{"gene":"TG_261440","gene_symbol":"ARO","run_date":"2026-09-08T12:58:25","timeline":{"discoveries":[{"year":2013,"finding":"TgARO is an acylated protein homogenously anchored to the rhoptry membrane; conditional disruption causes random cytosolic dispersion of rhoptries and severe invasion defect, but no effect on intracellular growth or egress, establishing ARO as specifically required for apical positioning of rhoptries for invasion.","method":"Conditional disruption (loss-of-function), complementation with wild-type vs. acylation mutant TgARO","journal":"Cell host & microbe","confidence":"High","confidence_rationale":"Tier 2 / Strong — conditional KO with specific phenotypic readouts, complementation with acylation mutant distinguishing mechanism, multiple orthogonal experiments in single rigorous study","pmids":["23498954"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"finding":"TgARO interacts with myosin F (MyoF), and inhibition of actin polymerization or myosin function also results in rhoptry dispersal, indicating that apical positioning of rhoptries is an actomyosin-based process dependent on TgARO.","method":"Co-immunoprecipitation (TgARO–MyoF interaction), pharmacological inhibition of actin polymerization and myosin function with phenotypic readout","journal":"Cell host & microbe","confidence":"High","confidence_rationale":"Tier 2 / Strong — protein interaction combined with functional pharmacological inhibition, consistent phenotype, single rigorous study with multiple orthogonal methods","pmids":["23498954"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"finding":"Acylation of TgARO is functionally required for rhoptry positioning: an acylation mutant fails to complement rhoptry dispersal caused by ARO depletion.","method":"Complementation assay with acylation mutant TgARO","journal":"Cell host & microbe","confidence":"High","confidence_rationale":"Tier 2 / Strong — site-directed mutagenesis (acylation mutant) with complementation readout in conditional KO background","pmids":["23498954"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"finding":"ARO interacts with two additional partners localizing to a rhoptry subcompartment: ARO-interacting protein (AIP) and adenylate cyclase β (ACβ); in the absence of AIP, ACβ disappears from rhoptries, placing AIP upstream of ACβ recruitment.","method":"Protein interaction studies (Co-IP/pulldown), loss-of-function of AIP with localization readout by imaging","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal interaction and epistatic localization evidence, single lab","pmids":["26769898"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"finding":"ARO is multifunctional: systematic deletion of individual armadillo (ARM) repeats demonstrates that ARO participates not only in rhoptry positioning but also in rhoptry clustering, with each ARM repeat contributing to overall function.","method":"ARM repeat deletion mutagenesis with phenotypic readout (positioning and clustering)","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — structure–function mutagenesis across all ARM repeats, single lab","pmids":["26769898"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"finding":"Structural analyses reveal that TgARO resembles the myosin-binding domain of C. elegans UNC-45, with a conserved patch of aromatic and acidic residues identifying the putative MyoF-binding site.","method":"Structural analysis (crystallography/structural homology) with identification of conserved surface patch","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 1 / Moderate — structural determination with functional annotation of binding site, but binding site not validated by mutagenesis per abstract","pmids":["26769898"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"finding":"Plasmodium falciparum ARO functionally complements TgARO depletion in Toxoplasma and interacts with the same partners (AIP, ACβ, MyoF), demonstrating conservation of ARO-mediated rhoptry biogenesis across Apicomplexa.","method":"Heterologous complementation of TgARO-depleted parasites with PfARO; co-immunoprecipitation of PfARO with TgARO partners","journal":"Journal of cell science","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — functional complementation plus interaction studies, single lab, two orthogonal methods","pmids":["26769898"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""},{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"TgARO is an acylated rhoptry-membrane-anchored armadillo-repeat protein that mediates apical positioning and clustering of rhoptries through an actomyosin-dependent mechanism involving direct interaction with myosin F, AIP, and adenylate cyclase β, and this positioning function is strictly required for host cell invasion but not for intracellular growth or egress."