{"gene":"TG_313380","gene_symbol":"ILP1","run_date":"2026-09-11T11:01:00","timeline":{"discoveries":[{"year":2019,"finding":"ILP1's C-terminal coiled-coil domain directly binds to alveolins IMC3 and IMC6, as well as IMC27, in the Toxoplasma IMC cytoskeletal network. Distinct regions of the C-terminal coiled-coil domain of ILP1 crosslink to IMC3 and IMC6; the IMC3 C-terminal domain and the IMC6 N-terminal domain are necessary for binding to ILP1.","method":"Photoactivatable unnatural amino acid (UAA) crosslinking system in live parasites, mapping binding interfaces between ILP1 and IMC3, IMC6, and IMC27","journal":"PLoS biology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — site-specific in vivo crosslinking with deletion/domain mapping in a single rigorous study; multiple orthogonal approaches including domain-specific crosslinking and binding interface mapping","pmids":["31584943"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"finding":"The alveolin domain of IMC6 contains multiple binding interfaces with IMC3 and ILP1, providing direct evidence that protein-protein interactions within the alveolin domain mediate filament formation in the subpellicular network (SPN). ILP1 is thus a binding partner of IMC6 within the alveolin domain.","method":"Unnatural amino acid photoreactive crosslinking applied to the IMC6 alveolin domain; deletion analyses for localization and function","journal":"PLoS biology","confidence":"High","confidence_rationale":"Tier 1 / Moderate — in-cell crosslinking with domain mutagenesis, single rigorous study with multiple orthogonal methods confirming ILP1–IMC6 interaction at the alveolin domain level","pmids":["39264987"],"is_preprint":false,"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2023,"finding":"ILP1 is identified as a binding partner of IMC6 within the alveolin domain of the Toxoplasma subpellicular network, consistent with a role in maintaining SPN architecture and parasite shape.","method":"Unnatural amino acid photoreactive crosslinking of the IMC6 alveolin domain","journal":"bioRxiv","confidence":"Medium","confidence_rationale":"Tier 1 / Weak — in-cell crosslinking in single preprint study; largely superseded by the peer-reviewed version (PMID:39264987)","pmids":["37609316"],"is_preprint":true,"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"current_model":"ILP1 (also called IAP1) is an inner membrane complex (IMC) cytoskeletal protein in Toxoplasma gondii whose C-terminal coiled-coil domain directly interacts with alveolin proteins IMC3 and IMC6 (as well as IMC27) to form the interconnected subpellicular network, and whose IMC-associated function additionally includes serving as the key determinant for restricting myosin C localization to the parasite's basal polar ring within the MyoC-glideosome."},"narrative":{"mechanistic_narrative":"ILP1 is a cytoskeletal protein of the inner membrane complex (IMC) in Toxoplasma gondii that contributes to the architecture of the subpellicular network (SPN) underlying the parasite pellicle [PMID:31584943]. Its C-terminal coiled-coil domain directly binds the alveolin proteins IMC3 and IMC6 (and IMC27), with distinct regions of the coiled-coil crosslinking to IMC3 versus IMC6, and the IMC3 C-terminal domain and IMC6 N-terminal domain being required for binding [PMID:31584943]; ILP1 engages IMC6 through multiple binding interfaces within its alveolin domain, part of the network of alveolin-domain interactions that mediate SPN filament formation [PMID:39264987]. Beyond these interactions, no further mechanistic detail on ILP1 has been characterized in the available corpus.","teleology":[{"year":2019,"claim":"It was unknown which SPN components ILP1 physically contacts; site-specific in vivo crosslinking established that ILP1's C-terminal coiled-coil domain directly binds alveolins IMC3, IMC6, and IMC27 through distinct interfaces, placing ILP1 in the interconnected cytoskeletal network.","evidence":"Photoactivatable unnatural amino acid crosslinking in live parasites with domain deletion/mapping in Toxoplasma gondii","pmids":["31584943"],"confidence":"High","gaps":["Functional consequence of disrupting individual ILP1-alveolin contacts not tested","Stoichiometry and higher-order assembly of the network not determined"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]},{"year":2024,"claim":"How alveolin-domain interactions drive SPN filament formation was unresolved; mapping the IMC6 alveolin domain showed it contains multiple binding interfaces for both IMC3 and ILP1, providing direct evidence that these interactions mediate filament assembly in the network.","evidence":"In-cell unnatural amino acid photoreactive crosslinking of the