{"gene":"PF3D7_0802100","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2021,"finding":"AP2-LT (PF3D7_0802100) was identified as an integral subunit of a divergent PfGCN5-containing complex in Plasmodium falciparum. The complex also contains two plant homeodomain (PHD) proteins (PfPHD1 and PfPHD2). Deletion of the bromodomain in PfGCN5 or the PHD domain in PfPHD1 caused down-regulation of merozoite invasion genes, many of which contain the AP2-LT binding motif, suggesting targeted recruitment of the PfGCN5 complex to invasion genes by AP2-LT together with AP2-I and BDP1.","method":"Co-immunoprecipitation/mass spectrometry to identify complex members; domain deletion mutants (ΔBrd, ΔPHD) with transcriptomic profiling; binding motif analysis","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal complex identification by MS in single lab, two orthogonal methods (Co-IP/MS + transcriptomics with motif analysis), but full mechanistic dissection of AP2-LT's specific contribution not independently replicated","pmids":["34403450"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"finding":"CUT&Tag-seq chromatin mapping confirmed that AP2-LT (PF3D7_0802100) co-localizes with PfGCN5 and H3K9ac at gene promoters in P. falciparum asexual blood stages, validating AP2-LT as an integral component of the PfGCN5 complex and indicating it recruits the complex to target promoters.","method":"CUT&Tag-seq chromatin localization mapping; co-localization analysis with PfGCN5 and H3K9ac signals","journal":"Cells","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct chromatin localization by CUT&Tag-seq, single lab, consistent with prior Co-IP/MS data from a separate study","pmids":["40558503"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2016,"finding":"AP2-LT (PF3D7_0802100) was found to be lysine-acetylated as part of a proteome-wide characterization of the P. falciparum acetylome. Acetylation of ApiAP2 DNA-binding domains was shown experimentally to ablate DNA-binding propensity, suggesting that acetylation of AP2-LT may regulate its DNA-binding activity.","method":"Mass spectrometry-based acetylome profiling; in vitro DNA-binding assay with acetylated AP2 domain","journal":"Scientific reports","confidence":"Low","confidence_rationale":"Tier 3 / Weak — acetylation of AP2-LT detected in a pan-proteome screen; the functional ablation of DNA binding was demonstrated for ApiAP2 domains generally, not specifically for AP2-LT","pmids":["26813983"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"AP2-LT (PF3D7_0802100) is an integral subunit of a divergent PfGCN5 histone acetyltransferase complex in Plasmodium falciparum that also contains PfPHD1 and PfPHD2; it co-localizes with PfGCN5 and the active histone mark H3K9ac at gene promoters and its binding motif is enriched at merozoite invasion genes co-regulated by AP2-I and BDP1, suggesting AP2-LT recruits the PfGCN5 complex to drive transcription of erythrocyte invasion genes."},"narrative":{"mechanistic_narrative":"AP2-LT (PF3D7_0802100) is an AP2-domain transcription factor of Plasmodium falciparum that functions as an integral subunit of a divergent PfGCN5 histone acetyltransferase complex, which additionally contains the plant homeodomain proteins PfPHD1 and PfPHD2 [PMID:34403450]. Chromatin mapping by CUT&Tag-seq places AP2-LT together with PfGCN5 and the active mark H3K9ac at gene promoters in asexual blood stages, consistent with a role in recruiting the acetyltransferase complex to its target promoters [PMID:40558503]. Its binding motif is enriched at merozoite invasion genes that are down-regulated when the PfGCN5 bromodomain or the PfPHD1 PHD domain is deleted, indicating that AP2-LT, alongside AP2-I and BDP1, directs the complex to activate erythrocyte invasion genes [PMID:34403450]. Beyond its role within the PfGCN5 complex and its promoter co-localization, no further mechanistic detail specific to AP2-LT has been characterized in the available corpus.","teleology":[{"year":2016,"claim":"Whether AP2-LT is subject to post-translational regulation was addressed by proteome-wide acetylome profiling, which detected AP2-LT as a lysine-acetylated protein and established acetylation as a candidate switch on ApiAP2 DNA binding.","evidence":"Mass spectrometry acetylome profiling plus in vitro DNA-binding assays on acetylated AP2 domains","pmids":["26813983"],"confidence":"Low","gaps":["The DNA-binding ablation was shown for ApiAP2 domains generally, not demonstrated specifically for the AP2-LT domain","No in vivo consequence of AP2-LT acetylation established","Acetylation site occupancy and the enzyme responsible not defined for AP2-LT"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2021,"claim":"The functional context of AP2-LT was resolved by defining it as an integral subunit of a divergent PfGCN5 acetyltransferase complex and linking that complex to activation of merozoite invasion genes bearing the AP2-LT motif.","evidence":"Co-IP/mass spectrometry complex identification with ΔBrd/ΔPHD domain-deletion mutants, transcriptomics, and binding-motif analysis in P. falciparum","pmids":["34403450"],"confidence":"Medium","gaps":["The specific contribution of AP2-LT versus AP2-I and BDP1 to recruitment was