{"gene":"PF3D7_1224300","run_date":"2026-09-08T14:19:06","timeline":{"discoveries":[{"year":2009,"finding":"PfPABP1 (PF3D7_1224300) binds poly(A) RNA specifically, as demonstrated by in vitro binding assays, and interacts with the translation initiation factor PfeIF4G, establishing its role in the eIF4F translation initiation complex in P. falciparum.","method":"Biochemical binding assay (poly(A) binding), co-immunoprecipitation/interaction assay with eIF4G","journal":"Parasitology international","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — direct binding assay for poly(A) specificity and protein–protein interaction with eIF4G demonstrated, single lab with two orthogonal methods","pmids":["19751846"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"PfPABP1 (PF3D7_1224300) is a component of the DOZI/CITH messenger ribonucleoprotein (mRNP) complex purified from P. berghei female gametocytes. This mRNP contains translationally silent transcripts, integrates eIF4E and poly(A)-binding protein, but excludes P body RNA degradation factors and translation-initiation-promoting eIF4G, indicating PABP1 resides in a translationally repressive mRNP.","method":"Affinity purification coupled with mass spectrometric analysis of the DOZI/CITH mRNP from gametocytes","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — mass spectrometry-based complex identification with functional context (translational repression), single study but highly systematic","pmids":["20169188"],"is_preprint":false,"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2018,"finding":"PABP1 (PF3D7_1224300) is a component of stress granules in P. falciparum female gametocytes and interacts with the seven-helix protein 7-Helix-1, as well as with CITH and DOZI, as shown by co-immunoprecipitation, placing PABP1 in a stress granule ribonucleoprotein complex that regulates translational repression during gametocytogenesis.","method":"Co-immunoprecipitation (interaction with 7-Helix-1, CITH, DOZI); localization by immunofluorescence assay","journal":"PLoS pathogens","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal co-IP demonstrating complex membership, supported by localization data, single lab","pmids":["30133543"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"finding":"The P. yoelii ortholog of PABP1 (PyPABP1, ortholog of PF3D7_1224300) is a cytoplasmic PABP during blood stages, binds poly(A) sequences specifically and strongly in vitro, forms homopolymeric chains in vitro even after exhaustive RNase treatment, and is additionally localized on the surface of salivary gland sporozoites where it is deposited in gliding trails.","method":"Multiple independent poly(A) binding assays; indirect immunofluorescence assay (IFA) for localization; in vitro RNase treatment followed by chain formation assay","journal":"mSphere","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — multiple orthogonal binding assays and direct localization experiments, single lab, performed in P. yoelii ortholog","pmids":["29359180"],"is_preprint":false,"attribution":[{"species":"Plasmodium yoelii","strain":""}]},{"year":2023,"finding":"PABP1 (PF3D7_1224300) interacts with the CCCH zinc finger protein MD3 in P. falciparum male gametocytes, as identified by BioID proximity labeling and confirmed by co-immunoprecipitation, placing PABP1 within a post-transcriptional regulatory complex that also includes ALBA3, eIF4G, PUF1, NOT1, and CITH, and is required for male gametocytogenesis.","method":"BioID proximity labeling; co-immunoprecipitation","journal":"Molecular microbiology","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — two orthogonal methods (BioID + Co-IP) in a single lab establishing complex membership","pmids":["38148574"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PF3D7_1224300 (PABP1) is a cytoplasmic poly(A)-binding protein that specifically binds poly(A) RNA, interacts with the translation initiation factor eIF4G as part of the eIF4F complex, and is also a component of translationally repressive mRNP/stress granule complexes (containing DOZI, CITH, 7-Helix-1, and MD3) in female and male gametocytes that store silenced transcripts required for mosquito transmission; in P. yoelii, the ortholog additionally localizes to the surface of sporozoites and is deposited during gliding."