{"gene":"TG_246950","gene_symbol":"AC9","run_date":"2026-09-08T15:31:36+00:00","timeline":{"discoveries":[{"year":2020,"finding":"AC9 localizes to the alveolin network of the inner membrane complex (IMC), intercalated between the subpellicular microtubules (SPMTs), at the apical cap of Toxoplasma gondii, as determined by ultrastructure expansion microscopy (U-ExM) combined with BioID proximity biotinylation.","method":"Ultrastructure expansion microscopy (U-ExM), BioID proximity biotinylation","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Moderate — direct localization by U-ExM with two orthogonal methods (U-ExM + BioID), single lab but rigorous spatial resolution","pmids":["32379047"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"finding":"Conditional depletion of AC9 results in loss of the conoid, disorganization of SPMTs, loss of the apical polar ring (APR), defective microneme secretion, and failure to invade or egress from host cells, establishing AC9 as essential for apical complex integrity and parasite lytic cycle.","method":"Conditional knockdown (auxin-inducible degron or analogous system), electron microscopy, U-ExM, invasion and egress assays, microneme secretion assay","journal":"eLife","confidence":"High","confidence_rationale":"Tier 2 / Strong — clean conditional depletion with multiple orthogonal readouts (EM, U-ExM, functional assays), independently replicated across two labs (PMID 32379047 and 32409604)","pmids":["32379047","32409604"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"finding":"AC9 directly binds the kinase ERK7 through a conserved C-terminal motif of AC9, and this interaction is essential for ERK7 localization and function at the apical cap.","method":"Proximity biotinylation (BioID), direct binding assays, crystal structure of ERK7-AC9 complex","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 1 / Strong — crystal structure of the complex, direct binding demonstrated, functional mutagenesis of the interaction motif, replicated by subsequent study","pmids":["32409604"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"finding":"The crystal structure of the ERK7-AC9 complex reveals that AC9 acts as an inhibitory scaffold: it not only localizes ERK7 to the apical cap but also inhibits ERK7 kinase activity through an unusual set of contacts that displaces nucleotide from the kinase active site.","method":"X-ray crystallography (crystal structure of ERK7-AC9 complex), kinase activity assays","journal":"Proceedings of the National Academy of Sciences of the United States of America","confidence":"High","confidence_rationale":"Tier 1 / Moderate — crystal structure with mechanistic interpretation of nucleotide displacement, single lab but structure-based","pmids":["32409604"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"Depletion of ERK7 phenocopies depletion of AC9 (and AC10), causing loss of the APR, disorganization of SPMTs, severe microneme secretion impairment, dilated apical plasma membrane, and altered rhoptry positioning, confirming that AC9 and ERK7 act in the same pathway for apical complex maintenance.","method":"Conditional depletion, U-ExM with NHS-ester staining, electron microscopy, comparative proteomics, microneme secretion assay","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Strong — genetic epistasis confirmed by multiple orthogonal structural and functional methods, independent replication of AC9 phenotype","pmids":["34607461"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"AC9, AC10, and ERK7 form a ternary complex in the apical cap organized by multivalent pairwise interactions; AC10 is a foundational component of the AC9:AC10:ERK7 complex, and the multiple independent interaction regions among the three proteins drive oligomerization and tethering of ERK7 kinase activity in the apical cap cytoskeleton.","method":"Deletion analysis, yeast two-hybrid, co-immunoprecipitation","journal":"mBio","confidence":"High","confidence_rationale":"Tier 2 / Moderate — reciprocal interaction mapping by yeast two-hybrid and deletion analyses with multiple domain pairs tested, single lab but multiple orthogonal methods","pmids":["35130732"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"AC9 is an intrinsically disordered alveolin/IMC apical cap protein that localizes between the subpellicular microtubules and serves as an inhibitory scaffold for the MAPK ERK7: it directly binds ERK7 via a conserved C-terminal motif (crystal structure resolved), displacing nucleotide from the ERK7 active site to hold it in an 'off' state, while simultaneously concentrating ERK7 at the apical cap through multivalent interactions within an essential AC9:AC10:ERK7 ternary complex; loss of AC9 dismantles this complex and causes catastrophic failure of apical polar ring and conoid assembly, SPMT disorganization, and consequent defects in microneme secretion, invasion, and egress."