{"gene":"TG_315670","gene_symbol":"PP2A-A","run_date":"2026-09-11T11:01:00","timeline":{"discoveries":[{"year":2022,"finding":"The T. gondii PP2A holoenzyme is composed of a catalytic subunit PP2A-C, a scaffold subunit PP2A-A, and a regulatory subunit PP2A-B; disruption of any single subunit (including PP2A-A) increases starch accumulation and blocks tachyzoite-to-bradyzoite differentiation. PP2A contributes to amylopectin metabolism via dephosphorylation of calcium-dependent protein kinase 2 (CDPK2) at S679.","method":"Genetic disruption of individual subunits, phosphoproteomics, biochemical characterization of holoenzyme composition, in vivo starch accumulation assays","journal":"Nature communications","confidence":"High","confidence_rationale":"Tier 2 / Strong — multiple subunit knockouts each recapitulate phenotype, phosphoproteomics identifies substrate (CDPK2-S679), multiple orthogonal methods in a single rigorous study","pmids":["36476594"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2025,"finding":"PTPA (phosphotyrosyl phosphatase activator) forms a ternary complex with PP2A A and C subunits in T. gondii, validated by reciprocal pull-down assays; depletion of PTPA impairs tachyzoite proliferation, invasion, gliding motility, and stress-induced bradyzoite cyst formation, and causes amylopectin accumulation and lipid droplet proliferation. The PP2A inhibitor LB-100 phenocopies PTPA depletion.","method":"Reciprocal pull-down assays (ternary complex validation), conditional depletion of PTPA, LB-100 chemical inhibition, phenotypic assays (proliferation, invasion, gliding, cyst formation)","journal":"Cells","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal pull-down confirms complex, chemical phenocopy with LB-100, single lab with multiple orthogonal methods","pmids":["40498010"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"The T. gondii PP2A-A (scaffold/structural) subunit assembles with catalytic (PP2A-C) and regulatory (PP2A-B) subunits into distinct holoenzyme complexes that regulate parasite starch/amylopectin metabolism via dephosphorylation of CDPK2-S679, control tachyzoite cytokinesis and daughter cell emergence (PP2A-2 holoenzyme with PP2A-A2/PP2A-C2/TgPR48), and participate in a PTPA-regulated axis governing tachyzoite proliferation and bradyzoite differentiation; exported parasite effectors (GRA16, GRA18) also exploit host PP2A complexes containing the A subunit to reprogram host gene expression and immune signaling."},"narrative":{"mechanistic_narrative":"PP2A-A is the scaffold/structural subunit of Toxoplasma gondii PP2A phosphatase holoenzymes, assembling with a catalytic subunit (PP2A-C) and a variable regulatory subunit (PP2A-B) to form distinct complexes that govern parasite carbohydrate metabolism and division [PMID:36476594]. Through a PP2A-A/PP2A-C/PP2A-B holoenzyme, the phosphatase controls amylopectin/starch metabolism by dephosphorylating CDPK2 at S679, and disruption of any single subunit — including PP2A-A — causes starch over-accumulation and blocks tachyzoite-to-bradyzoite differentiation [PMID:36476594]. Assembly and activity of the PP2A A/C core are promoted by PTPA, which forms a ternary complex with the A and C subunits and is needed for proliferation, invasion, gliding, and cyst formation [PMID:40498010]. Nothing further is known about PP2A-A-specific mechanistic roles in Toxoplasma gondii from the remaining literature.","teleology":[{"year":2022,"claim":"Defining the parasite's own PP2A-A/B/C holoenzyme and a phospho-substrate answered what intrinsic process PP2A controls, linking it to starch metabolism and stage differentiation.","evidence":"Genetic disruption of individual subunits, phosphoproteomics identifying CDPK2-S679, and starch accumulation assays","pmids":["36476594"],"confidence":"High","gaps":["Direct dephosphorylation of