IMC6 alveolin domain with deletion analyses in Toxoplasma gondii (peer-reviewed; preprint version 2023, PMID:37609316)","pmids":["39264987","37609316"],"confidence":"High","gaps":["Precise contribution of ILP1 versus IMC3 to filament rigidity/architecture not separated","Structural model of the assembled alveolin filament not established"],"attribution":[{"species":"Toxoplasma gondii","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Subpellicular network / alveolin cytoskeletal network (with IMC3, IMC6, IMC27)"],"partners":["IMC3","IMC6","IMC27"],"other_free_text":["ILP1 (also known as IAP1); C-terminal coiled-coil domain mediates alveolin binding.","Distinct regions of ILP1's C-terminal coiled-coil crosslink to IMC3 versus IMC6; IMC3 C-terminal domain and IMC6 N-terminal/alveolin domain are required for ILP1 binding.","Acts as the key determinant restricting MyoC to the parasite basal polar ring/posterior pole."]},"strain_conflicts":[]},"prefetch_data":{},"corpus_meta":[{"pmid":"25691595","id":"PMC_25691595","title":"Novel components of the Toxoplasma inner membrane complex revealed by BioID.","date":"2015","source":"mBio","url":"https://pubmed.ncbi.nlm.nih.gov/25691595","citation_count":148,"is_preprint":false},{"pmid":"19561073","id":"PMC_19561073","title":"A novel family of Apicomplexan glideosome-associated proteins with an inner membrane-anchoring role.","date":"2009","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/19561073","citation_count":102,"is_preprint":false},{"pmid":"10704375","id":"PMC_10704375","title":"Microtubules, but not actin filaments, drive daughter cell budding and cell division in Toxoplasma gondii.","date":"2000","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/10704375","citation_count":95,"is_preprint":false},{"pmid":"24612102","id":"PMC_24612102","title":"The inner membrane complex through development of Toxoplasma gondii and Plasmodium.","date":"2014","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/24612102","citation_count":78,"is_preprint":false},{"pmid":"24928899","id":"PMC_24928899","title":"Dynamics of the Toxoplasma gondii inner membrane complex.","date":"2014","source":"Journal of cell science","url":"https://pubmed.ncbi.nlm.nih.gov/24928899","citation_count":54,"is_preprint":false},{"pmid":"23027733","id":"PMC_23027733","title":"Targeted proteomic dissection of Toxoplasma cytoskeleton sub-compartments using MORN1.","date":"2012","source":"Cytoskeleton (Hoboken, N.J.)","url":"https://pubmed.ncbi.nlm.nih.gov/23027733","citation_count":44,"is_preprint":false},{"pmid":"31584943","id":"PMC_31584943","title":"A photoactivatable crosslinking system reveals protein interactions in the Toxoplasma gondii inner membrane complex.","date":"2019","source":"PLoS biology","url":"https://pubmed.ncbi.nlm.nih.gov/31584943","citation_count":33,"is_preprint":false},{"pmid":"27548677","id":"PMC_27548677","title":"Virus-Like Nanoparticle Vaccine Confers Protection against Toxoplasma gondii.","date":"2016","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/27548677","citation_count":33,"is_preprint":false},{"pmid":"21829561","id":"PMC_21829561","title":"Subcellular antigen location influences T-cell activation during acute infection with Toxoplasma gondii.","date":"2011","source":"PloS one","url":"https://pubmed.ncbi.nlm.nih.gov/21829561","citation_count":33,"is_preprint":false},{"pmid":"25088010","id":"PMC_25088010","title":"Identification and characterization of Toxoplasma SIP, a conserved apicomplexan cytoskeleton protein involved in maintaining the shape, motility and virulence of the parasite.","date":"2014","source":"Cellular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/25088010","citation_count":28,"is_preprint":false},{"pmid":"39264987","id":"PMC_39264987","title":"Alveolin proteins in the Toxoplasma inner membrane complex form a highly interconnected structure that maintains parasite shape and replication.","date":"2024","source":"PLoS biology","url":"https://pubmed.ncbi.nlm.nih.gov/39264987","citation_count":10,"is_preprint":false},{"pmid":"37609316","id":"PMC_37609316","title":"The Toxoplasma subpellicular network is highly interconnected and defines parasite shape for efficient motility and replication.","date":"2023","source":"bioRxiv : the preprint server for biology","url":"https://pubmed.ncbi.nlm.nih.gov/37609316","citation_count":3,"is_preprint":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":22158,"output_tokens":1193,"usd":0.042184,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6155,"output_tokens":2207,"usd":0.042975,"stage2_stop_reason":"end_turn"},"total_usd":0.003102,"stage1_batch_id":"msgbatch_01WgHz6kceqm573AGLyz57at","stage2_batch_id":"msgbatch_01LK4wDYj5zYquahv7gi9893","note":"batch pricing = 50% of standard","skipped":true,"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\": 2019,\n      \"finding\": \"ILP1's C-terminal coiled-coil domain directly binds to alveolins IMC3 and IMC6, as well as IMC27, in the Toxoplasma IMC cytoskeletal network. Distinct regions of the C-terminal coiled-coil domain of ILP1 crosslink to IMC3 and IMC6; the IMC3 C-terminal domain and the IMC6 N-terminal domain are necessary for binding to ILP1.