{"gene":"TG_306030","gene_symbol":"GST2","run_date":"2026-09-08T15:15:13","timeline":{"discoveries":[{"year":2021,"finding":"TgGST2 is a membrane protein that localizes to the Golgi-endosomal system in T. gondii, colocalizing with vesicle transport factors synaptobrevin, putative sortilin (VPS10), Rab5, and Rab6, as determined by immunofluorescence and colocalization experiments.","method":"Indirect immunofluorescence assay (IFA), colocalization microscopy","journal":"FASEB Journal","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct localization experiments with colocalization to multiple vesicle transport markers, single lab, single paper","pmids":["33543805"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"Loss of TgGST2 causes mislocalization and decreased expression of several secretory proteins (microneme, rhoptry, and dense granule proteins), and disrupts the distribution of Rab5 and Rab6 to discrete puncta, establishing TgGST2 as required for accurate vesicle trafficking of secretory proteins through the Golgi-endosomal system.","method":"Genetic knockout (loss-of-function), IFA, Western blot","journal":"FASEB Journal","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — clean knockout with defined cellular phenotype (secretory protein mislocalization, Rab distribution disruption), single lab","pmids":["33543805"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"Loss of TgGST2 significantly reduces parasite invasion capacity and virulence in mice, linking its vesicle trafficking function to the parasite lytic cycle.","method":"Invasion assay, mouse virulence model (loss-of-function)","journal":"FASEB Journal","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — genetic knockout with defined phenotypic readouts (invasion and in vivo virulence), single lab","pmids":["33543805"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"finding":"TgGST2 localization to the Golgi-endosomal system is dependent on post-Golgi trafficking, as shown by perturbation of its distribution upon disruption of post-Golgi transport.","method":"Subcellular localization analysis with vesicle transport perturbation","journal":"FASEB Journal","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, localization dependency inferred without detailed mechanistic dissection described in abstract","pmids":["33543805"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"TgGST2 possesses glutathione S-transferase enzymatic activity that is inhibited by exogenous estradiol (E2) and progesterone (P4) in a concentration-dependent manner, and TgGST2 binds to E2 and P4 as determined by molecular docking and enzyme activity assays.","method":"GST enzyme activity assay, molecular docking (trRosetta, Autodock Vina)","journal":"Parasites & Vectors","confidence":"Low","confidence_rationale":"Tier 3 / Weak — enzyme activity assay supports binding and inhibition, but molecular docking is computational; single lab, single paper","pmids":["36510329"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"finding":"Progesterone (P4) treatment causes TgGST2 to relocalize from the Golgi and vesicles to hollow circles, leading to abnormal localization of sortilin (VPS10) and microneme proteins MIC2 and M2AP, and ultimately impairing parasite motility; estradiol (E2) had no significant effect on TgGST2 localization.","method":"IFA, indirect immunofluorescence, drug treatment assay","journal":"Parasites & Vectors","confidence":"Low","confidence_rationale":"Tier 3 / Weak — localization change with functional consequence observed by IFA, single lab, single paper, largely pharmacological/indirect approach","pmids":["36510329"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"TgGST2 is a Golgi-endosomal membrane protein in Toxoplasma gondii with glutathione S-transferase enzymatic activity that physically associates with vesicle transport factors (synaptobrevin, VPS10/sortilin, Rab5, Rab6) and is required for accurate post-Golgi vesicle trafficking of secretory proteins to micronemes, rhoptries, and dense granules, thereby supporting parasite invasion and virulence; its localization and function can be disrupted by progesterone treatment, and its enzymatic activity is inhibited by steroid hormones in a concentration-dependent manner."