CDPK2-S679 by the holoenzyme not reconstituted in vitro","Additional substrates beyond CDPK2 not enumerated"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2025,"claim":"Identifying PTPA as a ternary partner of the A and C subunits established an upstream regulator that activates PP2A to sustain proliferation, invasion, motility, and differentiation.","evidence":"Reciprocal pull-down assays, conditional PTPA depletion, LB-100 chemical phenocopy, and phenotypic assays","pmids":["40498010"],"confidence":"Medium","gaps":["Mechanism by which PTPA activates the A/C complex not resolved","Whether PTPA acts on all PP2A holoenzymes or a subset unclear"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["PP2A holoenzyme (PP2A-A scaffold / PP2A-C catalytic / PP2A-B regulatory)","PTPA-PP2A A/C ternary complex"],"partners":["PP2A-C (CATALYTIC SUBUNIT)","PP2A-B (REGULATORY SUBUNIT)","PTPA","CDPK2 (SUBSTRATE, S679)"],"other_free_text":["PP2A-A serves as the shared scaffold across at least two distinct parasite holoenzymes with separable roles in amylopectin metabolism/differentiation and in cytokinesis.","Chemical inhibition with okadaic acid and LB-100 phenocopies genetic subunit loss, corroborating PP2A activity requirement.","Toxoplasma effectors GRA16 and GRA18 exploit host PP2A-A-containing holoenzymes to reprogram host p53/cell-cycle and β-catenin/anti-inflammatory signaling."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"36476594","id":"PMC_36476594","title":"The protein phosphatase 2A holoenzyme is a key regulator of starch metabolism and bradyzoite differentiation in Toxoplasma gondii.","date":"2022","source":"Nature communications","url":"https://pubmed.ncbi.nlm.nih.gov/36476594","citation_count":46,"is_preprint":false},{"pmid":"40783178","id":"PMC_40783178","title":"Live-attenuated Toxoplasma gondii PruΔpp2a-c mutant elicits protective immunity against toxoplasmosis in mice and cats.","date":"2025","source":"International journal for parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/40783178","citation_count":4,"is_preprint":false},{"pmid":"36804381","id":"PMC_36804381","title":"Converting and hoarding driven by protein phosphorylation in Toxoplasma gondii.","date":"2023","source":"Trends in parasitology","url":"https://pubmed.ncbi.nlm.nih.gov/36804381","citation_count":1,"is_preprint":false},{"pmid":"40498010","id":"PMC_40498010","title":"PTPA Governs Stress-Responsive Differentiation and Metabolic Homeostasis in Toxoplasma gondii.","date":"2025","source":"Cells","url":"https://pubmed.ncbi.nlm.nih.gov/40498010","citation_count":0,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":7840,"output_tokens":1916,"usd":0.02613,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":7220,"output_tokens":3858,"usd":0.066275,"stage2_stop_reason":"end_turn"},"total_usd":0.096737,"stage1_batch_id":"msgbatch_01S6GjoYQm8LTPUsdhASdqag","stage2_batch_id":"msgbatch_01VX63RTMdBJqsG6gQMqoCjz","note":"batch pricing = 50% of standard","corrective_rerun":"2026-09-10 wrong-gene rerun (round-4 rules)","corrective_reason":"summary amended","hand_review_patch":"2026-09-11 AK hand-review verdicts (handoff/tools_2026-09-11/patch)","hand_review_verdict":"edit"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2013,\n      \"finding\": \"Toxoplasma GRA16 binds host PP2A phosphatase (the A scaffold subunit-containing holoenzyme) and induces nuclear translocation of the PP2A holoenzyme in host cells, contributing to modulation of the p53 pathway and cell-cycle gene expression.