},"narrative":{"mechanistic_narrative":"PF3D7_1224300 (PABP1) is a cytoplasmic poly(A)-binding protein that couples poly(A) RNA recognition to both translation initiation and translational repression across the Plasmodium life cycle [PMID:19751846, PMID:20169188]. In P. falciparum asexual/general contexts it binds poly(A) RNA specifically in vitro and interacts with the translation initiation factor eIF4G, consistent with a role in the eIF4F initiation complex [PMID:19751846]. During sexual development, however, PABP1 is redirected into translationally repressive messenger ribonucleoprotein and stress granule complexes: in P. berghei female gametocytes it is a component of the DOZI/CITH mRNP that stores silenced transcripts and integrates eIF4E and poly(A)-binding protein while excluding eIF4G and P-body degradation factors [PMID:20169188], and in P. falciparum female gametocytes it associates with 7-Helix-1, CITH, and DOZI in stress granules regulating translational repression during gametocytogenesis [PMID:30133543]. In P. falciparum male gametocytes PABP1 sits within an MD3-containing post-transcriptional regulatory complex (also including ALBA3, eIF4G, PUF1, NOT1, and CITH) required for male gametocytogenesis [PMID:38148574]. The P. yoelii ortholog binds poly(A) strongly, self-associates into RNase-resistant homopolymeric chains, and, beyond its cytoplasmic blood-stage role, localizes to the sporozoite surface and is deposited in gliding trails [PMID:29359180].","teleology":[{"year":2009,"claim":"Establishing whether PABP1 is a bona fide poly(A)-binding protein wired into translation initiation, this work showed specific poly(A) binding and a direct interaction with eIF4G, placing it in the eIF4F initiation complex.","evidence":"In vitro poly(A) binding assay plus co-immunoprecipitation/interaction with eIF4G in P. falciparum","pmids":["19751846"],"confidence":"Medium","gaps":["No structural mapping of the RNA-binding or eIF4G-interacting regions","Functional consequence of the eIF4G interaction on translation not tested in vivo"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"Addressing whether PABP1 also participates in transcript storage rather than only active translation, purification of the female-gametocyte DOZI/CITH mRNP placed PABP1 in a translationally repressive complex that contained eIF4E but excluded eIF4G and degradation factors.","evidence":"Affinity purification and mass spectrometry of the DOZI/CITH mRNP from P. berghei female gametocytes","pmids":["20169188"],"confidence":"Medium","gaps":["Does not establish whether PABP1 is required for repression or merely co-purifies","Mechanism switching PABP1 between eIF4G-bound (active) and eIF4E-bound repressive contexts unresolved"],"attribution":[{"species":"Plasmodium berghei","strain":""}]},{"year":2018,"claim":"To define PABP1's partners in the repressive machinery, reciprocal co-IP placed it in female-gametocyte stress granules with 7-Helix-1, CITH, and DOZI, linking it to translational repression during gametocytogenesis.","evidence":"Co-immunoprecipitation with 7-Helix-1/CITH/DOZI and immunofluorescence localization in P. falciparum female gametocytes","pmids":["30133543"],"confidence":"Medium","gaps":["Direct versus bridged nature of each interaction not resolved","Effect of PABP1 loss on stress granule assembly not tested"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2018,"claim":"Testing whether PABP1 has functions beyond RNA regulation, the P. yoelii ortholog was shown to bind poly(A) strongly, self-assemble into RNase-resistant chains, and unexpectedly localize to the sporozoite surface and gliding trails.","evidence":"Multiple poly(A) binding assays, RNase-resistant chain-formation assay, and IFA in P. yoelii","pmids":["29359180"],"confidence":"Medium","gaps":["Functional role of surface/gliding-trail deposition unknown","Whether P. falciparum PABP1 shares the sporozoite surface localization not tested","Physiological relevance of in vitro homopolymeric chains unclear"],"attribution":[{"species":"Plasmodium yoelii","strain":""}]},{"year":2023,"claim":"Extending PABP1's repressive role to the male lineage, proximity labeling and co-IP placed it in an MD3-anchored