},"narrative":{"mechanistic_narrative":"TgGST2 is a Golgi-endosomal membrane protein of Toxoplasma gondii that couples glutathione S-transferase activity to the machinery of post-Golgi secretory trafficking [PMID:33543805]. It colocalizes with vesicle transport factors synaptobrevin, the putative sortilin VPS10, Rab5, and Rab6, and its own residence in the Golgi-endosomal system depends on intact post-Golgi transport [PMID:33543805]. Loss of TgGST2 mislocalizes and reduces microneme, rhoptry, and dense granule proteins and disperses Rab5/Rab6 puncta, establishing it as required for accurate vesicle trafficking of secretory cargo; this trafficking role is functionally linked to the lytic cycle, as knockout parasites show reduced invasion and attenuated virulence in mice [PMID:33543805]. TgGST2 also carries glutathione S-transferase enzymatic activity, and progesterone disrupts its Golgi localization with downstream mislocalization of VPS10 and micronemal MIC2/M2AP and impaired motility [PMID:36510329].","teleology":[{"year":2021,"claim":"Establishing where TgGST2 resides addressed whether a parasite glutathione S-transferase is linked to secretory trafficking rather than cytosolic detoxification, placing it in the Golgi-endosomal vesicle transport system.","evidence":"Immunofluorescence and colocalization with synaptobrevin, VPS10/sortilin, Rab5, and Rab6 in T. gondii","pmids":["33543805"],"confidence":"Medium","gaps":["Colocalization does not demonstrate direct physical binding to these transport factors","Single lab, single study","Membrane topology and orientation not defined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"Genetic ablation tested whether TgGST2 is functionally required for trafficking, showing it is needed for correct delivery of secretory proteins and for maintaining Rab5/Rab6 organization.","evidence":"Knockout with IFA and Western blot showing mislocalization/reduced expression of microneme, rhoptry, and dense granule proteins and disrupted Rab distribution","pmids":["33543805"],"confidence":"Medium","gaps":["Molecular mechanism by which a GST supports vesicle trafficking is unresolved","Whether the trafficking defect requires enzymatic activity is untested"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"Phenotyping the knockout connected the trafficking defect to the parasite lytic cycle, showing TgGST2 loss reduces invasion and virulence.","evidence":"Invasion assay and mouse virulence model of TgGST2 knockout","pmids":["33543805"],"confidence":"Medium","gaps":["Does not separate invasion defect from upstream secretory protein mislocalization","Contribution of each affected organelle class to virulence not dissected"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2021,"claim":"Perturbing post-Golgi transport tested whether TgGST2 localization is a passive consequence of the trafficking system it supports, showing its distribution depends on intact post-Golgi transport.","evidence":"Subcellular localization analysis under vesicle transport perturbation","pmids":["33543805"],"confidence":"Low","gaps":["Localization dependency inferred without detailed mechanistic dissection","Single lab"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Characterizing the enzyme addressed whether TgGST2 is an active glutathione S-transferase and whether steroid hormones engage it, showing GST activity that is inhibited by estradiol and progesterone.","evidence":"GST enzyme activity assay with E2/P4 inhibition plus molecular docking (computational)","pmids":["36510329"],"confidence":"Low","gaps":["Steroid binding rests on computational docking, awaiting direct biophysical binding measurement","Endogenous physiological substrate not identified","Single lab, single study"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2022,"claim":"Hormone treatment tested whether steroid engagement has cellular consequences, showing progesterone relocalizes TgGST2, mislocalizes VPS10 and MIC2/M2AP, and impairs motility, while estradiol does not affect localization.","evidence":"IFA under progesterone and estradiol drug treatment in T. gondii","pmids":["36510329"],"confidence":"Low","gaps":["Pharmacological/indirect approach does not prove the effect is mediated through TgGST2 itself","Discordance between E2 enzyme inhibition and lack of localization effect unexplained"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":null,"claim":"How TgGST2 mechanistically links glutathione S-transferase chemistry to vesicle sorting, and whether its enzymatic activity is required for trafficking, remains unresolved.","evidence":"","pmids":[],"confidence":"Low","gaps":["No physiological GST substrate identified","Direct physical interaction with Rab/SNARE/sortilin