\",\n      \"method\": \"Dense granule protein identification, binding assays (GRA16 co-purification with host PP2A and HAUSP), nuclear translocation assay, GRA16 knockout virulence assessment\",\n      \"journal\": \"Cell host & microbe\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct binding demonstrated with functional consequence (nuclear translocation, p53 modulation), single lab but multiple orthogonal approaches\",\n      \"pmids\": [\"23601110\"],\n      \"is_preprint\": false,\n      \"attribution\": []\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"Toxoplasma GRA18 forms complexes with host GSK3/PP2A-B56 (a PP2A regulatory subunit-containing complex) in the host cell cytoplasm, driving β-catenin up-regulation and downstream anti-inflammatory gene expression in macrophages.\",\n      \"method\": \"Co-immunoprecipitation, mass spectrometry identification of GRA18-interacting partners, gene expression analysis in macrophages\",\n      \"journal\": \"eLife\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP and MS interactome, single lab with two orthogonal methods\",\n      \"pmids\": [\"30320549\"],\n      \"is_preprint\": false,\n      \"attribution\": []\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"The T. gondii PP2A holoenzyme is composed of a catalytic subunit PP2A-C, a scaffold subunit PP2A-A, and a regulatory subunit PP2A-B; disruption of any single subunit (including PP2A-A) increases starch accumulation and blocks tachyzoite-to-bradyzoite differentiation. PP2A contributes to amylopectin metabolism via dephosphorylation of calcium-dependent protein kinase 2 (CDPK2) at S679.\",\n      \"method\": \"Genetic disruption of individual subunits, phosphoproteomics, biochemical characterization of holoenzyme composition, in vivo starch accumulation assays\",\n      \"journal\": \"Nature communications\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — multiple subunit knockouts each recapitulate phenotype, phosphoproteomics identifies substrate (CDPK2-S679), multiple orthogonal methods in a single rigorous study\",\n      \"pmids\": [\"36476594\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"The PP2Acα-B'/PR61 holoenzyme complex (containing PP2A-A scaffold subunit) is required for carbohydrate (amylopectin) metabolism and intracellular proliferation of T. gondii tachyzoites; loss of either PP2Acα or B'/PR61 leads to polysaccharide accumulation, disrupted glucose metabolism, reduced ATP production, and impaired virulence.\",\n      \"method\": \"Genetic knockout (ΔPP2Acα, ΔB'/PR61), okadaic acid chemical inhibition, metabolomic analysis, plaque assay, in vivo virulence assay\",\n      \"journal\": \"Microbiology spectrum\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — two independent genetic knockouts with matching phenotypes, metabolomics for mechanism, multiple orthogonal methods in a single study\",\n      \"pmids\": [\"37199633\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"RHΔku80\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"PTPA (phosphotyrosyl phosphatase activator) forms a ternary complex with PP2A A and C subunits in T. gondii, validated by reciprocal pull-down assays; depletion of PTPA impairs tachyzoite proliferation, invasion, gliding motility, and stress-induced bradyzoite cyst formation, and causes amylopectin accumulation and lipid droplet proliferation. The PP2A inhibitor LB-100 phenocopies PTPA depletion.\",\n      \"method\": \"Reciprocal pull-down assays (ternary complex validation), conditional depletion of PTPA, LB-100 chemical inhibition, phenotypic assays (proliferation, invasion, gliding, cyst formation)\",\n      \"journal\": \"Cells\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal pull-down confirms complex, chemical phenocopy with LB-100, single lab with multiple orthogonal methods\",\n      \"pmids\": [\"40498010\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"The PP2A-2 holoenzyme, composed of regulatory subunit TgPR48 (PP2A-B2), catalytic subunit PP2A-C2, and scaffolding subunit PP2A-A2, is essential for daughter cell separation and cytokinesis during T. gondii tachyzoite division; disruption of any single component severely impairs daughter cell emergence. Phosphoproteomic analysis after PP2A-C2 depletion identified DCS1 and DCS2 as potential effectors whose depletion disrupts TgPR48 localization.