{"gene":"TG_233030","gene_symbol":"GAP70","run_date":"2026-09-08T15:31:29+00:00","timeline":{"discoveries":[{"year":2010,"finding":"GAP70 is a coccidian-specific paralog of GAP45 that specifically recruits the MyoA-glideosome to the apical cap of the parasite, a function distinct from the broader pellicle recruitment role of GAP45.","method":"Functional dissection including transgenera complementation experiments; GAP45 orthologs from Plasmodium falciparum could substitute for Toxoplasma GAP45, but the coccidian GAP45 homolog (GAP70) was shown to specifically localize glideosome recruitment to the apical cap.","journal":"Cell host & microbe","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional complementation experiment with defined localization phenotype, single lab, single study","pmids":["20951968"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"finding":"GAP70 is confirmed as a paralog of GAP45 tailored to recruit MyoA at the apical cap specifically in the coccidian subgroup of Apicomplexa, establishing its role as an apical-cap-restricted glideosome scaffolding protein.","method":"Genetic and biochemical dissection of glideosome components; deletion of glideosome components and analysis of compensatory relocalization between MyoA- and MyoC-glideosomes.","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — deletion genetics with defined localization and functional readouts, single lab, corroborates prior finding","pmids":["25393004"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"GAP70 is a coccidian-specific paralog of GAP45 that functions as an apical-cap-restricted scaffolding component of the MyoA-glideosome, specifically recruiting myosin A to the apical cap of Toxoplasma gondii to power parasite motility and host cell invasion."},"narrative":{"mechanistic_narrative":"GAP70 is a coccidian-specific paralog of the glideosome scaffolding protein GAP45 that spatially specializes the MyoA-glideosome in Toxoplasma gondii by recruiting myosin A to the apical cap of the parasite, a subcellular domain distinct from the broader pellicle recruitment mediated by GAP45 [PMID:20951968]. Functional dissection established that whereas Plasmodium falciparum GAP45 can substitute for Toxoplasma GAP45, GAP70 confers apical-cap-restricted glideosome localization, marking it as a coccidian-tailored scaffolding component [PMID:20951968]. Deletion genetics of glideosome components and analysis of compensatory relocalization between the MyoA- and MyoC-glideosomes corroborated GAP70's role as an apical-cap-restricted glideosome scaffold [PMID:25393004]. Beyond this scaffolding/recruitment role at the apical cap, no further mechanistic detail has been characterized in the available corpus.","teleology":[{"year":2010,"claim":"It was unknown how glideosome recruitment could be spatially subdivided within the parasite pellicle; identifying GAP70 as a GAP45 paralog that recruits the MyoA-glideosome specifically to the apical cap established a mechanism for domain-specific motor positioning.","evidence":"Functional dissection with transgenera complementation, showing Plasmodium GAP45 could substitute for Toxoplasma GAP45 but GAP70 localized glideosome recruitment to the apical cap","pmids":["20951968"],"confidence":"Medium","gaps":["Molecular basis of GAP70's apical-cap targeting was not defined","Direct biochemical interaction between GAP70 and MyoA was not resolved","Consequence for parasite motility and invasion not quantified in this study"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2014,"claim":"Whether GAP70 functions as a bona fide apical-cap-restricted scaffold, distinct from the MyoC-glideosome, was confirmed through deletion genetics and analysis of compensatory relocalization between the MyoA- and MyoC-glideosomes.","evidence":"Genetic and biochemical dissection of glideosome components, including deletion and analysis of compensatory relocalization between MyoA- and MyoC-glideosomes","pmids":["25393004"],"confidence":"Medium","gaps":["Structural details of the GAP70 scaffold assembly not determined","Quantitative contribution of the apical-cap glideosome to invasion not isolated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The molecular determinants of GAP70's apical-cap targeting and its direct binding partners within the MyoA-glideosome remain uncharacterized.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No structural model of the GAP70 scaffold","Recruitment mechanism to the apical cap unknown","Direct MyoA-binding interface not mapped"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["MyoA-glideosome"],"partners":["MYOA (MYOSIN A)","GAP45 (PARALOG)"],"other_free_text":["Coccidian-specific paralog of GAP45 restricted to the apical cap of the parasite","Distinct from GAP45, which mediates broader pellicle recruitment of the glideosome","MyoA-glideosome and MyoC-glideosome show compensatory relocalization upon component deletion"]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"20951968","id":"PMC_20951968","title":"Functional dissection of the apicomplexan glideosome molecular architecture.","date":"2010","source":"Cell host & microbe","url":"https://pubmed.ncbi.nlm.nih.gov/20951968","citation_count":234,"is_preprint":false},{"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":3688,"output_tokens":607,"usd":0.010084,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5287,"output_tokens":1651,"usd":0.033855,"stage2_stop_reason":"end_turn"},"total_usd":0.0,"stage1_batch_id":"msgbatch_01WgHz6kceqm573AGLyz57at","stage2_batch_id":"msgbatch_01LK4wDYj5zYquahv7gi9893","note":"batch pricing = 50% of standard","skipped":true},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2010,\n      \"finding\": \"GAP70 is a coccidian-specific paralog of GAP45 that specifically recruits the MyoA-glideosome to the apical cap of the parasite, a function distinct from the broader pellicle recruitment role of GAP45.