not dissected by AP2-LT loss-of-function","Direct binding of AP2-LT to invasion-gene promoters not demonstrated in this study","Complex identification from a single lab, not independently replicated"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2025,"claim":"Whether AP2-LT physically occupies promoters with the PfGCN5 complex on chromatin was tested by direct in vivo mapping, showing co-localization with PfGCN5 and H3K9ac at promoters and supporting a promoter-recruitment role.","evidence":"CUT&Tag-seq chromatin localization mapping and co-localization analysis in P. falciparum asexual blood stages","pmids":["40558503"],"confidence":"Medium","gaps":["Causal test of whether AP2-LT is required for PfGCN5 or H3K9ac deposition at promoters not performed","Genome-wide direct DNA sequence recognition by AP2-LT not resolved","Single-lab dataset"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"It remains unknown whether AP2-LT is functionally required for PfGCN5 complex recruitment and invasion-gene activation, and how its acetylation modulates DNA binding in vivo.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No AP2-LT-specific knockout or knockdown phenotype reported","Direct in vitro DNA-binding specificity of the AP2-LT domain not characterized","Mechanism connecting acetylation of AP2-LT to its chromatin occupancy unestablished"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Divergent PfGCN5 histone acetyltransferase complex (with PfGCN5, PfPHD1, PfPHD2)"],"partners":["PFGCN5","PFPHD1","PFPHD2","AP2-I (CO-REGULATOR AT INVASION GENES)","BDP1 (CO-REGULATOR AT INVASION GENES)"],"other_free_text":["Binding motif enriched at merozoite erythrocyte-invasion genes co-regulated with AP2-I and BDP1 [#0]","Co-localizes with the active histone mark H3K9ac at promoters in asexual blood stages [#1]","Detected as lysine-acetylated in the P. falciparum acetylome; acetylation of ApiAP2 domains generally ablates DNA binding [#2]"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"24572369","id":"PMC_24572369","title":"A transcriptional switch underlies commitment to sexual development in malaria 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The complex also contains two plant homeodomain (PHD) proteins (PfPHD1 and PfPHD2). Deletion of the bromodomain in PfGCN5 or the PHD domain in PfPHD1 caused down-regulation of merozoite invasion genes, many of which contain the AP2-LT binding motif, suggesting targeted recruitment of the PfGCN5 complex to invasion genes by AP2-LT together with AP2-I and BDP1.\",\n      \"method\": \"Co-immunoprecipitation/mass spectrometry to identify complex members; domain deletion mutants (ΔBrd, ΔPHD) with transcriptomic profiling; binding motif analysis\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal complex identification by MS in single lab, two orthogonal methods (Co-IP/MS + transcriptomics with motif analysis), but full mechanistic dissection of AP2-LT's specific contribution not independently replicated\",\n      \"pmids\": [\"34403450\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2025,\n      \"finding\": \"CUT&Tag-seq chromatin mapping confirmed that AP2-LT (PF3D7_0802100) co-localizes with PfGCN5 and H3K9ac at gene promoters in P. falciparum asexual blood stages, validating AP2-LT as an integral component of the PfGCN5 complex and indicating it recruits the complex to target promoters.\",\n      \"method\": \"CUT&Tag-seq chromatin localization mapping; co-localization analysis with PfGCN5 and H3K9ac signals\",\n      \"journal\": \"Cells\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct chromatin localization by CUT&Tag-seq, single lab, consistent with prior Co-IP/MS data from a separate study\",\n      \"pmids\": [\"40558503\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2016,\n      \"finding\": \"AP2-LT (PF3D7_0802100) was found to be lysine-acetylated as part of a proteome-wide characterization of the P. falciparum acetylome. Acetylation of ApiAP2 DNA-binding domains was shown experimentally to ablate DNA-binding propensity, suggesting that acetylation of AP2-LT may regulate its DNA-binding activity.\",\n      \"method\": \"Mass spectrometry-based acetylome profiling; in vitro DNA-binding assay with acetylated AP2 domain\",\n      \"journal\": \"Scientific reports\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — acetylation of AP2-LT detected in a pan-proteome screen; the functional ablation of DNA binding was demonstrated for ApiAP2 domains generally, not specifically for AP2-LT\",\n      \"pmids\": [\"26813983\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"AP2-LT (PF3D7_0802100) is an integral subunit of a divergent PfGCN5 histone acetyltransferase complex in Plasmodium falciparum that also contains PfPHD1 and PfPHD2; it co-localizes with PfGCN5 and the active histone mark H3K9ac at gene promoters and its binding motif is enriched at merozoite invasion genes co-regulated by AP2-I and BDP1, suggesting AP2-LT recruits the PfGCN5 complex to drive transcription of erythrocyte invasion genes.