{"gene":"TG_246940","gene_symbol":"GAP80","run_date":"2026-09-08T12:58:25","timeline":{"discoveries":[{"year":2014,"finding":"GAP80 assembles a new glideosome that recruits the class XIV myosin C (MyoC) at the basal polar ring of Toxoplasma gondii, distinct from the MyoA-glideosome.","method":"Genetic deletion and localization studies (loss-of-function with phenotypic readout, subcellular localization)","journal":"PLoS pathogens","confidence":"High","confidence_rationale":"Tier 2 / Moderate — clean genetic deletions with defined phenotypic readouts combined with localization data, single lab but multiple orthogonal approaches","pmids":["25393004"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"MyoC (recruited by GAP80) shares the same myosin light chains as MyoA and interacts with the integral IMC proteins GAP50 and GAP40, demonstrating shared glideosome components between the MyoA- and MyoC-glideosomes.","method":"Co-immunoprecipitation / protein interaction studies","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — interaction data reported in single lab, multiple interactions identified but method details limited in abstract","pmids":["25393004"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"IAP1 (IMC-associated protein 1) acts as the key determinant for the restricted localization of MyoC to the posterior pole within the GAP80-assembled glideosome.","method":"Genetic deletion with localization analysis (loss-of-function, subcellular localization)","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Weak — genetic deletion with defined localization phenotype, single lab, single method described in abstract","pmids":["25393004"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"Deletion of specific components of the MyoC-glideosome (which includes GAP80) triggers compensatory relocalization of MyoC along the pellicle and apical cap upon MyoA removal, demonstrating plasticity between the two glideosomes that sustains residual invasion.","method":"Genetic deletion of MyoA with subsequent localization analysis and invasion assay","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic epistasis via sequential deletions with functional invasion readout and localization, single lab, multiple complementary approaches","pmids":["25393004"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"GAP80 is a member of the GAP45/GAP70 family that assembles a distinct basal-pole glideosome in Toxoplasma gondii by recruiting class XIV myosin C (MyoC) — together with shared light chains, GAP50, GAP40, and the localization determinant IAP1 — to the basal polar ring, and this MyoC-glideosome exhibits functional plasticity with the apical MyoA-glideosome to sustain parasite motility, invasion, and egress."},"narrative":{"mechanistic_narrative":"GAP80 is a glideosome-associated protein of Toxoplasma gondii that nucleates a distinct basal-pole motor complex, recruiting the class XIV myosin C (MyoC) to the basal polar ring in a spatial arrangement separate from the canonical apical MyoA-glideosome [PMID:25393004]. Within this complex, MyoC shares the same myosin light chains as MyoA and engages the integral IMC proteins GAP50 and GAP40, establishing that the two glideosomes are built from overlapping core components differing in their motor and positional determinants [PMID:25393004]. Restriction of MyoC to the posterior pole depends on the IMC-associated protein IAP1, which acts as the localization determinant for the GAP80-assembled complex [PMID:25393004]. The two glideosomes are functionally plastic: removal of MyoA triggers compensatory relocalization of MyoC along the pellicle and apical cap, sustaining residual host-cell invasion [PMID:25393004]. Beyond these findings, no further mechanistic detail on GAP80 has been characterized in the available corpus.","teleology":[{"year":2014,"claim":"Whether Toxoplasma possesses motor complexes beyond the apical MyoA-glideosome was unresolved; identifying GAP80 as the scaffold of a MyoC-recruiting basal complex established a second, spatially distinct glideosome.","evidence":"genetic deletion and subcellular localization in Toxoplasma gondii","pmids":["25393004"],"confidence":"High","gaps":["structural basis of how GAP80 tethers MyoC to the basal polar ring not defined","biochemical activity of GAP80 itself not characterized","quantitative contribution of the basal glideosome to motility not measured"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"It was unknown whether the two glideosomes were biochemically independent or shared parts; co-immunoprecipitation showed MyoC uses the same light chains as MyoA and binds GAP50 and GAP40, revealing a shared core architecture.","evidence":"co-immunoprecipitation / protein interaction studies in Toxoplasma gondii","pmids":["25393004"],"confidence":"Medium","gaps":["stoichiometry and direct versus indirect nature of interactions not resolved","no reciprocal validation of the shared light-chain interactions reported"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"What confines MyoC to the posterior pole was unclear; deletion analysis identified IAP1 as the determinant restricting MyoC localization within the GAP80 complex.","evidence":"genetic deletion with localization analysis in Toxoplasma gondii","pmids":["25393004"],"confidence":"Medium","gaps":["molecular mechanism by which IAP1 restricts