\",\n      \"method\": \"Functional dissection including transgenera complementation experiments; GAP45 orthologs from Plasmodium falciparum could substitute for Toxoplasma GAP45, but the coccidian GAP45 homolog (GAP70) was shown to specifically localize glideosome recruitment to the apical cap.\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional complementation experiment with defined localization phenotype, single lab, single study\",\n      \"pmids\": [\"20951968\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"GAP70 is confirmed as a paralog of GAP45 tailored to recruit MyoA at the apical cap specifically in the coccidian subgroup of Apicomplexa, establishing its role as an apical-cap-restricted glideosome scaffolding protein.\",\n      \"method\": \"Genetic and biochemical dissection of glideosome components; deletion of glideosome components and analysis of compensatory relocalization between MyoA- and MyoC-glideosomes.\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — deletion genetics with defined localization and functional readouts, single lab, corroborates prior finding\",\n      \"pmids\": [\"25393004\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"GAP70 is a coccidian-specific paralog of GAP45 that functions as an apical-cap-restricted scaffolding component of the MyoA-glideosome, specifically recruiting myosin A to the apical cap of Toxoplasma gondii to power parasite motility and host cell invasion.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"GAP70 is a coccidian-specific paralog of the glideosome scaffolding protein GAP45 that spatially specializes the MyoA-glideosome in Toxoplasma gondii by recruiting myosin A to the apical cap of the parasite, a subcellular domain distinct from the broader pellicle recruitment mediated by GAP45 [#0]. Functional dissection established that whereas Plasmodium falciparum GAP45 can substitute for Toxoplasma GAP45, GAP70 confers apical-cap-restricted glideosome localization, marking it as a coccidian-tailored scaffolding component [#0]. Deletion genetics of glideosome components and analysis of compensatory relocalization between the MyoA- and MyoC-glideosomes corroborated GAP70's role as an apical-cap-restricted glideosome scaffold [#1]. Beyond this scaffolding/recruitment role at the apical cap, no further mechanistic detail has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"It was unknown how glideosome recruitment could be spatially subdivided within the parasite pellicle; identifying GAP70 as a GAP45 paralog that recruits the MyoA-glideosome specifically to the apical cap established a mechanism for domain-specific motor positioning.\",\n      \"evidence\": \"Functional dissection with transgenera complementation, showing Plasmodium GAP45 could substitute for Toxoplasma GAP45 but GAP70 localized glideosome recruitment to the apical cap\",\n      \"pmids\": [\"20951968\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Molecular basis of GAP70's apical-cap targeting was not defined\",\n        \"Direct biochemical interaction between GAP70 and MyoA was not resolved\",\n        \"Consequence for parasite motility and invasion not quantified in this study\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"claim\": \"Whether GAP70 functions as a bona fide apical-cap-restricted scaffold, distinct from the MyoC-glideosome, was confirmed through deletion genetics and analysis of compensatory relocalization between the MyoA- and MyoC-glideosomes.\",\n      \"evidence\": \"Genetic and biochemical dissection of glideosome components, including deletion and analysis of compensatory relocalization between MyoA- and MyoC-glideosomes\",\n      \"pmids\": [\"25393004\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Structural details of the GAP70 scaffold assembly not determined\",\n        \"Quantitative contribution of the apical-cap glideosome to invasion not isolated\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The molecular determinants of GAP70's apical-cap targeting and its direct binding partners within the MyoA-glideosome remain uncharacterized.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural model of the GAP70 scaffold\",\n        \"Recruitment mechanism to the apical cap unknown\",\n        \"Direct MyoA-binding interface not mapped\"\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:0071944\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0052126\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\"MyoA-glideosome\"],\n    \"partners\": [\"MyoA (myosin A)\", \"GAP45 (paralog)\"],\n    \"other_free_text\": [\n      \"Coccidian-specific paralog of GAP45 restricted to the apical cap of the parasite\",\n      \"Distinct from GAP45, which mediates broader pellicle recruitment of the glideosome\",\n      \"MyoA-glideosome and MyoC-glideosome show compensatory relocalization upon component deletion\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_233030","name":"GAP70","product":"gliding-associated protein GAP70","uniprot_acc":"S8F2K4","chromosome":"TGME49_chrVIII","start_pos":2352831},{"strain":"GT1","gene_id":"TGGT1_233030","name":"GAP70","product":"gliding-associated protein GAP70","uniprot_acc":null,"chromosome":"TGGT1_chrVIII","start_pos":2349458},{"strain":"RH88","gene_id":"TGRH88_077010","name":null,"product":"gliding-associated protein GAP70","uniprot_acc":null,"chromosome":"CM023089","start_pos":7459723},{"strain":"VEG","gene_id":"TGVEG_233030","name":null,"product":"gliding-associated protein GAP70","uniprot_acc":"V4ZV66","chromosome":"TGVEG_chrVIII","start_pos":2362425}]}