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"AP2-LT (PF3D7_0802100) is an AP2-domain transcription factor of Plasmodium falciparum that functions as an integral subunit of a divergent PfGCN5 histone acetyltransferase complex, which additionally contains the plant homeodomain proteins PfPHD1 and PfPHD2 [#0]. Chromatin mapping by CUT&Tag-seq places AP2-LT together with PfGCN5 and the active mark H3K9ac at gene promoters in asexual blood stages, consistent with a role in recruiting the acetyltransferase complex to its target promoters [#1]. Its binding motif is enriched at merozoite invasion genes that are down-regulated when the PfGCN5 bromodomain or the PfPHD1 PHD domain is deleted, indicating that AP2-LT, alongside AP2-I and BDP1, directs the complex to activate erythrocyte invasion genes [#0]. Beyond its role within the PfGCN5 complex and its promoter co-localization, no further mechanistic detail specific to AP2-LT has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2016,\n      \"claim\": \"Whether AP2-LT is subject to post-translational regulation was addressed by proteome-wide acetylome profiling, which detected AP2-LT as a lysine-acetylated protein and established acetylation as a candidate switch on ApiAP2 DNA binding.\",\n      \"evidence\": \"Mass spectrometry acetylome profiling plus in vitro DNA-binding assays on acetylated AP2 domains\",\n      \"pmids\": [\"26813983\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"The DNA-binding ablation was shown for ApiAP2 domains generally, not demonstrated specifically for the AP2-LT domain\",\n        \"No in vivo consequence of AP2-LT acetylation established\",\n        \"Acetylation site occupancy and the enzyme responsible not defined for AP2-LT\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2021,\n      \"claim\": \"The functional context of AP2-LT was resolved by defining it as an integral subunit of a divergent PfGCN5 acetyltransferase complex and linking that complex to activation of merozoite invasion genes bearing the AP2-LT motif.\",\n      \"evidence\": \"Co-IP/mass spectrometry complex identification with ΔBrd/ΔPHD domain-deletion mutants, transcriptomics, and binding-motif analysis in P. falciparum\",\n      \"pmids\": [\"34403450\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"The specific contribution of AP2-LT versus AP2-I and BDP1 to recruitment was not dissected by AP2-LT loss-of-function\",\n        \"Direct binding of AP2-LT to invasion-gene promoters not demonstrated in this study\",\n        \"Complex identification from a single lab, not independently replicated\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2025,\n      \"claim\": \"Whether AP2-LT physically occupies promoters with the PfGCN5 complex on chromatin was tested by direct in vivo mapping, showing co-localization with PfGCN5 and H3K9ac at promoters and supporting a promoter-recruitment role.\",\n      \"evidence\": \"CUT&Tag-seq chromatin localization mapping and co-localization analysis in P. falciparum asexual blood stages\",\n      \"pmids\": [\"40558503\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Causal test of whether AP2-LT is required for PfGCN5 or H3K9ac deposition at promoters not performed\",\n        \"Genome-wide direct DNA sequence recognition by AP2-LT not resolved\",\n        \"Single-lab dataset\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"It remains unknown whether AP2-LT is functionally required for PfGCN5 complex recruitment and invasion-gene activation, and how its acetylation modulates DNA binding in vivo.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No AP2-LT-specific knockout or knockdown phenotype reported\",\n        \"Direct in vitro DNA-binding specificity of the AP2-LT domain not characterized\",\n        \"Mechanism connecting acetylation of AP2-LT to its chromatin occupancy unestablished\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003700\", \"supporting_discovery_ids\": [0, 1]},\n      {\"term_id\": \"GO:0003677\", \"supporting_discovery_ids\": [2]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005634\", \"supporting_discovery_ids\": [1]},\n      {\"term_id\": \"GO:0000785\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0045944\", \"supporting_discovery_ids\": [0, 1]}\n    ],\n    \"complexes\": [\n      \"Divergent PfGCN5 histone acetyltransferase complex (with PfGCN5, PfPHD1, PfPHD2)\"\n    ],\n    \"partners\": [\n      \"PfGCN5\",\n      \"PfPHD1\",\n      \"PfPHD2\",\n      \"AP2-I (co-regulator at invasion genes)\",\n      \"BDP1 (co-regulator at invasion genes)\"\n    ],\n    \"other_free_text\": [\n      \"Binding motif enriched at merozoite erythrocyte-invasion genes co-regulated with AP2-I and BDP1 [#0]\",\n      \"Co-localizes with the active histone mark H3K9ac at promoters in asexual blood stages [#1]\",\n      \"Detected as lysine-acetylated in the P. falciparum acetylome; acetylation of ApiAP2 domains generally ablates DNA binding [#2]\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0802100","name":null,"product":"AP2 domain transcription factor AP2-LT","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1228100","name":null,"product":"AP2 domain transcription factor AP2-LT, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0116800","name":null,"product":"AP2 domain transcription factor AP2-LT, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"AP2-LT","evaluation":null}