machinery not demonstrated","No structural model of the trafficking-active protein"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["SYNAPTOBREVIN (COLOCALIZATION)","VPS10/PUTATIVE SORTILIN (COLOCALIZATION)","RAB5 (COLOCALIZATION)","RAB6 (COLOCALIZATION)"],"other_free_text":["Loss of TgGST2 mislocalizes and reduces microneme, rhoptry, and dense granule proteins and disperses Rab5/Rab6 puncta [#1].","TgGST2 knockout reduces parasite invasion and virulence in mice [#2].","GST activity inhibited by estradiol and progesterone in a concentration-dependent manner; steroid binding supported by molecular docking [#4].","Progesterone (not estradiol) relocalizes TgGST2 and mislocalizes VPS10, MIC2, and M2AP, impairing motility [#5]."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"33543805","id":"PMC_33543805","title":"Toxoplasma gondii glutathione S-transferase 2 plays an important role in partial secretory protein transport.","date":"2021","source":"FASEB journal : official publication of the Federation of American Societies for Experimental Biology","url":"https://pubmed.ncbi.nlm.nih.gov/33543805","citation_count":15,"is_preprint":false},{"pmid":"36510329","id":"PMC_36510329","title":"Effects of different drugs and hormone treatment on Toxoplasma gondii glutathione S-transferase 2.","date":"2022","source":"Parasites & vectors","url":"https://pubmed.ncbi.nlm.nih.gov/36510329","citation_count":3,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3607,"output_tokens":1507,"usd":0.016713,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6605,"output_tokens":2883,"usd":0.05255,"stage2_stop_reason":"end_turn"},"total_usd":0.069263,"stage1_batch_id":"msgbatch_01S6GjoYQm8LTPUsdhASdqag","stage2_batch_id":"msgbatch_01VX63RTMdBJqsG6gQMqoCjz","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2021,\n      \"finding\": \"TgGST2 is a membrane protein that localizes to the Golgi-endosomal system in T. gondii, colocalizing with vesicle transport factors synaptobrevin, putative sortilin (VPS10), Rab5, and Rab6, as determined by immunofluorescence and colocalization experiments.\",\n      \"method\": \"Indirect immunofluorescence assay (IFA), colocalization microscopy\",\n      \"journal\": \"FASEB Journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct localization experiments with colocalization to multiple vesicle transport markers, single lab, single paper\",\n      \"pmids\": [\"33543805\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Loss of TgGST2 causes mislocalization and decreased expression of several secretory proteins (microneme, rhoptry, and dense granule proteins), and disrupts the distribution of Rab5 and Rab6 to discrete puncta, establishing TgGST2 as required for accurate vesicle trafficking of secretory proteins through the Golgi-endosomal system.\",\n      \"method\": \"Genetic knockout (loss-of-function), IFA, Western blot\",\n      \"journal\": \"FASEB Journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — clean knockout with defined cellular phenotype (secretory protein mislocalization, Rab distribution disruption), single lab\",\n      \"pmids\": [\"33543805\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"Loss of TgGST2 significantly reduces parasite invasion capacity and virulence in mice, linking its vesicle trafficking function to the parasite lytic cycle.\",\n      \"method\": \"Invasion assay, mouse virulence model (loss-of-function)\",\n      \"journal\": \"FASEB Journal\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — genetic knockout with defined phenotypic readouts (invasion and in vivo virulence), single lab\",\n      \"pmids\": [\"33543805\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"finding\": \"TgGST2 localization to the Golgi-endosomal system is dependent on post-Golgi trafficking, as shown by perturbation of its distribution upon disruption of post-Golgi transport.\",\n      \"method\": \"Subcellular localization analysis with vesicle transport perturbation\",\n      \"journal\": \"FASEB Journal\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, localization dependency inferred without detailed mechanistic dissection described in abstract\",\n      \"pmids\": [\"33543805\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"TgGST2 possesses glutathione S-transferase enzymatic activity that is inhibited by exogenous estradiol (E2) and progesterone (P4) in a concentration-dependent manner, and TgGST2 binds to E2 and P4 as determined by molecular docking and enzyme activity assays.