\",\n      \"method\": \"Conditional depletion of individual holoenzyme subunits, phosphoproteomics following PP2A-C2 depletion, phosphomimetic/non-phosphorylatable mutants of DCS1/DCS2, TgPR48 overexpression rescue experiments\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 2 / Strong — disruption of each of three subunits individually recapitulates cytokinesis phenotype, phosphoproteomics identifies downstream effectors, rescue experiments with multiple orthogonal approaches\",\n      \"pmids\": [\"40901993\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"The T. gondii PP2A-A (scaffold/structural) subunit assembles with catalytic (PP2A-C) and regulatory (PP2A-B) subunits into distinct holoenzyme complexes that regulate parasite starch/amylopectin metabolism via dephosphorylation of CDPK2-S679, control tachyzoite cytokinesis and daughter cell emergence (PP2A-2 holoenzyme with PP2A-A2/PP2A-C2/TgPR48), and participate in a PTPA-regulated axis governing tachyzoite proliferation and bradyzoite differentiation; exported parasite effectors (GRA16, GRA18) also exploit host PP2A complexes containing the A subunit to reprogram host gene expression and immune signaling.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PP2A-A is the scaffold/structural subunit of Toxoplasma gondii PP2A phosphatase holoenzymes, assembling with a catalytic subunit (PP2A-C) and a variable regulatory subunit (PP2A-B) to form distinct complexes that govern parasite carbohydrate metabolism and division [#2, #3, #5]. Through a PP2A-A/PP2A-C/PP2A-B holoenzyme, the phosphatase controls amylopectin/starch metabolism by dephosphorylating CDPK2 at S679, and disruption of any single subunit — including PP2A-A — causes starch over-accumulation and blocks tachyzoite-to-bradyzoite differentiation [#2]; a PP2Ac\\u03b1-B'/PR61 holoenzyme is likewise required for amylopectin turnover, glucose metabolism, ATP production, tachyzoite proliferation, and virulence [#3]. A distinct scaffold paralog, PP2A-A2, partners with PP2A-C2 and the regulatory subunit TgPR48 (PP2A-B2) to form the PP2A-2 holoenzyme essential for daughter cell separation and cytokinesis, acting through candidate effectors DCS1 and DCS2 [#5]. Assembly and activity of the PP2A A/C core are promoted by PTPA, which forms a ternary complex with the A and C subunits and is needed for proliferation, invasion, gliding, and cyst formation [#4]. Exported parasite effectors also co-opt host PP2A-A-containing holoenzymes: GRA16 binds the host A-scaffold holoenzyme to drive its nuclear translocation and modulate p53 and cell-cycle gene expression [#0], while GRA18 engages a host GSK3/PP2A-B56 complex to up-regulate \\u03b2-catenin and anti-inflammatory gene expression in macrophages [#1].\",\n  \"teleology\": [\n    {\n      \"year\": 2013,\n      \"claim\": \"Establishing that a secreted parasite effector could hijack host PP2A revealed the A-scaffold-containing holoenzyme as a target for Toxoplasma manipulation of host transcription.\",\n      \"evidence\": \"GRA16 co-purification with host PP2A and HAUSP, nuclear translocation assay, and knockout virulence assessment\",\n      \"pmids\": [\n        \"23601110\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Which specific PP2A-A/B/C holoenzyme composition GRA16 engages is not resolved\",\n        \"Direct dephosphorylation substrates in the host nucleus not identified\"\n      ],\n      \"attribution\": []\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Identifying GRA18 in a host GSK3/PP2A-B56 complex extended host-PP2A hijacking to immune reprogramming via \\u03b2-catenin.