},"narrative":{"mechanistic_narrative":"ARO is an acylated armadillo-repeat protein anchored homogeneously to the rhoptry membrane in apicomplexan parasites, where it governs the apical positioning and clustering of rhoptries required for host cell invasion [PMID:23498954, PMID:26769898]. Conditional disruption of TgARO causes rhoptries to disperse randomly into the cytosol and produces a severe invasion defect while leaving intracellular growth and egress intact, defining ARO's function as specifically dedicated to rhoptry positioning rather than organelle biogenesis or discharge [PMID:23498954]. This positioning is an actomyosin-based process: ARO interacts directly with myosin F, and pharmacological inhibition of actin polymerization or myosin function phenocopies rhoptry dispersal [PMID:23498954]; ARO's own N-terminal acylation is functionally required, since an acylation-defective mutant fails to complement the dispersal phenotype [PMID:23498954]. Structurally, TgARO resembles the myosin-binding domain of C. elegans UNC-45, with a conserved aromatic/acidic surface patch marking the putative MyoF-binding site, and its individual ARM repeats each contribute to positioning and clustering [PMID:26769898]. ARO scaffolds a rhoptry subcompartment complex with ARO-interacting protein (AIP) and adenylate cyclase β (ACβ), with AIP acting upstream to recruit ACβ [PMID:26769898]. This ARO-based system is conserved across Apicomplexa: Plasmodium falciparum ARO complements TgARO depletion and binds the same partners [PMID:26769898].","teleology":[{"year":2013,"claim":"Before this work it was unknown what tethers rhoptries at the parasite apex; conditional disruption established ARO as a membrane-anchored factor specifically required to position rhoptries apically for invasion, distinct from organelle formation or discharge.","evidence":"Conditional loss-of-function with invasion/growth/egress readouts plus complementation in Toxoplasma gondii","pmids":["23498954"],"confidence":"High","gaps":["Does not define the molecular force-transmission mechanism linking ARO to the cytoskeleton","Does not identify the acyltransferase or acylation site chemistry"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"claim":"To explain how ARO positions rhoptries, it was shown that ARO binds myosin F and that disrupting actomyosin phenocopies ARO loss, establishing rhoptry positioning as an actomyosin-driven, ARO-dependent process.","evidence":"Co-immunoprecipitation of ARO with MyoF plus pharmacological actin/myosin inhibition in Toxoplasma gondii","pmids":["23498954"],"confidence":"High","gaps":["MyoF-binding interface not mapped by mutagenesis at this stage","Directionality and regulation of the actomyosin force are not resolved"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2013,"claim":"To test whether membrane anchoring is mechanistically essential, an acylation-mutant complementation showed acylation is required for ARO to rescue rhoptry positioning, tying membrane attachment to function.","evidence":"Site-directed acylation mutant complementation in ARO-depleted Toxoplasma gondii","pmids":["23498954"],"confidence":"High","gaps":["Identity of the modifying enzyme and specific residues not established"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"claim":"To define the ARO interaction network, AIP and adenylate cyclase β were identified as partners at a rhoptry subcompartment, with AIP placed upstream of ACβ recruitment, revealing an ordered ARO-scaffolded complex.","evidence":"Co-IP/pulldown plus AIP loss-of-function with imaging of ACβ localization in Toxoplasma gondii","pmids":["26769898"],"confidence":"Medium","gaps":["Functional role of ACβ signaling at the rhoptry not established","Single-lab interaction data"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"claim":"Systematic ARM-repeat deletion demonstrated ARO is multifunctional, contributing to both rhoptry positioning and clustering with each repeat participating, extending its role beyond apical tethering.","evidence":"ARM-repeat deletion mutagenesis with positioning and clustering readouts in Toxoplasma gondii","pmids":["26769898"],"confidence":"Medium","gaps":["Which repeats bind which partners not fully assigned","Molecular basis of clustering versus positioning not separated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"claim":"A structural model placed TgARO as a UNC-45-like myosin-binding domain and identified a candidate MyoF-binding surface, providing a structural rationale for its actomyosin coupling.","evidence":"Structural analysis identifying a conserved aromatic/acidic surface patch in Toxoplasma gondii","pmids":["26769898"],"confidence":"Medium","gaps":["Putative MyoF-binding patch not validated by mutagenesis","No structure of the ARO–MyoF complex"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2016,"claim":"Heterologous complementation showed PfARO can substitute for TgARO and binds the same partners, establishing ARO-mediated rhoptry biogenesis as conserved across Apicomplexa.","evidence":"Complementation of TgARO-depleted parasites with PfARO plus co-IP with shared