},"narrative":{"mechanistic_narrative":"AC9 is an alveolin-network component of the inner membrane complex (IMC) that functions as an essential regulatory scaffold for apical complex assembly in Toxoplasma gondii, localizing to the apical cap intercalated between the subpellicular microtubules (SPMTs) [PMID:32379047]. Its central mechanistic role is to control the MAP kinase ERK7: AC9 directly binds ERK7 through a conserved C-terminal motif, and the crystal structure of the ERK7–AC9 complex shows AC9 acting as an inhibitory scaffold that displaces nucleotide from the kinase active site while concentrating ERK7 at the apical cap [PMID:32409604]. AC9 operates within an AC9:AC10:ERK7 ternary complex assembled through multivalent pairwise interactions that oligomerize and tether ERK7 kinase activity to the apical cap cytoskeleton [PMID:35130732]. Conditional depletion of AC9 dismantles this system, causing loss of the conoid and apical polar ring, SPMT disorganization, defective microneme secretion, and failure of invasion and egress; depletion of ERK7 phenocopies these defects, placing AC9 and ERK7 in a single pathway for apical complex integrity [PMID:32379047, PMID:32409604, PMID:34607461].","teleology":[{"year":2020,"claim":"Establishing where AC9 resides addressed whether it is a bona fide apical cytoskeletal protein and pinpointed it to the alveolin network between SPMTs, the structural context needed to interpret its function.","evidence":"Ultrastructure expansion microscopy combined with BioID proximity biotinylation in T. gondii","pmids":["32379047"],"confidence":"High","gaps":["Localization alone does not reveal molecular activity","Does not identify binding partners at the apical cap"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"claim":"Conditional depletion tested whether AC9 is functionally required, showing it is essential for conoid, APR, and SPMT integrity and for the parasite lytic cycle.","evidence":"Conditional knockdown with EM, U-ExM, and invasion/egress/microneme secretion assays in T. gondii","pmids":["32379047","32409604"],"confidence":"High","gaps":["Phenotype does not by itself define the molecular mechanism linking AC9 to apical assembly"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2020,"claim":"Identifying ERK7 as a direct AC9 binding partner and solving the complex structure explained how AC9 works mechanistically — as an inhibitory scaffold that both localizes and switches off the kinase by displacing nucleotide from its active site.","evidence":"BioID, direct binding assays, X-ray crystallography of the ERK7–AC9 complex, and kinase activity assays with interaction-motif mutagenesis","pmids":["32409604"],"confidence":"High","gaps":["Does not resolve how the AC9-imposed 'off' state is relieved or regulated in vivo","In vitro nucleotide displacement not directly tracked in the living parasite"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"Testing ERK7 depletion asked whether AC9 and ERK7 act in the same pathway, and the phenocopy established genetic epistasis for apical complex maintenance.","evidence":"Conditional depletion with U-ExM/NHS-ester staining, EM, comparative proteomics, and microneme secretion assays in T. gondii","pmids":["34607461"],"confidence":"High","gaps":["Does not define the ERK7 substrates whose phosphorylation drives apical assembly"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Interaction mapping addressed how the scaffold is organized, showing AC9, AC10, and ERK7 form a multivalent ternary complex that oligomerizes and tethers ERK7 to the apical cap cytoskeleton.","evidence":"Deletion analysis, yeast two-hybrid, and co-immunoprecipitation in T. gondii","pmids":["35130732"],"confidence":"High","gaps":["Stoichiometry and higher-order architecture of the assembled complex not resolved","Does not establish how the complex couples ERK7 regulation to conoid/APR biogenesis"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"The physiological ERK7 substrates and the trigger that