\",\n      \"method\": \"Photoactivatable unnatural amino acid (UAA) crosslinking system in live parasites, mapping binding interfaces between ILP1 and IMC3, IMC6, and IMC27\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — site-specific in vivo crosslinking with deletion/domain mapping in a single rigorous study; multiple orthogonal approaches including domain-specific crosslinking and binding interface mapping\",\n      \"pmids\": [\"31584943\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"finding\": \"The alveolin domain of IMC6 contains multiple binding interfaces with IMC3 and ILP1, providing direct evidence that protein-protein interactions within the alveolin domain mediate filament formation in the subpellicular network (SPN). ILP1 is thus a binding partner of IMC6 within the alveolin domain.\",\n      \"method\": \"Unnatural amino acid photoreactive crosslinking applied to the IMC6 alveolin domain; deletion analyses for localization and function\",\n      \"journal\": \"PLoS biology\",\n      \"confidence\": \"High\",\n      \"confidence_rationale\": \"Tier 1 / Moderate — in-cell crosslinking with domain mutagenesis, single rigorous study with multiple orthogonal methods confirming ILP1–IMC6 interaction at the alveolin domain level\",\n      \"pmids\": [\"39264987\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"ILP1 is identified as a binding partner of IMC6 within the alveolin domain of the Toxoplasma subpellicular network, consistent with a role in maintaining SPN architecture and parasite shape.\",\n      \"method\": \"Unnatural amino acid photoreactive crosslinking of the IMC6 alveolin domain\",\n      \"journal\": \"bioRxiv\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 1 / Weak — in-cell crosslinking in single preprint study; largely superseded by the peer-reviewed version (PMID:39264987)\",\n      \"pmids\": [\"37609316\"],\n      \"is_preprint\": true,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2014,\n      \"finding\": \"IMC-associated protein 1 (IAP1, also referred to as ILP1 in context of the MyoC-glideosome) acts as the key determinant for the restricted localization of myosin C (MyoC) to the posterior pole/basal polar ring of Toxoplasma gondii, forming a component of the MyoC-glideosome complex.\",\n      \"method\": \"Deletion of specific glideosome components (IAP1/ILP1), co-immunoprecipitation, and complementation assays; conditional knockouts with localization readout by fluorescence microscopy\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal interaction and KO phenotype in single lab, two orthogonal methods (co-IP and localization/functional KO)\",\n      \"pmids\": [\"25393004\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"ILP1 (also called IAP1) is an inner membrane complex (IMC) cytoskeletal protein in Toxoplasma gondii whose C-terminal coiled-coil domain directly interacts with alveolin proteins IMC3 and IMC6 (as well as IMC27) to form the interconnected subpellicular network, and whose IMC-associated function additionally includes serving as the key determinant for restricting myosin C localization to the parasite's basal polar ring within the MyoC-glideosome.\"\n}\n```","stage2_raw":"```json\n{\n  \"mechanistic_narrative\": \"ILP1 (also called IAP1) is a cytoskeletal protein of the inner membrane complex (IMC) in Toxoplasma gondii that contributes to the architecture of the subpellicular network (SPN) underlying the parasite pellicle [#0]. Its C-terminal coiled-coil domain directly binds the alveolin proteins IMC3 and IMC6 (and IMC27), with distinct regions of the coiled-coil crosslinking to IMC3 versus IMC6, and the IMC3 C-terminal domain and IMC6 N-terminal domain being required for binding [#0]; ILP1 engages IMC6 through multiple binding interfaces within its alveolin domain, part of the network of alveolin-domain interactions that mediate SPN filament formation [#1]. In addition to its structural role in the SPN, ILP1 serves as the key determinant restricting myosin C (MyoC) localization to the posterior/basal polar ring of the parasite as a component of the MyoC-glideosome [#3]. Beyond these interactions, no further mechanistic detail on ILP1 has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2014,\n      \"claim\": \"Before this work it was unclear how the basal-specific myosin MyoC is confined to the posterior pole; identifying IAP1/ILP1 as a MyoC-glideosome component established ILP1 as the positional determinant restricting MyoC to the basal polar ring.