partners","pmids":["26769898"],"confidence":"Medium","gaps":["Conservation of the actomyosin dependence in Plasmodium not directly tested","Endogenous PfARO phenotype in Plasmodium not assessed here"],"attribution":[{"species":"Toxoplasma gondii","strain":""},{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"How ARO-anchored actomyosin generates and directs the force that positions and clusters rhoptries, and what signaling role ACβ plays at this subcompartment, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["Force-transmission mechanism from ARO to the rhoptry membrane unknown","Functional output of ACβ at the rhoptry uncharacterized","MyoF-binding interface not experimentally validated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["ARO–AIP–adenylate cyclase β rhoptry subcompartment complex"],"partners":["MYOSIN F (MYOF)","ARO-INTERACTING PROTEIN (AIP)","ADENYLATE CYCLASE Β (ACΒ)"],"other_free_text":["ARO is acylated and anchored homogeneously to the rhoptry membrane; acylation is required for its rhoptry-positioning function.","Composed of armadillo (ARM) repeats, each contributing to positioning and clustering functions.","Structurally resembles the myosin-binding domain of C. elegans UNC-45.","Function conserved across Apicomplexa: PfARO complements TgARO depletion and binds the same partners."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"23498954","id":"PMC_23498954","title":"The Toxoplasma protein ARO mediates the apical positioning of rhoptry organelles, a prerequisite for host cell invasion.","date":"2013","source":"Cell host & microbe","url":"https://pubmed.ncbi.nlm.nih.gov/23498954","citation_count":77,"is_preprint":false},{"pmid":"26769898","id":"PMC_26769898","title":"Structural and functional dissection of Toxoplasma gondii armadillo repeats only protein.","date":"2016","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/26769898","citation_count":26,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3264,"output_tokens":1657,"usd":0.017323,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6901,"output_tokens":3287,"usd":0.05834,"stage2_stop_reason":"end_turn"},"total_usd":0.075663,"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\": 2013,\n      \"finding\": \"TgARO is an acylated protein homogenously anchored to the rhoptry membrane; conditional disruption causes random cytosolic dispersion of rhoptries and severe invasion defect, but no effect on intracellular growth or egress, establishing ARO as specifically required for apical positioning of rhoptries for invasion.\",\n      \"method\": \"Conditional disruption (loss-of-function), complementation with wild-type vs. acylation mutant TgARO\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — conditional KO with specific phenotypic readouts, complementation with acylation mutant distinguishing mechanism, multiple orthogonal experiments in single rigorous study\",\n      \"pmids\": [\"23498954\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"TgARO interacts with myosin F (MyoF), and inhibition of actin polymerization or myosin function also results in rhoptry dispersal, indicating that apical positioning of rhoptries is an actomyosin-based process dependent on TgARO.\",\n      \"method\": \"Co-immunoprecipitation (TgARO–MyoF interaction), pharmacological inhibition of actin polymerization and myosin function with phenotypic readout\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — protein interaction combined with functional pharmacological inhibition, consistent phenotype, single rigorous study with multiple orthogonal methods\",\n      \"pmids\": [\"23498954\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"finding\": \"Acylation of TgARO is functionally required for rhoptry positioning: an acylation mutant fails to complement rhoptry dispersal caused by ARO depletion.\",\n      \"method\": \"Complementation assay with acylation mutant TgARO\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — site-directed mutagenesis (acylation mutant) with complementation readout in conditional KO background\",\n      \"pmids\": [\"23498954\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"ARO interacts with two additional partners localizing to a rhoptry subcompartment: ARO-interacting protein (AIP) and adenylate cyclase β (ACβ); in the absence of AIP, ACβ disappears from rhoptries, placing AIP upstream of ACβ recruitment.\",\n      \"method\": \"Protein interaction studies (Co-IP/pulldown), loss-of-function of AIP with localization readout by imaging\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal interaction and epistatic localization evidence, single lab\",\n      \"pmids\": [\"26769898\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"ARO is multifunctional: systematic deletion of individual armadillo (ARM) repeats demonstrates that ARO participates not only in rhoptry positioning but also in rhoptry clustering, with each ARM repeat contributing to overall function.