relieves AC9-mediated kinase inhibition during apical complex assembly remain unidentified.","evidence":"","pmids":[],"confidence":"High","gaps":["No ERK7 substrate at the apical cap identified in the corpus","Mechanism regulating the AC9-imposed inhibitory state in vivo unknown"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["AC9:AC10:ERK7 ternary complex","ERK7-AC9 complex"],"partners":["ERK7","AC10"],"other_free_text":["AC9 binds ERK7 via a conserved C-terminal motif and inhibits the kinase by displacing nucleotide from its active site while concentrating it at the apical cap [#2, #3].","AC9 loss dismantles the AC9:AC10:ERK7 complex and causes loss of conoid, APR, SPMT disorganization, and failure of microneme secretion, invasion, and egress [#1, #4, #5]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"32379047","id":"PMC_32379047","title":"Essential function of the alveolin network in the subpellicular microtubules and conoid assembly in Toxoplasma gondii.","date":"2020","source":"eLife","url":"https://pubmed.ncbi.nlm.nih.gov/32379047","citation_count":82,"is_preprint":false},{"pmid":"32409604","id":"PMC_32409604","title":"Ancient MAPK ERK7 is regulated by an unusual inhibitory scaffold required for Toxoplasma apical complex biogenesis.","date":"2020","source":"Proceedings of the National Academy of Sciences of the United States of America","url":"https://pubmed.ncbi.nlm.nih.gov/32409604","citation_count":44,"is_preprint":false},{"pmid":"34607461","id":"PMC_34607461","title":"Revisiting the Role of Toxoplasma gondii ERK7 in the Maintenance and Stability of the Apical Complex.","date":"2021","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/34607461","citation_count":28,"is_preprint":false},{"pmid":"35130732","id":"PMC_35130732","title":"Multivalent Interactions Drive the Toxoplasma AC9:AC10:ERK7 Complex To Concentrate ERK7 in the Apical Cap.","date":"2022","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/35130732","citation_count":21,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":4801,"output_tokens":1669,"usd":0.019719,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6853,"output_tokens":2639,"usd":0.05012,"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\": 2020,\n      \"finding\": \"AC9 localizes to the alveolin network of the inner membrane complex (IMC), intercalated between the subpellicular microtubules (SPMTs), at the apical cap of Toxoplasma gondii, as determined by ultrastructure expansion microscopy (U-ExM) combined with BioID proximity biotinylation.\",\n      \"method\": \"Ultrastructure expansion microscopy (U-ExM), BioID proximity biotinylation\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization by U-ExM with two orthogonal methods (U-ExM + BioID), single lab but rigorous spatial resolution\",\n      \"pmids\": [\"32379047\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"Conditional depletion of AC9 results in loss of the conoid, disorganization of SPMTs, loss of the apical polar ring (APR), defective microneme secretion, and failure to invade or egress from host cells, establishing AC9 as essential for apical complex integrity and parasite lytic cycle.\",\n      \"method\": \"Conditional knockdown (auxin-inducible degron or analogous system), electron microscopy, U-ExM, invasion and egress assays, microneme secretion assay\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — clean conditional depletion with multiple orthogonal readouts (EM, U-ExM, functional assays), independently replicated across two labs (PMID 32379047 and 32409604)\",\n      \"pmids\": [\"32379047\", \"32409604\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"AC9 directly binds the kinase ERK7 through a conserved C-terminal motif of AC9, and this interaction is essential for ERK7 localization and function at the apical cap.\",\n      \"method\": \"Proximity biotinylation (BioID), direct binding assays, crystal structure of ERK7-AC9 complex\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Strong — crystal structure of the complex, direct binding demonstrated, functional mutagenesis of the interaction motif, replicated by subsequent study\",\n      \"pmids\": [\"32409604\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"finding\": \"The crystal structure of the ERK7-AC9 complex reveals that AC9 acts as an inhibitory scaffold: it not only localizes ERK7 to the apical cap but also inhibits ERK7 kinase activity through an unusual set of contacts that displaces nucleotide from the kinase active site.