localization not defined","relationship between IAP1 and GAP80 in complex assembly not established"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"Whether the basal glideosome could substitute for the apical motor was untested; sequential MyoA deletion showed MyoC relocalizes to the pellicle and apical cap and sustains residual invasion, demonstrating functional plasticity.","evidence":"genetic deletion of MyoA with localization and invasion assays in Toxoplasma gondii","pmids":["25393004"],"confidence":"Medium","gaps":["signal triggering compensatory relocalization unknown","efficiency of MyoC-driven invasion relative to MyoA not quantified in detail"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The intrinsic biochemical function of GAP80, its structure, and how it is targeted to the basal polar ring remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["no structural model of GAP80 or the basal glideosome","no defined enzymatic or binding activity for GAP80 itself","recruitment mechanism to the basal polar ring uncharacterized"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["MyoC-glideosome (basal-pole glideosome) comprising GAP80, MyoC, shared myosin light chains, GAP50, GAP40, and IAP1"],"partners":["MYOC (CLASS XIV MYOSIN C)","SHARED MYOSIN LIGHT CHAINS","GAP50","GAP40","IAP1"],"other_free_text":["GAP80 assembles a basal-pole glideosome distinct from the apical MyoA-glideosome [#0].","The MyoC- and MyoA-glideosomes exhibit functional plasticity, with MyoC relocalizing to compensate for MyoA loss and sustain residual invasion [#3]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"25393004","id":"PMC_25393004","title":"Plasticity between MyoC- and MyoA-glideosomes: an example of functional compensation in Toxoplasma gondii invasion.","date":"2014","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/25393004","citation_count":77,"is_preprint":false},{"pmid":"30130043","id":"PMC_30130043","title":"[Research Advances on Gliding-associated Proteins of Toxoplasma gondii].","date":"2016","source":"Zhongguo ji sheng chong xue yu ji sheng chong bing za zhi = Chinese journal of parasitology & parasitic diseases","url":"https://pubmed.ncbi.nlm.nih.gov/30130043","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3312,"output_tokens":983,"usd":0.012341,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5865,"output_tokens":2170,"usd":0.041787,"stage2_stop_reason":"end_turn"},"total_usd":0.054128,"stage1_batch_id":"msgbatch_01TEPNZ4MCzJ7xtsNwosiDRk","stage2_batch_id":"msgbatch_01FQShM7n1sfCr4pWTDShmki","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2014,\n      \"finding\": \"GAP80 assembles a new glideosome that recruits the class XIV myosin C (MyoC) at the basal polar ring of Toxoplasma gondii, distinct from the MyoA-glideosome.\",\n      \"method\": \"Genetic deletion and localization studies (loss-of-function with phenotypic readout, subcellular localization)\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean genetic deletions with defined phenotypic readouts combined with localization data, single lab but multiple orthogonal approaches\",\n      \"pmids\": [\"25393004\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"MyoC (recruited by GAP80) shares the same myosin light chains as MyoA and interacts with the integral IMC proteins GAP50 and GAP40, demonstrating shared glideosome components between the MyoA- and MyoC-glideosomes.\",\n      \"method\": \"Co-immunoprecipitation / protein interaction studies\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — interaction data reported in single lab, multiple interactions identified but method details limited in abstract\",\n      \"pmids\": [\"25393004\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"IAP1 (IMC-associated protein 1) acts as the key determinant for the restricted localization of MyoC to the posterior pole within the GAP80-assembled glideosome.\",\n      \"method\": \"Genetic deletion with localization analysis (loss-of-function, subcellular localization)\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Weak — genetic deletion with defined localization phenotype, single lab, single method described in abstract\",\n      \"pmids\": [\"25393004\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"Deletion of specific components of the MyoC-glideosome (which includes GAP80) triggers compensatory relocalization of MyoC along the pellicle and apical cap upon MyoA removal, demonstrating plasticity between the two glideosomes that sustains residual invasion.\",\n      \"method\": \"Genetic deletion of MyoA with subsequent localization analysis and invasion assay\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic epistasis via sequential deletions with functional invasion readout and localization, single lab, multiple complementary approaches\",\n      \"pmids\": [\"25393004\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"GAP80 is a member of the GAP45/GAP70 family that assembles a distinct basal-pole glideosome in Toxoplasma gondii by recruiting class XIV myosin C (MyoC) — together with shared light chains, GAP50, GAP40, and the localization determinant IAP1 — to the basal polar ring, and this MyoC-glideosome exhibits functional plasticity with the apical MyoA-glideosome to sustain parasite motility, invasion, and egress.