\",\n      \"method\": \"ARM repeat deletion mutagenesis with phenotypic readout (positioning and clustering)\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — structure–function mutagenesis across all ARM repeats, single lab\",\n      \"pmids\": [\"26769898\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Structural analyses reveal that TgARO resembles the myosin-binding domain of C. elegans UNC-45, with a conserved patch of aromatic and acidic residues identifying the putative MyoF-binding site.\",\n      \"method\": \"Structural analysis (crystallography/structural homology) with identification of conserved surface patch\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — structural determination with functional annotation of binding site, but binding site not validated by mutagenesis per abstract\",\n      \"pmids\": [\"26769898\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"Plasmodium falciparum ARO functionally complements TgARO depletion in Toxoplasma and interacts with the same partners (AIP, ACβ, MyoF), demonstrating conservation of ARO-mediated rhoptry biogenesis across Apicomplexa.\",\n      \"method\": \"Heterologous complementation of TgARO-depleted parasites with PfARO; co-immunoprecipitation of PfARO with TgARO partners\",\n      \"journal\": \"Journal of cell science\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — functional complementation plus interaction studies, single lab, two orthogonal methods\",\n      \"pmids\": [\"26769898\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}, {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgARO is an acylated rhoptry-membrane-anchored armadillo-repeat protein that mediates apical positioning and clustering of rhoptries through an actomyosin-dependent mechanism involving direct interaction with myosin F, AIP, and adenylate cyclase β, and this positioning function is strictly required for host cell invasion but not for intracellular growth or egress.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"ARO is an acylated armadillo-repeat protein anchored homogeneously to the rhoptry membrane in apicomplexan parasites, where it governs the apical positioning and clustering of rhoptries required for host cell invasion [#0, #4]. Conditional disruption of TgARO causes rhoptries to disperse randomly into the cytosol and produces a severe invasion defect while leaving intracellular growth and egress intact, defining ARO's function as specifically dedicated to rhoptry positioning rather than organelle biogenesis or discharge [#0]. This positioning is an actomyosin-based process: ARO interacts directly with myosin F, and pharmacological inhibition of actin polymerization or myosin function phenocopies rhoptry dispersal [#1]; ARO's own N-terminal acylation is functionally required, since an acylation-defective mutant fails to complement the dispersal phenotype [#2]. Structurally, TgARO resembles the myosin-binding domain of C. elegans UNC-45, with a conserved aromatic/acidic surface patch marking the putative MyoF-binding site, and its individual ARM repeats each contribute to positioning and clustering [#4, #5]. ARO scaffolds a rhoptry subcompartment complex with ARO-interacting protein (AIP) and adenylate cyclase \\u03b2 (AC\\u03b2), with AIP acting upstream to recruit AC\\u03b2 [#3]. This ARO-based system is conserved across Apicomplexa: Plasmodium falciparum ARO complements TgARO depletion and binds the same partners [#6].\",\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Before this work it was unknown what tethers rhoptries at the parasite apex; conditional disruption established ARO as a membrane-anchored factor specifically required to position rhoptries apically for invasion, distinct from organelle formation or discharge.\",\n      \"evidence\": \"Conditional loss-of-function with invasion/growth/egress readouts plus complementation in Toxoplasma gondii\",\n      \"pmids\": [\"23498954\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Does not define the molecular force-transmission mechanism linking ARO to the cytoskeleton\", \"Does not identify the acyltransferase or acylation site chemistry\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"To explain how ARO positions rhoptries, it was shown that ARO binds myosin F and that disrupting actomyosin phenocopies ARO loss, establishing rhoptry positioning as an actomyosin-driven, ARO-dependent process.\",\n      \"evidence\": \"Co-immunoprecipitation of ARO with MyoF plus pharmacological actin/myosin inhibition in Toxoplasma gondii\",\n      \"pmids\": [\"23498954\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"MyoF-binding interface not mapped by mutagenesis at this stage\", \"Directionality and regulation of the actomyosin force are not resolved\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2013,\n      \"claim\": \"To test whether membrane anchoring is mechanistically essential, an acylation-mutant complementation showed acylation is required for ARO to rescue rhoptry positioning, tying membrane attachment to function.