complex (ALBA3, eIF4G, PUF1, NOT1, CITH) required for male gametocytogenesis.","evidence":"BioID proximity labeling and co-immunoprecipitation in P. falciparum male gametocytes","pmids":["38148574"],"confidence":"Medium","gaps":["Individual requirement of PABP1 (versus MD3) for the phenotype not isolated","Target transcripts regulated by this complex not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":null,"claim":"How PABP1 is molecularly switched between the active eIF4G-associated initiation complex and the repressive eIF4E/DOZI/CITH mRNP and stress granules, and what its poly(A)-independent sporozoite-surface role is, remain unresolved.","evidence":"","pmids":[],"confidence":"Medium","gaps":["No direct loss-of-function of PABP1 itself linking it to any life-cycle phenotype","No structural model of PABP1 or its complexes","Regulatory signal governing complex partitioning unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["eIF4F translation initiation complex (with eIF4G)","DOZI/CITH translationally repressive mRNP (with eIF4E, DOZI, CITH)","Female gametocyte stress granule complex (with 7-Helix-1, CITH, DOZI)","MD3-containing male-gametocyte post-transcriptional complex (with ALBA3, eIF4G, PUF1, NOT1, CITH)"],"partners":["EIF4G","EIF4E","DOZI","CITH","7-HELIX-1","MD3","ALBA3","PUF1","NOT1"],"other_free_text":["Binds poly(A) RNA specifically in vitro (P. falciparum and P. yoelii ortholog)","P. yoelii ortholog forms RNase-resistant homopolymeric chains in vitro","P. yoelii ortholog deposited in sporozoite gliding trails; function of this localization uncharacterized","MD3 complex required for male gametocytogenesis; PABP1's individual requirement not isolated"]}},"prefetch_data":{},"corpus_meta":[{"pmid":"20169188","id":"PMC_20169188","title":"Universal features of post-transcriptional gene regulation are critical for Plasmodium zygote development.","date":"2010","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/20169188","citation_count":216,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["curated_ref"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"30133543","id":"PMC_30133543","title":"A seven-helix protein constitutes stress granules crucial for regulating translation during human-to-mosquito transmission of Plasmodium falciparum.","date":"2018","source":"PLoS pathogens","url":"https://pubmed.ncbi.nlm.nih.gov/30133543","citation_count":22,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PABP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19641745","id":"PMC_19641745","title":"Identification and bioinformatics characterization of translation initiation complex eIF4F components and poly(A)-binding protein from Plasmodium falciparum.","date":"2009","source":"Communicative & integrative biology","url":"https://pubmed.ncbi.nlm.nih.gov/19641745","citation_count":19,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PABP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"29359180","id":"PMC_29359180","title":"Nuclear, Cytosolic, and Surface-Localized Poly(A)-Binding Proteins of Plasmodium yoelii.","date":"2018","source":"mSphere","url":"https://pubmed.ncbi.nlm.nih.gov/29359180","citation_count":17,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PABP","PyPABP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"19751846","id":"PMC_19751846","title":"Isolation and functional characterization of eIF4F components and poly(A)-binding protein from Plasmodium falciparum.","date":"2009","source":"Parasitology international","url":"https://pubmed.ncbi.nlm.nih.gov/19751846","citation_count":16,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PABP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"21331256","id":"PMC_21331256","title":"PfeIF4E and PfeIF4A colocalize and their double-stranded RNA inhibits Plasmodium falciparum proliferation.","date":"2010","source":"Communicative & integrative biology","url":"https://pubmed.ncbi.nlm.nih.gov/21331256","citation_count":13,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PABP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"38148574","id":"PMC_38148574","title":"The Plasmodium falciparum CCCH zinc finger protein MD3 regulates male gametocytogenesis through its interaction with RNA-binding