\",\n      \"method\": \"X-ray crystallography (crystal structure of ERK7-AC9 complex), kinase activity assays\",\n      \"journal\": \"Proceedings of the National Academy of Sciences of the United States of America\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — crystal structure with mechanistic interpretation of nucleotide displacement, single lab but structure-based\",\n      \"pmids\": [\"32409604\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Depletion of ERK7 phenocopies depletion of AC9 (and AC10), causing loss of the APR, disorganization of SPMTs, severe microneme secretion impairment, dilated apical plasma membrane, and altered rhoptry positioning, confirming that AC9 and ERK7 act in the same pathway for apical complex maintenance.\",\n      \"method\": \"Conditional depletion, U-ExM with NHS-ester staining, electron microscopy, comparative proteomics, microneme secretion assay\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — genetic epistasis confirmed by multiple orthogonal structural and functional methods, independent replication of AC9 phenotype\",\n      \"pmids\": [\"34607461\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"AC9, AC10, and ERK7 form a ternary complex in the apical cap organized by multivalent pairwise interactions; AC10 is a foundational component of the AC9:AC10:ERK7 complex, and the multiple independent interaction regions among the three proteins drive oligomerization and tethering of ERK7 kinase activity in the apical cap cytoskeleton.\",\n      \"method\": \"Deletion analysis, yeast two-hybrid, co-immunoprecipitation\",\n      \"journal\": \"mBio\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal interaction mapping by yeast two-hybrid and deletion analyses with multiple domain pairs tested, single lab but multiple orthogonal methods\",\n      \"pmids\": [\"35130732\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"AC9 is an intrinsically disordered alveolin/IMC apical cap protein that localizes between the subpellicular microtubules and serves as an inhibitory scaffold for the MAPK ERK7: it directly binds ERK7 via a conserved C-terminal motif (crystal structure resolved), displacing nucleotide from the ERK7 active site to hold it in an 'off' state, while simultaneously concentrating ERK7 at the apical cap through multivalent interactions within an essential AC9:AC10:ERK7 ternary complex; loss of AC9 dismantles this complex and causes catastrophic failure of apical polar ring and conoid assembly, SPMT disorganization, and consequent defects in microneme secretion, invasion, and egress.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"AC9 is an alveolin-network component of the inner membrane complex (IMC) that functions as an essential regulatory scaffold for apical complex assembly in Toxoplasma gondii, localizing to the apical cap intercalated between the subpellicular microtubules (SPMTs) [#0]. Its central mechanistic role is to control the MAP kinase ERK7: AC9 directly binds ERK7 through a conserved C-terminal motif, and the crystal structure of the ERK7–AC9 complex shows AC9 acting as an inhibitory scaffold that displaces nucleotide from the kinase active site while concentrating ERK7 at the apical cap [#2, #3]. AC9 operates within an AC9:AC10:ERK7 ternary complex assembled through multivalent pairwise interactions that oligomerize and tether ERK7 kinase activity to the apical cap cytoskeleton [#5]. Conditional depletion of AC9 dismantles this system, causing loss of the conoid and apical polar ring, SPMT disorganization, defective microneme secretion, and failure of invasion and egress; depletion of ERK7 phenocopies these defects, placing AC9 and ERK7 in a single pathway for apical complex integrity [#1, #4].\",\n  \"teleology\": [\n    {\n      \"year\": 2020,\n      \"claim\": \"Establishing where AC9 resides addressed whether it is a bona fide apical cytoskeletal protein and pinpointed it to the alveolin network between SPMTs, the structural context needed to interpret its function.\",\n      \"evidence\": \"Ultrastructure expansion microscopy combined with BioID proximity biotinylation in T. gondii\",\n      \"pmids\": [\"32379047\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Localization alone does not reveal molecular activity\", \"Does not identify binding partners at the apical cap\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Conditional depletion tested whether AC9 is functionally required, showing it is essential for conoid, APR, and SPMT integrity and for the parasite lytic cycle.