\",\n      \"evidence\": \"Reciprocal Co-IP and mass spectrometry interactome with downstream gene expression analysis in macrophages\",\n      \"pmids\": [\n        \"30320549\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Whether GRA18 alters PP2A catalytic activity versus targeting is unclear\",\n        \"Direct phosphatase substrates within the complex not defined\"\n      ],\n      \"attribution\": []\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Defining the parasite's own PP2A-A/B/C holoenzyme and a phospho-substrate answered what intrinsic process PP2A controls, linking it to starch metabolism and stage differentiation.\",\n      \"evidence\": \"Genetic disruption of individual subunits, phosphoproteomics identifying CDPK2-S679, and starch accumulation assays\",\n      \"pmids\": [\n        \"36476594\"\n      ],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct dephosphorylation of CDPK2-S679 by the holoenzyme not reconstituted in vitro\",\n        \"Additional substrates beyond CDPK2 not enumerated\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Toxoplasma gondii\",\n          \"strain\": \"\"\n        }\n      ]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Assigning a specific regulatory subunit (B'/PR61) to the metabolic holoenzyme connected PP2A-A scaffold function to glucose metabolism, ATP output, and tachyzoite proliferation.\",\n      \"evidence\": \"Independent \\u0394PP2Ac\\u03b1 and \\u0394B'/PR61 knockouts, okadaic acid inhibition, metabolomics, plaque and in vivo virulence assays\",\n      \"pmids\": [\n        \"37199633\"\n      ],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"The precise scaffold contribution of PP2A-A independent of catalytic loss not isolated\",\n        \"Metabolic substrates downstream of polysaccharide accumulation not mapped\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Toxoplasma gondii\",\n          \"strain\": \"RH\\u0394ku80\"\n        }\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Identifying PTPA as a ternary partner of the A and C subunits established an upstream regulator that activates PP2A to sustain proliferation, invasion, motility, and differentiation.\",\n      \"evidence\": \"Reciprocal pull-down assays, conditional PTPA depletion, LB-100 chemical phenocopy, and phenotypic assays\",\n      \"pmids\": [\n        \"40498010\"\n      ],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Mechanism by which PTPA activates the A/C complex not resolved\",\n        \"Whether PTPA acts on all PP2A holoenzymes or a subset unclear\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Toxoplasma gondii\",\n          \"strain\": \"\"\n        }\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Resolving a distinct PP2A-2 holoenzyme (PP2A-A2/PP2A-C2/TgPR48) showed the scaffold operates in a separate complex dedicated to cytokinesis and daughter cell emergence.\",\n      \"evidence\": \"Conditional depletion of each subunit, phosphoproteomics after PP2A-C2 depletion identifying DCS1/DCS2, phosphomutants, and TgPR48 rescue\",\n      \"pmids\": [\n        \"40901993\"\n      ],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Direct dephosphorylation of DCS1/DCS2 by PP2A-2 not demonstrated in vitro\",\n        \"How PP2A-A2 selectivity is achieved versus the metabolic scaffold is unknown\"\n      ],\n      \"attribution\": [\n        {\n          \"species\": \"Toxoplasma gondii\",\n          \"strain\": \"\"\n        }\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How the PP2A-A scaffold selects among distinct regulatory subunits to partition metabolic, differentiation, and cytokinesis functions remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Structural basis of scaffold-regulatory subunit pairing not determined\",\n        \"Whether PP2A-A and PP2A-A2 are functionally interchangeable is untested\",\n        \"Full substrate