\",\n      \"evidence\": \"Conditional knockouts with fluorescence localization, co-immunoprecipitation, and complementation in Toxoplasma gondii\",\n      \"pmids\": [\"25393004\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Molecular mechanism by which ILP1 anchors MyoC to the basal polar ring is not defined\",\n        \"Relationship between ILP1's glideosome role and its SPN/alveolin interactions not resolved\",\n        \"Single-lab characterization\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2019,\n      \"claim\": \"It was unknown which SPN components ILP1 physically contacts; site-specific in vivo crosslinking established that ILP1's C-terminal coiled-coil domain directly binds alveolins IMC3, IMC6, and IMC27 through distinct interfaces, placing ILP1 in the interconnected cytoskeletal network.\",\n      \"evidence\": \"Photoactivatable unnatural amino acid crosslinking in live parasites with domain deletion/mapping in Toxoplasma gondii\",\n      \"pmids\": [\"31584943\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Functional consequence of disrupting individual ILP1-alveolin contacts not tested\",\n        \"Stoichiometry and higher-order assembly of the network not determined\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2024,\n      \"claim\": \"How alveolin-domain interactions drive SPN filament formation was unresolved; mapping the IMC6 alveolin domain showed it contains multiple binding interfaces for both IMC3 and ILP1, providing direct evidence that these interactions mediate filament assembly in the network.\",\n      \"evidence\": \"In-cell unnatural amino acid photoreactive crosslinking of the IMC6 alveolin domain with deletion analyses in Toxoplasma gondii (peer-reviewed; preprint version 2023, PMID:37609316)\",\n      \"pmids\": [\"39264987\", \"37609316\"],\n      \"confidence\": \"High\",\n      \"gaps\": [\n        \"Precise contribution of ILP1 versus IMC3 to filament rigidity/architecture not separated\",\n        \"Structural model of the assembled alveolin filament not established\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How ILP1's dual roles — as an SPN alveolin-network component and as the basal MyoC-glideosome positional determinant — are integrated within a single protein remains unknown.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No unified mechanistic model links ILP1's SPN scaffolding and MyoC-restriction functions\",\n        \"Regulation of ILP1 localization and assembly not characterized\"\n      ],\n      \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0005198\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0005515\", \"supporting_discovery_ids\": [0, 1, 3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0033113\", \"supporting_discovery_ids\": [0, 1], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]},\n      {\"term_id\": \"GO:0071944\", \"supporting_discovery_ids\": [3], \"attribution\": [{\"species\": \"Toxoplasma gondii\", \"strain\": \"\"}]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [\n      \"Subpellicular network / alveolin cytoskeletal network (with IMC3, IMC6, IMC27)\",\n      \"MyoC-glideosome\"\n    ],\n    \"partners\": [\n      \"IMC3\",\n      \"IMC6\",\n      \"IMC27\",\n      \"MyoC (myosin C)\"\n    ],\n    \"other_free_text\": [\n      \"ILP1 (also known as IAP1); C-terminal coiled-coil domain mediates alveolin binding.\",\n      \"Distinct regions of ILP1's C-terminal coiled-coil crosslink to IMC3 versus IMC6; IMC3 C-terminal domain and IMC6 N-terminal/alveolin domain are required for ILP1 binding.\",\n      \"Acts as the key determinant restricting MyoC to the parasite basal polar ring/posterior pole.\"\n    ]\n  },\n  \"strain_conflicts\": []\n}\n```","audit_flag":null,"strains":[{"strain":"ME49","gene_id":"TGME49_313380","name":"ILP1","product":"IMC localizing protein ILP1","uniprot_acc":"A0A125YKB4","chromosome":"TGME49_chrXI","start_pos":3328839},{"strain":"GT1","gene_id":"TGGT1_313380","name":null,"product":"hypothetical protein","uniprot_acc":null,"chromosome":"TGGT1_chrXI","start_pos":3292372},{"strain":"RH88","gene_id":"TGRH88_052520","name":null,"product":"unspecified product","uniprot_acc":null,"chromosome":"CM023092","start_pos":3377185},{"strain":"VEG","gene_id":"TGVEG_313380","name":null,"product":"hypothetical protein","uniprot_acc":"B9PIK4","chromosome":"TGVEG_chrXI","start_pos":3342055}]}