\",\n      \"evidence\": \"Conditional knockdown with EM, U-ExM, and invasion/egress/microneme secretion assays in T. gondii\",\n      \"pmids\": [\"32379047\", \"32409604\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Phenotype does not by itself define the molecular mechanism linking AC9 to apical assembly\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2020,\n      \"claim\": \"Identifying ERK7 as a direct AC9 binding partner and solving the complex structure explained how AC9 works mechanistically — as an inhibitory scaffold that both localizes and switches off the kinase by displacing nucleotide from its active site.\",\n      \"evidence\": \"BioID, direct binding assays, X-ray crystallography of the ERK7–AC9 complex, and kinase activity assays with interaction-motif mutagenesis\",\n      \"pmids\": [\"32409604\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not resolve how the AC9-imposed 'off' state is relieved or regulated in vivo\", \"In vitro nucleotide displacement not directly tracked in the living parasite\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Testing ERK7 depletion asked whether AC9 and ERK7 act in the same pathway, and the phenocopy established genetic epistasis for apical complex maintenance.\",\n      \"evidence\": \"Conditional depletion with U-ExM/NHS-ester staining, EM, comparative proteomics, and microneme secretion assays in T. gondii\",\n      \"pmids\": [\"34607461\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not define the ERK7 substrates whose phosphorylation drives apical assembly\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Interaction mapping addressed how the scaffold is organized, showing AC9, AC10, and ERK7 form a multivalent ternary complex that oligomerizes and tethers ERK7 to the apical cap cytoskeleton.\",\n      \"evidence\": \"Deletion analysis, yeast two-hybrid, and co-immunoprecipitation in T. gondii\",\n      \"pmids\": [\"35130732\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Stoichiometry and higher-order architecture of the assembled complex not resolved\", \"Does not establish how the complex couples ERK7 regulation to conoid/APR biogenesis\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The physiological ERK7 substrates and the trigger that relieves AC9-mediated kinase inhibition during apical complex assembly remain unidentified.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"High\",\n      \"gaps\": [\"No ERK7 substrate at the apical cap identified in the corpus\", \"Mechanism regulating the AC9-imposed inhibitory state in vivo unknown\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0019210\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0019900\", \"supporting_discovery_ids\": [2, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0030674\", \"supporting_discovery_ids\": [2, 5], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0070258\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0120227\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0009405\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0007163\", \"supporting_discovery_ids\": [1, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\"AC9:AC10:ERK7 ternary complex\", \"ERK7-AC9 complex\"],\n    \"partners\": [\"ERK7\", \"AC10\"],\n    \"other_free_text\": [\n      \"AC9 binds ERK7 via a conserved C-terminal motif and inhibits the kinase by displacing nucleotide from its active site while concentrating it at the apical cap [#2, #3].\",\n      \"AC9 loss dismantles the AC9:AC10:ERK7 complex and causes loss of conoid, APR, SPMT disorganization, and failure of microneme secretion, invasion, and egress [#1, #4, #5].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_246950","name":"AC9","product":"apical cap protein AC9","uniprot_acc":"A0A125YMK0","chromosome":"TGME49_chrXII","start_pos":3030072},{"strain":"GT1","gene_id":"TGGT1_246950","name":null,"product":"hypothetical protein","uniprot_acc":null,"chromosome":"TGGT1_chrXII","start_pos":2962303},{"strain":"RH88","gene_id":"TGRH88_061150","name":null,"product":"unspecified product","uniprot_acc":null,"chromosome":"CM023093","start_pos":3083637},{"strain":"VEG","gene_id":"TGVEG_246950","name":null,"product":"hypothetical protein","uniprot_acc":"B6KGU9","chromosome":"TGVEG_chrXII","start_pos":2999631}]}