proteins.","date":"2023","source":"Molecular microbiology","url":"https://pubmed.ncbi.nlm.nih.gov/38148574","citation_count":8,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PABP1"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"42615421","id":"PMC_42615421","title":"Poly(A)-binding proteins in trypanosomatids and Plasmodium.","date":"2026","source":"Journal of biosciences","url":"https://pubmed.ncbi.nlm.nih.gov/42615421","citation_count":0,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["PABP"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":6837,"output_tokens":1556,"usd":0.021926,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":6467,"output_tokens":3081,"usd":0.05468,"stage2_stop_reason":"end_turn"},"total_usd":0.076606,"stage1_batch_id":"msgbatch_011BPjN2BL33F8cJXD1r7V7T","stage2_batch_id":"msgbatch_01Qwg6vP7qxkpL6Gsc7tajsb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2009,\n      \"finding\": \"PfPABP1 (PF3D7_1224300) binds poly(A) RNA specifically, as demonstrated by in vitro binding assays, and interacts with the translation initiation factor PfeIF4G, establishing its role in the eIF4F translation initiation complex in P. falciparum.\",\n      \"method\": \"Biochemical binding assay (poly(A) binding), co-immunoprecipitation/interaction assay with eIF4G\",\n      \"journal\": \"Parasitology international\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — direct binding assay for poly(A) specificity and protein–protein interaction with eIF4G demonstrated, single lab with two orthogonal methods\",\n      \"pmids\": [\"19751846\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"PfPABP1 (PF3D7_1224300) is a component of the DOZI/CITH messenger ribonucleoprotein (mRNP) complex purified from P. berghei female gametocytes. This mRNP contains translationally silent transcripts, integrates eIF4E and poly(A)-binding protein, but excludes P body RNA degradation factors and translation-initiation-promoting eIF4G, indicating PABP1 resides in a translationally repressive mRNP.\",\n      \"method\": \"Affinity purification coupled with mass spectrometric analysis of the DOZI/CITH mRNP from gametocytes\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — mass spectrometry-based complex identification with functional context (translational repression), single study but highly systematic\",\n      \"pmids\": [\"20169188\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"PABP1 (PF3D7_1224300) is a component of stress granules in P. falciparum female gametocytes and interacts with the seven-helix protein 7-Helix-1, as well as with CITH and DOZI, as shown by co-immunoprecipitation, placing PABP1 in a stress granule ribonucleoprotein complex that regulates translational repression during gametocytogenesis.\",\n      \"method\": \"Co-immunoprecipitation (interaction with 7-Helix-1, CITH, DOZI); localization by immunofluorescence assay\",\n      \"journal\": \"PLoS pathogens\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal co-IP demonstrating complex membership, supported by localization data, single lab\",\n      \"pmids\": [\"30133543\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"finding\": \"The P. yoelii ortholog of PABP1 (PyPABP1, ortholog of PF3D7_1224300) is a cytoplasmic PABP during blood stages, binds poly(A) sequences specifically and strongly in vitro, forms homopolymeric chains in vitro even after exhaustive RNase treatment, and is additionally localized on the surface of salivary gland sporozoites where it is deposited in gliding trails.\",\n      \"method\": \"Multiple independent poly(A) binding assays; indirect immunofluorescence assay (IFA) for localization; in vitro RNase treatment followed by chain formation assay\",\n      \"journal\": \"mSphere\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — multiple orthogonal binding assays and direct localization experiments, single lab, performed in P. yoelii ortholog\",\n      \"pmids\": [\"29359180\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"finding\": \"PABP1 (PF3D7_1224300) interacts with the CCCH zinc finger protein MD3 in P. falciparum male gametocytes, as identified by BioID proximity labeling and confirmed by co-immunoprecipitation, placing PABP1 within a post-transcriptional regulatory complex that also includes ALBA3, eIF4G, PUF1, NOT1, and CITH, and is required for male gametocytogenesis.