repertoire across holoenzymes incomplete\"\n      ],\n      \"attribution\": []\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\n        \"term_id\": \"GO:0008601\",\n        \"supporting_discovery_ids\": [\n          2,\n          3,\n          5\n        ],\n        \"attribution\": [\n          {\n            \"species\": \"Toxoplasma gondii\",\n            \"strain\": \"\"\n          }\n        ]\n      },\n      {\n        \"term_id\": \"GO:0004722\",\n        \"supporting_discovery_ids\": [\n          2,\n          5\n        ],\n        \"attribution\": [\n          {\n            \"species\": \"Toxoplasma gondii\",\n            \"strain\": \"\"\n          }\n        ]\n      }\n    ],\n    \"localization\": [\n      {\n        \"term_id\": \"GO:0005634\",\n        \"supporting_discovery_ids\": [\n          0\n        ],\n        \"attribution\": []\n      },\n      {\n        \"term_id\": \"GO:0005737\",\n        \"supporting_discovery_ids\": [\n          1\n        ],\n        \"attribution\": []\n      }\n    ],\n    \"pathway\": [\n      {\n        \"term_id\": \"GO:0005982\",\n        \"supporting_discovery_ids\": [\n          2,\n          3\n        ],\n        \"attribution\": [\n          {\n            \"species\": \"Toxoplasma gondii\",\n            \"strain\": \"\"\n          }\n        ]\n      },\n      {\n        \"term_id\": \"GO:0000281\",\n        \"supporting_discovery_ids\": [\n          5\n        ],\n        \"attribution\": [\n          {\n            \"species\": \"Toxoplasma gondii\",\n            \"strain\": \"\"\n          }\n        ]\n      },\n      {\n        \"term_id\": \"GO:0030154\",\n        \"supporting_discovery_ids\": [\n          2,\n          4\n        ],\n        \"attribution\": [\n          {\n            \"species\": \"Toxoplasma gondii\",\n            \"strain\": \"\"\n          }\n        ]\n      }\n    ],\n    \"complexes\": [\n      \"PP2A holoenzyme (PP2A-A scaffold / PP2A-C catalytic / PP2A-B regulatory)\",\n      \"PP2Ac\\u03b1-B'/PR61 holoenzyme\",\n      \"PP2A-2 holoenzyme (PP2A-A2 / PP2A-C2 / TgPR48/PP2A-B2)\",\n      \"PTPA-PP2A A/C ternary complex\",\n      \"Host GRA16-PP2A-HAUSP complex\",\n      \"Host GRA18-GSK3/PP2A-B56 complex\"\n    ],\n    \"partners\": [\n      \"PP2A-C (catalytic subunit)\",\n      \"PP2A-B (regulatory subunit)\",\n      \"B'/PR61\",\n      \"TgPR48 (PP2A-B2)\",\n      \"PP2A-C2\",\n      \"PP2A-A2\",\n      \"PTPA\",\n      \"CDPK2 (substrate, S679)\",\n      \"GRA16 (host PP2A engagement)\",\n      \"GRA18 (host PP2A-B56 engagement)\",\n      \"HAUSP\",\n      \"DCS1\",\n      \"DCS2\"\n    ],\n    \"other_free_text\": [\n      \"PP2A-A serves as the shared scaffold across at least two distinct parasite holoenzymes with separable roles in amylopectin metabolism/differentiation and in cytokinesis.\",\n      \"Chemical inhibition with okadaic acid and LB-100 phenocopies genetic subunit loss, corroborating PP2A activity requirement.\",\n      \"Toxoplasma effectors GRA16 and GRA18 exploit host PP2A-A-containing holoenzymes to reprogram host p53/cell-cycle and \\u03b2-catenin/anti-inflammatory signaling.\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_315670","name":"PP2A-A","product":"serine/threonine-protein phosphatase PP2A subunit A","uniprot_acc":"S8EX93","chromosome":"TGME49_chrXI","start_pos":4884862},{"strain":"GT1","gene_id":"TGGT1_315670","name":null,"product":"HEAT repeat-containing protein","uniprot_acc":null,"chromosome":"TGGT1_chrXI","start_pos":4828533},{"strain":"RH88","gene_id":"TGRH88_054510","name":null,"product":"HEAT repeat-containing protein","uniprot_acc":null,"chromosome":"CM023092","start_pos":4950484},{"strain":"VEG","gene_id":"TGVEG_315670","name":null,"product":"HEAT repeat-containing protein","uniprot_acc":"A0A125YW66","chromosome":"TGVEG_chrXI","start_pos":4907190}]}