDC120 or altered CCDC120 phase-separation properties impairs intercalated disc structure and causes cardiac dysfunction in mice.\",\n      \"method\": \"Live-cell imaging of LLPS condensates, co-condensation assays with PKP2, PKCα phosphorylation assays, CCDC120 knockout mice with cardiac phenotype readout, immunofluorescence of intercalated disc structure\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal methods (LLPS reconstitution, co-condensation, phosphorylation assay, in vivo KO with cardiac phenotype) in a single focused study\",\n      \"pmids\": [\"42098154\"],\n      \"is_preprint\": false\n    },\n    {\n      \"year\": 2026,\n      \"finding\": \"C-terminal truncations of CEP170 impair its centrosomal and microtubule localization via disrupted interactions with CCDC120, establishing CCDC120 as a centrosomal targeting mediator for CEP170.\",\n      \"method\": \"Co-immunoprecipitation, subcellular localization studies with CEP170 truncation constructs, microtubule regrowth assays in CRISPR/Cas9 CEP170-KO cells\",\n      \"journal\": \"Journal of biomedical science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — Co-IP and localization with domain truncations in a single lab; CCDC120 interaction is a secondary finding within a CEP170-focused study\",\n      \"pmids\": [\"41888776\"],\n      \"is_preprint\": false\n    }\n  ],\n  \"current_model\": \"CCDC120 is a multi-compartment scaffold protein: at the centriole subdistal appendages it is anchored by ODF2 and hierarchically recruits CEP170 and Ninein (via distinct N-terminal coiled-coil domains) to mediate microtubule anchoring; in neurons its CC1 domain binds cytohesin-2 and directs anterograde vesicular transport of this Arf6-GEF to mediate neurite growth; and at cardiac desmosomes it undergoes PKCα-regulated liquid-liquid phase separation, co-condensing with plakophilin-2 to maintain desmosomal integrity and cardiac function.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"CCDC120 is a multi-compartment coiled-coil scaffold protein that organizes microtubule-anchoring and junctional machinery across distinct cellular contexts [#0, #1, #2]. At the centriole subdistal appendages it is anchored by ODF2 and uses distinct N-terminal coiled-coil domains to hierarchically recruit CEP170 and Ninein, an activity required for centrosomal microtubule anchoring in interphase cells; its recruitment of CEP170 is antagonized by CCDC68, which competes for the same interaction [#0]. CCDC120 serves as the centrosomal targeting mediator for CEP170, whose C-terminal truncations lose centrosomal and microtubule localization when the CCDC120 interaction is disrupted [#3]. In neurons, the CC1 coiled-coil domain binds cytohesin-2, an Arf6 guanine-nucleotide exchange factor, and directs its anterograde vesicular transport into growing neurites; loss of CCDC120 disperses cytohesin-2, reduces Arf6 activation, and inhibits neurite growth [#1]. At cardiac desmosomes CCDC120 undergoes liquid-liquid phase separation and co-condenses with plakophilin-2 to preserve desmosomal and intercalated disc integrity, a behavior tuned by PKCα-mediated phosphorylation; its loss causes cardiac dysfunction in mice [#2].\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Established the first molecular function for CCDC120 by showing its CC1 domain couples the Arf6-GEF cytohesin-2 to vesicular transport driving neurite outgrowth, defining it as a transport scaffold rather than an inert structural protein.\",\n      \"evidence\": \"Co-IP, domain-deletion rescue, live-cell vesicle imaging, and Arf6 GGA-pulldown activation assay in N1E-115 neuronal cells\",\n      \"pmids\": [\"25326380\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural basis of the CC1-cytohesin-2 interaction unresolved\",\n        \"Whether the same domain mediates the centriolar functions later described was not tested\",\n        \"Identity of the motor/vesicle machinery transporting the complex not defined\"\n      ]\n    },\n    {\n      \"year\": 2017,\n      \"claim\": \"Defined CCDC120 as a subdistal appendage component that uses ODF2 for anchoring and separate N-terminal coiled-coil domains to recruit CEP170 and Ninein, placing it within a hierarchical microtubule-anchoring module subject to CCDC68 competition.\",\n      \"evidence\": \"siRNA knockdown, reciprocal co-IP, domain-mapping deletion constructs, and immunofluorescence in human cells\",\n      \"pmids\": [\"28422092\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Structural architecture of the SDA scaffold not resolved\",\n        \"Regulation of the CCDC120/CCDC68 competition not defined\",\n        \"Relationship between centriolar and neuronal functions unaddressed\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Extended CCDC120 into a third compartment, showing it phase-separates and co-condenses with plakophilin-2 under PKCα control to maintain desmosomal/intercalated-disc integrity, with knockout causing cardiac dysfunction in vivo.\",\n      \"evidence\": \"Live-cell LLPS imaging, PKP2 co-condensation assays, PKCα phosphorylation assays, and CCDC120 knockout mice with cardiac phenotyping\",\n      \"pmids\": [\"42098154\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Phosphosites controlling condensate behavior not mapped\",\n        \"Whether desmosomal LLPS and centriolar scaffolding share determinants is unknown\",\n        \"Composition of the condensates beyond PKP2 not defined\"\n      ]\n    },\n    {\n      \"year\": 2026,\n      \"claim\": \"Reinforced CCDC120 as the centrosomal targeting mediator for CEP170 by showing CEP170 C-terminal truncations lose centrosomal/microtubule localization through disrupted CCDC120 binding.\",\n      \"evidence\": \"Co-IP, localization with CEP170 truncation constructs, and microtubule regrowth assays in CRISPR CEP170-KO cells\",\n      \"pmids\": [\"41888776\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"CCDC120 interaction is a secondary finding within a CEP170-focused study\",\n        \"Binding interface on CCDC120 not mapped\",\n        \"Functional consequence for CCDC120 itself not directly tested\"\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How a single coiled-coil scaffold is partitioned among centrioles, neuronal vesicles, and cardiac desmosomes, and what regulates this compartment switching, remains unresolved.\",\n      \"evidence\": \"No integrative study addresses cross-compartment regulation in the available corpus\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No structural model of CCDC120\",\n        \"No mechanism linking its distinct localizations\",\n        \"Tissue-specific expression and isoform usage not characterized\"\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0060090\", \"supporting_discovery_ids\": [0, 1, 2]},\n      {\"term_id\": \"GO:0008092\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005815\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0031410\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0005886\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"R-HSA-1852241\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"R-HSA-1266738\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"complexes\": [\"centriole subdistal appendage\", \"desmosome\"],\n    \"partners\": [\"ODF2\", \"CEP170\", \"Ninein\", \"CCDC68\", \"cytohesin-2\", \"PKP2\", \"PKCalpha\"],\n    \"other_free_text\": []\n  }\n}","audit_flag":null,"evaluation":{"pairwise":"win","faith_supported":5,"faith_total":5,"faith_pct":100.0}}