\",\n      \"method\": \"BioID proximity labeling; co-immunoprecipitation\",\n      \"journal\": \"Molecular microbiology\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — two orthogonal methods (BioID + Co-IP) in a single lab establishing complex membership\",\n      \"pmids\": [\"38148574\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PF3D7_1224300 (PABP1) is a cytoplasmic poly(A)-binding protein that specifically binds poly(A) RNA, interacts with the translation initiation factor eIF4G as part of the eIF4F complex, and is also a component of translationally repressive mRNP/stress granule complexes (containing DOZI, CITH, 7-Helix-1, and MD3) in female and male gametocytes that store silenced transcripts required for mosquito transmission; in P. yoelii, the ortholog additionally localizes to the surface of sporozoites and is deposited during gliding.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PF3D7_1224300 (PABP1) is a cytoplasmic poly(A)-binding protein that couples poly(A) RNA recognition to both translation initiation and translational repression across the Plasmodium life cycle [#0, #1]. In P. falciparum asexual/general contexts it binds poly(A) RNA specifically in vitro and interacts with the translation initiation factor eIF4G, consistent with a role in the eIF4F initiation complex [#0]. During sexual development, however, PABP1 is redirected into translationally repressive messenger ribonucleoprotein and stress granule complexes: in P. berghei female gametocytes it is a component of the DOZI/CITH mRNP that stores silenced transcripts and integrates eIF4E and poly(A)-binding protein while excluding eIF4G and P-body degradation factors [#1], and in P. falciparum female gametocytes it associates with 7-Helix-1, CITH, and DOZI in stress granules regulating translational repression during gametocytogenesis [#2]. In P. falciparum male gametocytes PABP1 sits within an MD3-containing post-transcriptional regulatory complex (also including ALBA3, eIF4G, PUF1, NOT1, and CITH) required for male gametocytogenesis [#4]. The P. yoelii ortholog binds poly(A) strongly, self-associates into RNase-resistant homopolymeric chains, and, beyond its cytoplasmic blood-stage role, localizes to the sporozoite surface and is deposited in gliding trails [#3].\",\n  \"teleology\": [\n    {\n      \"year\": 2009,\n      \"claim\": \"Establishing whether PABP1 is a bona fide poly(A)-binding protein wired into translation initiation, this work showed specific poly(A) binding and a direct interaction with eIF4G, placing it in the eIF4F initiation complex.\",\n      \"evidence\": \"In vitro poly(A) binding assay plus co-immunoprecipitation/interaction with eIF4G in P. falciparum\",\n      \"pmids\": [\"19751846\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No structural mapping of the RNA-binding or eIF4G-interacting regions\",\n        \"Functional consequence of the eIF4G interaction on translation not tested in vivo\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Addressing whether PABP1 also participates in transcript storage rather than only active translation, purification of the female-gametocyte DOZI/CITH mRNP placed PABP1 in a translationally repressive complex that contained eIF4E but excluded eIF4G and degradation factors.\",\n      \"evidence\": \"Affinity purification and mass spectrometry of the DOZI/CITH mRNP from P. berghei female gametocytes\",\n      \"pmids\": [\"20169188\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Does not establish whether PABP1 is required for repression or merely co-purifies\",\n        \"Mechanism switching PABP1 between eIF4G-bound (active) and eIF4E-bound repressive contexts unresolved\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"To define PABP1's partners in the repressive machinery, reciprocal co-IP placed it in female-gametocyte stress granules with 7-Helix-1, CITH, and DOZI, linking it to translational repression during gametocytogenesis.