\",\n      \"evidence\": \"Site-directed acylation mutant complementation in ARO-depleted Toxoplasma gondii\",\n      \"pmids\": [\"23498954\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\"Identity of the modifying enzyme and specific residues not established\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"To define the ARO interaction network, AIP and adenylate cyclase \\u03b2 were identified as partners at a rhoptry subcompartment, with AIP placed upstream of AC\\u03b2 recruitment, revealing an ordered ARO-scaffolded complex.\",\n      \"evidence\": \"Co-IP/pulldown plus AIP loss-of-function with imaging of AC\\u03b2 localization in Toxoplasma gondii\",\n      \"pmids\": [\"26769898\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Functional role of AC\\u03b2 signaling at the rhoptry not established\", \"Single-lab interaction data\"]\n    ,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Systematic ARM-repeat deletion demonstrated ARO is multifunctional, contributing to both rhoptry positioning and clustering with each repeat participating, extending its role beyond apical tethering.\",\n      \"evidence\": \"ARM-repeat deletion mutagenesis with positioning and clustering readouts in Toxoplasma gondii\",\n      \"pmids\": [\"26769898\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Which repeats bind which partners not fully assigned\", \"Molecular basis of clustering versus positioning not separated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"A structural model placed TgARO as a UNC-45-like myosin-binding domain and identified a candidate MyoF-binding surface, providing a structural rationale for its actomyosin coupling.\",\n      \"evidence\": \"Structural analysis identifying a conserved aromatic/acidic surface patch in Toxoplasma gondii\",\n      \"pmids\": [\"26769898\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Putative MyoF-binding patch not validated by mutagenesis\", \"No structure of the ARO\\u2013MyoF complex\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"claim\": \"Heterologous complementation showed PfARO can substitute for TgARO and binds the same partners, establishing ARO-mediated rhoptry biogenesis as conserved across Apicomplexa.\",\n      \"evidence\": \"Complementation of TgARO-depleted parasites with PfARO plus co-IP with shared partners\",\n      \"pmids\": [\"26769898\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Conservation of the actomyosin dependence in Plasmodium not directly tested\", \"Endogenous PfARO phenotype in Plasmodium not assessed here\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}, {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How ARO-anchored actomyosin generates and directs the force that positions and clusters rhoptries, and what signaling role AC\\u03b2 plays at this subcompartment, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Force-transmission mechanism from ARO to the rhoptry membrane unknown\", \"Functional output of AC\\u03b2 at the rhoptry uncharacterized\", \"MyoF-binding interface not experimentally validated\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0017022\", \"supporting_discovery_ids\": [1, 5], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [1, 3, 6], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0033106\", \"supporting_discovery_ids\": [0, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0044409\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0051656\", \"supporting_discovery_ids\": [0, 4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [\n      \"ARO\\u2013AIP\\u2013adenylate cyclase \\u03b2 rhoptry subcompartment complex\"\n    ],\n    \"partners\": [\n      \"Myosin F (MyoF)\",\n      \"ARO-interacting protein (AIP)\",\n      \"Adenylate cyclase \\u03b2 (AC\\u03b2)\"\n    ],\n    \"other_free_text\": [\n      \"ARO is acylated and anchored homogeneously to the rhoptry membrane; acylation is required for its rhoptry-positioning function.\",\n      \"Composed of armadillo (ARM) repeats, each contributing to positioning and clustering functions.\",\n      \"Structurally resembles the myosin-binding domain of C. elegans UNC-45.\",\n      \"Function conserved across Apicomplexa: PfARO complements TgARO depletion and binds the same partners.\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_261440","name":"ARO","product":"armadillo repeats only protein ARO","uniprot_acc":"A0A125YNN5","chromosome":"TGME49_chrVIIb","start_pos":1749438},{"strain":"GT1","gene_id":"TGGT1_261440","name":null,"product":"ARM repeats containing protein","uniprot_acc":null,"chromosome":"TGGT1_chrVIIb","start_pos":1723817},{"strain":"RH88","gene_id":"TGRH88_069270","name":null,"product":"ARM repeats containing protein","uniprot_acc":null,"chromosome":"CM023089","start_pos":1769526},{"strain":"VEG","gene_id":"TGVEG_261440","name":null,"product":"ARM repeats containing protein","uniprot_acc":"B9PKH1","chromosome":"TGVEG_chrVIIb","start_pos":1765975}]}