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"GAP80 is a glideosome-associated protein of Toxoplasma gondii that nucleates a distinct basal-pole motor complex, recruiting the class XIV myosin C (MyoC) to the basal polar ring in a spatial arrangement separate from the canonical apical MyoA-glideosome [#0]. Within this complex, MyoC shares the same myosin light chains as MyoA and engages the integral IMC proteins GAP50 and GAP40, establishing that the two glideosomes are built from overlapping core components differing in their motor and positional determinants [#1]. Restriction of MyoC to the posterior pole depends on the IMC-associated protein IAP1, which acts as the localization determinant for the GAP80-assembled complex [#2]. The two glideosomes are functionally plastic: removal of MyoA triggers compensatory relocalization of MyoC along the pellicle and apical cap, sustaining residual host-cell invasion [#3]. Beyond these findings, no further mechanistic detail on GAP80 has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether Toxoplasma possesses motor complexes beyond the apical MyoA-glideosome was unresolved; identifying GAP80 as the scaffold of a MyoC-recruiting basal complex established a second, spatially distinct glideosome.\",\n      \"evidence\": \"genetic deletion and subcellular localization in Toxoplasma gondii\",\n      \"pmids\": [\"25393004\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"structural basis of how GAP80 tethers MyoC to the basal polar ring not defined\",\n        \"biochemical activity of GAP80 itself not characterized\",\n        \"quantitative contribution of the basal glideosome to motility not measured\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"It was unknown whether the two glideosomes were biochemically independent or shared parts; co-immunoprecipitation showed MyoC uses the same light chains as MyoA and binds GAP50 and GAP40, revealing a shared core architecture.\",\n      \"evidence\": \"co-immunoprecipitation / protein interaction studies in Toxoplasma gondii\",\n      \"pmids\": [\"25393004\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"stoichiometry and direct versus indirect nature of interactions not resolved\",\n        \"no reciprocal validation of the shared light-chain interactions reported\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"What confines MyoC to the posterior pole was unclear; deletion analysis identified IAP1 as the determinant restricting MyoC localization within the GAP80 complex.\",\n      \"evidence\": \"genetic deletion with localization analysis in Toxoplasma gondii\",\n      \"pmids\": [\"25393004\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"molecular mechanism by which IAP1 restricts localization not defined\",\n        \"relationship between IAP1 and GAP80 in complex assembly not established\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether the basal glideosome could substitute for the apical motor was untested; sequential MyoA deletion showed MyoC relocalizes to the pellicle and apical cap and sustains residual invasion, demonstrating functional plasticity.\",\n      \"evidence\": \"genetic deletion of MyoA with localization and invasion assays in Toxoplasma gondii\",\n      \"pmids\": [\"25393004\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"signal triggering compensatory relocalization unknown\",\n        \"efficiency of MyoC-driven invasion relative to MyoA not quantified in detail\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The intrinsic biochemical function of GAP80, its structure, and how it is targeted to the basal polar ring remain unresolved.\",\n      \"evidence\": null,\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"no structural model of GAP80 or the basal glideosome\",\n        \"no defined enzymatic or binding activity for GAP80 itself\",\n        \"recruitment mechanism to the basal polar ring uncharacterized\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0020007\", \"supporting_discovery_ids\": [0, 2], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006928\", \"supporting_discovery_ids\": [0, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\n      \"MyoC-glideosome (basal-pole glideosome) comprising GAP80, MyoC, shared myosin light chains, GAP50, GAP40, and IAP1\"\n    ],\n    \"partners\": [\n      \"MyoC (class XIV myosin C)\",\n      \"shared myosin light chains\",\n      \"GAP50\",\n      \"GAP40\",\n      \"IAP1\"\n    ],\n    \"other_free_text\": [\n      \"GAP80 assembles a basal-pole glideosome distinct from the apical MyoA-glideosome [#0].\",\n      \"The MyoC- and MyoA-glideosomes exhibit functional plasticity, with MyoC relocalizing to compensate for MyoA loss and sustain residual invasion [#3].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_246940","name":"GAP80","product":"gliding-associated protein GAP80","uniprot_acc":"A0A125YH80","chromosome":"TGME49_chrXII","start_pos":3026257},{"strain":"GT1","gene_id":"TGGT1_246940","name":null,"product":"hypothetical protein","uniprot_acc":null,"chromosome":"TGGT1_chrXII","start_pos":2958189},{"strain":"RH88","gene_id":"TGRH88_061140","name":null,"product":"unspecified product","uniprot_acc":null,"chromosome":"CM023093","start_pos":3079523},{"strain":"VEG","gene_id":"TGVEG_246940","name":null,"product":"hypothetical protein","uniprot_acc":"B6KGU8","chromosome":"TGVEG_chrXII","start_pos":2995517}]}