\",\n      \"evidence\": \"Co-immunoprecipitation with 7-Helix-1/CITH/DOZI and immunofluorescence localization in P. falciparum female gametocytes\",\n      \"pmids\": [\"30133543\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Direct versus bridged nature of each interaction not resolved\",\n        \"Effect of PABP1 loss on stress granule assembly not tested\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2018,\n      \"claim\": \"Testing whether PABP1 has functions beyond RNA regulation, the P. yoelii ortholog was shown to bind poly(A) strongly, self-assemble into RNase-resistant chains, and unexpectedly localize to the sporozoite surface and gliding trails.\",\n      \"evidence\": \"Multiple poly(A) binding assays, RNase-resistant chain-formation assay, and IFA in P. yoelii\",\n      \"pmids\": [\"29359180\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional role of surface/gliding-trail deposition unknown\",\n        \"Whether P. falciparum PABP1 shares the sporozoite surface localization not tested\",\n        \"Physiological relevance of in vitro homopolymeric chains unclear\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium yoelii\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2023,\n      \"claim\": \"Extending PABP1's repressive role to the male lineage, proximity labeling and co-IP placed it in an MD3-anchored complex (ALBA3, eIF4G, PUF1, NOT1, CITH) required for male gametocytogenesis.\",\n      \"evidence\": \"BioID proximity labeling and co-immunoprecipitation in P. falciparum male gametocytes\",\n      \"pmids\": [\"38148574\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Individual requirement of PABP1 (versus MD3) for the phenotype not isolated\",\n        \"Target transcripts regulated by this complex not defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"How PABP1 is molecularly switched between the active eIF4G-associated initiation complex and the repressive eIF4E/DOZI/CITH mRNP and stress granules, and what its poly(A)-independent sporozoite-surface role is, remain unresolved.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"No direct loss-of-function of PABP1 itself linking it to any life-cycle phenotype\",\n        \"No structural model of PABP1 or its complexes\",\n        \"Regulatory signal governing complex partitioning unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0008143\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0003723\", \"supporting_discovery_ids\": [0, 3]},\n      {\"term_id\": \"GO:0042803\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [3]},\n      {\"term_id\": \"GO:0010494\", \"supporting_discovery_ids\": [2]},\n      {\"term_id\": \"GO:0035770\", \"supporting_discovery_ids\": [1, 4]},\n      {\"term_id\": \"GO:0009986\", \"supporting_discovery_ids\": [3]}\n    ],\n    \"pathway\": [\n      {\"term_id\": \"GO:0006413\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0017148\", \"supporting_discovery_ids\": [1, 2]},\n      {\"term_id\": \"GO:0045131\", \"supporting_discovery_ids\": [2, 4]}\n    ],\n    \"complexes\": [\n      \"eIF4F translation initiation complex (with eIF4G)\",\n      \"DOZI/CITH translationally repressive mRNP (with eIF4E, DOZI, CITH)\",\n      \"Female gametocyte stress granule complex (with 7-Helix-1, CITH, DOZI)\",\n      \"MD3-containing male-gametocyte post-transcriptional complex (with ALBA3, eIF4G, PUF1, NOT1, CITH)\"\n    ],\n    \"partners\": [\n      \"eIF4G\",\n      \"eIF4E\",\n      \"DOZI\",\n      \"CITH\",\n      \"7-Helix-1\",\n      \"MD3\",\n      \"ALBA3\",\n      \"PUF1\",\n      \"NOT1\"\n    ],\n    \"other_free_text\": [\n      \"Binds poly(A) RNA specifically in vitro (P. falciparum and P. yoelii ortholog)\",\n      \"P. yoelii ortholog forms RNase-resistant homopolymeric chains in vitro\",\n      \"P. yoelii ortholog deposited in sporozoite gliding trails; function of this localization uncharacterized\",\n      \"MD3 complex required for male gametocytogenesis; PABP1's individual requirement not isolated\"\n    ]\n  }\n}","audit_flag":null,"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_1224300","name":null,"product":"polyadenylate-binding protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1439200","name":null,"product":"polyadenylate-binding protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1443600","name":null,"product":"polyadenylate-binding protein 1, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"PABP","evaluation":null}