\",\n      \"method\": \"GST enzyme activity assay, molecular docking (trRosetta, Autodock Vina)\",\n      \"journal\": \"Parasites & Vectors\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — enzyme activity assay supports binding and inhibition, but molecular docking is computational; single lab, single paper\",\n      \"pmids\": [\"36510329\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"finding\": \"Progesterone (P4) treatment causes TgGST2 to relocalize from the Golgi and vesicles to hollow circles, leading to abnormal localization of sortilin (VPS10) and microneme proteins MIC2 and M2AP, and ultimately impairing parasite motility; estradiol (E2) had no significant effect on TgGST2 localization.\",\n      \"method\": \"IFA, indirect immunofluorescence, drug treatment assay\",\n      \"journal\": \"Parasites & Vectors\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — localization change with functional consequence observed by IFA, single lab, single paper, largely pharmacological/indirect approach\",\n      \"pmids\": [\"36510329\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"TgGST2 is a Golgi-endosomal membrane protein in Toxoplasma gondii with glutathione S-transferase enzymatic activity that physically associates with vesicle transport factors (synaptobrevin, VPS10/sortilin, Rab5, Rab6) and is required for accurate post-Golgi vesicle trafficking of secretory proteins to micronemes, rhoptries, and dense granules, thereby supporting parasite invasion and virulence; its localization and function can be disrupted by progesterone treatment, and its enzymatic activity is inhibited by steroid hormones in a concentration-dependent manner.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"TgGST2 is a Golgi-endosomal membrane protein of Toxoplasma gondii that couples glutathione S-transferase activity to the machinery of post-Golgi secretory trafficking [#0, #1]. It colocalizes with vesicle transport factors synaptobrevin, the putative sortilin VPS10, Rab5, and Rab6, and its own residence in the Golgi-endosomal system depends on intact post-Golgi transport [#0, #3]. Loss of TgGST2 mislocalizes and reduces microneme, rhoptry, and dense granule proteins and disperses Rab5/Rab6 puncta, establishing it as required for accurate vesicle trafficking of secretory cargo; this trafficking role is functionally linked to the lytic cycle, as knockout parasites show reduced invasion and attenuated virulence in mice [#1, #2]. TgGST2 also carries glutathione S-transferase enzymatic activity, and progesterone disrupts its Golgi localization with downstream mislocalization of VPS10 and micronemal MIC2/M2AP and impaired motility [#4, #5].\",\n  \"teleology\": [\n    {\n      \"year\": 2021,\n      \"claim\": \"Establishing where TgGST2 resides addressed whether a parasite glutathione S-transferase is linked to secretory trafficking rather than cytosolic detoxification, placing it in the Golgi-endosomal vesicle transport system.\",\n      \"evidence\": \"Immunofluorescence and colocalization with synaptobrevin, VPS10/sortilin, Rab5, and Rab6 in T. gondii\",\n      \"pmids\": [\"33543805\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Colocalization does not demonstrate direct physical binding to these transport factors\", \"Single lab, single study\", \"Membrane topology and orientation not defined\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Genetic ablation tested whether TgGST2 is functionally required for trafficking, showing it is needed for correct delivery of secretory proteins and for maintaining Rab5/Rab6 organization.\",\n      \"evidence\": \"Knockout with IFA and Western blot showing mislocalization/reduced expression of microneme, rhoptry, and dense granule proteins and disrupted Rab distribution\",\n      \"pmids\": [\"33543805\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Molecular mechanism by which a GST supports vesicle trafficking is unresolved\", \"Whether the trafficking defect requires enzymatic activity is untested\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Phenotyping the knockout connected the trafficking defect to the parasite lytic cycle, showing TgGST2 loss reduces invasion and virulence.\",\n      \"evidence\": \"Invasion assay and mouse virulence model of TgGST2 knockout\",\n      \"pmids\": [\"33543805\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Does not separate invasion defect from upstream secretory protein mislocalization\", \"Contribution of each affected organelle class to virulence not dissected\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"Perturbing post-Golgi transport tested whether TgGST2 localization is a passive consequence of the trafficking system it supports, showing its distribution depends on intact post-Golgi transport.\",\n      \"evidence\": \"Subcellular localization analysis under vesicle transport perturbation\",\n      \"pmids\": [\"33543805\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Localization dependency inferred without detailed mechanistic dissection\", \"Single lab\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Characterizing the enzyme addressed whether TgGST2 is an active glutathione S-transferase and whether steroid hormones engage it, showing GST activity that is inhibited by estradiol and progesterone.\",\n      \"evidence\": \"GST enzyme activity assay with E2/P4 inhibition plus molecular docking (computational)\",\n      \"pmids\": [\"36510329\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Steroid binding rests on computational docking, awaiting direct biophysical binding measurement\", \"Endogenous physiological substrate not identified\", \"Single lab, single study\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2022,\n      \"claim\": \"Hormone treatment tested whether steroid engagement has cellular consequences, showing progesterone relocalizes TgGST2, mislocalizes VPS10 and MIC2/M2AP, and impairs motility, while estradiol does not affect localization.\",\n      \"evidence\": \"IFA under progesterone and estradiol drug treatment in T. gondii\",\n      \"pmids\": [\"36510329\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Pharmacological/indirect approach does not prove the effect is mediated through TgGST2 itself\", \"Discordance between E2 enzyme inhibition and lack of localization effect unexplained\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How TgGST2 mechanistically links glutathione S-transferase chemistry to vesicle sorting, and whether its enzymatic activity is required for trafficking, remains unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No physiological GST substrate identified\", \"Direct physical interaction with Rab/SNARE/sortilin machinery not demonstrated\", \"No structural model of the trafficking-active protein\"],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0004364\", \"supporting_discovery_ids\": [4], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005794\", \"supporting_discovery_ids\": [0, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0010008\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0016020\", \"supporting_discovery_ids\": [0], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006888\", \"supporting_discovery_ids\": [1, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0016192\", \"supporting_discovery_ids\": [1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"complexes\": [],\n    \"partners\": [\n      \"synaptobrevin (colocalization)\",\n      \"VPS10/putative sortilin (colocalization)\",\n      \"Rab5 (colocalization)\",\n      \"Rab6 (colocalization)\"\n    ],\n    \"other_free_text\": [\n      \"Loss of TgGST2 mislocalizes and reduces microneme, rhoptry, and dense granule proteins and disperses Rab5/Rab6 puncta [#1].\",\n      \"TgGST2 knockout reduces parasite invasion and virulence in mice [#2].\",\n      \"GST activity inhibited by estradiol and progesterone in a concentration-dependent manner; steroid binding supported by molecular docking [#4].\",\n      \"Progesterone (not estradiol) relocalizes TgGST2 and mislocalizes VPS10, MIC2, and M2AP, impairing motility [#5].\"\n    ]\n  },\n  \"strain_conflicts\": []\n}","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_306030","name":"GST2","product":"glutathione S-transferase 2","uniprot_acc":"A0A125YIG5","chromosome":"TGME49_chrIX","start_pos":5756382},{"strain":"GT1","gene_id":"TGGT1_306030","name":null,"product":"glutathione s-transferase, n-terminal domain containing protein","uniprot_acc":null,"chromosome":"TGGT1_chrIX","start_pos":5538577},{"strain":"RH88","gene_id":"TGRH88_017560","name":null,"product":"glutathione s-transferase, n-terminal domain containing protein","uniprot_acc":null,"chromosome":"CM023090","start_pos":5880180},{"strain":"VEG","gene_id":"TGVEG_306030","name":null,"product":"glutathione s-transferase, n-terminal domain containing protein","uniprot_acc":"B9PZA9","chromosome":"TGVEG_chrIX","start_pos":5795557}]}