{"gene":"PF3D7_0729800","run_date":"2026-09-08T12:51:27","timeline":{"discoveries":[{"year":2010,"finding":"PfDLC1 (PF3D7_0729800) physically interacts with P. falciparum myosin A and actin 1 in blood-stage parasites, as demonstrated by co-immunoprecipitation; the interacting domains were mapped to SDIE and/or EEMKT motifs in the upper 50-kDa segment of myosin A head domain and subdomain IV of actin 1, respectively.","method":"Co-immunoprecipitation, interaction domain mapping","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP with domain mapping, single lab, two orthogonal approaches (Co-IP + domain mapping)","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"PfDLC1 localizes to the cytoplasm in a pattern similar to actin and co-localizes with myosin A, as shown by fluorescence tagging and immunofluorescence staining in late trophozoites and schizonts.","method":"Fluorescence tagging, immunofluorescence microscopy","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization by two imaging methods (fluorescence tag and immunofluorescence), single lab, co-localization with known partners","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"Attempts to disrupt the dlc1 gene by reverse genetics in both P. falciparum and P. berghei were unsuccessful (negative result), suggesting essentiality for parasite survival or inaccessibility of the locus.","method":"Reverse genetic gene disruption attempts (failed)","journal":"The Journal of biological chemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — negative result from a single lab; essentiality is inferred but not directly demonstrated","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium berghei","strain":""}]},{"year":2010,"finding":"PfDLC1 protein is expressed at high levels in late trophozoites and schizonts, indicating a role in blood-stage development independent of flagella.","method":"Expression analysis (Western blot / protein detection across life stages)","journal":"The Journal of biological chemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single lab, single method (expression profiling), no direct functional readout","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PfDLC1 (PF3D7_0729800) is a cytoplasmic dynein light chain expressed in blood-stage P. falciparum (late trophozoites and schizonts) that physically associates with myosin A (via SDIE/EEMKT motifs in the myosin A head domain) and actin 1 (via subdomain IV), co-localizes with these motor proteins in the cytoplasm, and appears essential for parasite survival based on failed gene disruption attempts in P. falciparum and P. berghei."},"narrative":{"mechanistic_narrative":"PfDLC1 (PF3D7_0729800) is a putative dynein light chain of Plasmodium falciparum that associates with the actomyosin motor machinery during blood-stage development rather than with a flagellar apparatus [PMID:20421304]. Reciprocal co-immunoprecipitation with domain mapping places PfDLC1 in physical contact with myosin A—through the SDIE and/or EEMKT motifs in the upper 50-kDa segment of the myosin A head domain—and with actin 1 via subdomain IV [PMID:20421304], and the protein co-localizes with these partners in the cytoplasm of late trophozoites and schizonts [PMID:20421304]. Failed gene-disruption attempts in both P. falciparum and P. berghei are consistent with essentiality for parasite survival [PMID:20421304]. Beyond these physical associations, localization, and the negative knockout result, no downstream mechanistic function, substrate, or role in a defined motor complex has been characterized for PF3D7_0729800 in the available corpus.","teleology":[{"year":2010,"claim":"It was unknown whether this putative dynein light chain engages any specific partner in blood-stage parasites; reciprocal Co-IP with domain mapping established direct physical association with the actomyosin motor components myosin A and actin 1 and pinpointed the interacting surfaces.","evidence":"Co-immunoprecipitation and interaction domain mapping in blood-stage P. falciparum","pmids":["20421304"],"confidence":"Medium","gaps":["Interaction shown biochemically but functional consequence for motor activity not tested","Whether PfDLC1 acts as an adaptor bridging myosin A and actin 1 or binds them independently is not resolved","Stoichiometry and reconstitution of any complex not established"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"To test whether the interactions occur in a shared cellular compartment, imaging showed PfDLC1 resides in the cytoplasm in an actin-like pattern and co-localizes with myosin A in late trophozoites and schizonts, placing it spatially with its partners during blood-stage development.","evidence":"Fluorescence tagging and immunofluorescence microscopy in P. falciparum late trophozoites and schizonts","pmids":["20421304"],"confidence":"Medium","gaps":["Co-localization does not demonstrate a functional motor complex","Subcellular resolution insufficient to define specific structures","No live-imaging of dynamics"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"Because loss-of-function phenotype was unknown, gene-disruption was attempted; failure to disrupt dlc1 in both P. falciparum and P. berghei is consistent with essentiality, though the negative result does not directly demonstrate an essential function.","evidence":"Failed reverse-genetic gene disruption in P. falciparum and P. berghei","pmids":["20421304"],"confidence":"Low","gaps":["Essentiality inferred from a negative result, not demonstrated by conditional knockdown or rescue","Locus inaccessibility cannot be excluded as an alternative explanation","No stage-specific functional requirement defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"The molecular function of PF3D7_0729800 within the actomyosin machinery — whether it regulates myosin A motor activity, serves as a structural adaptor, or performs a dynein-related role — remains undefined.","evidence":"","pmids":[],"confidence":"Low","gaps":["No functional assay linking the interactions to gliding, invasion, or motor activity","No conditional loss-of-function phenotype","No structural model of the PfDLC1-myosin A-actin 1 association"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["MYOSIN A (P. FALCIPARUM)","ACTIN 1 (P. FALCIPARUM)"],"other_free_text":["PfDLC1 (PF3D7_0729800) is expressed at high levels in late trophozoites and schizonts, indicating a blood-stage role independent of flagella [#3].","Gene disruption failed in both P. falciparum and P. berghei, consistent with but not proving essentiality [#2].","Interaction surfaces mapped to SDIE/EEMKT motifs of the myosin A head domain and subdomain IV of actin 1 [#0]."]}},"prefetch_data":{},"corpus_meta":[{"pmid":"20421304","id":"PMC_20421304","title":"Plasmodium falciparum dynein light chain 1 interacts with actin/myosin during blood stage development.","date":"2010","source":"The Journal of biological chemistry","url":"https://pubmed.ncbi.nlm.nih.gov/20421304","citation_count":15,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["dynein light chain"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false},{"pmid":"18467191","id":"PMC_18467191","title":"Plasmodium possesses dynein light chain classes that are unique and conserved across species.","date":"2008","source":"Infection, genetics and evolution : journal of molecular epidemiology and evolutionary genetics in infectious diseases","url":"https://pubmed.ncbi.nlm.nih.gov/18467191","citation_count":3,"is_preprint":false,"source_species":["Pf"],"role":"primary","match_terms":["dynein light chain"],"competing_organism_flag":false,"competing_organism_match":"","competing_organism_only":false}],"cost":{"stage1":{"model":"claude-sonnet-4-6","input_tokens":3882,"output_tokens":1016,"usd":0.013443,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5743,"output_tokens":1870,"usd":0.037733,"stage2_stop_reason":"end_turn"},"total_usd":0.051176,"stage1_batch_id":"msgbatch_01DisAaTypwmC8QwdMBuePHo","stage2_batch_id":"msgbatch_0184zxZTqxiEfdYYfPMfkqjb","note":"batch pricing = 50% of standard"},"stage1_raw":"```json\n{\n  \"discoveries\": [\n    {\n      \"year\": 2010,\n      \"finding\": \"PfDLC1 (PF3D7_0729800) physically interacts with P. falciparum myosin A and actin 1 in blood-stage parasites, as demonstrated by co-immunoprecipitation; the interacting domains were mapped to SDIE and/or EEMKT motifs in the upper 50-kDa segment of myosin A head domain and subdomain IV of actin 1, respectively.\",\n      \"method\": \"Co-immunoprecipitation, interaction domain mapping\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 2 / Moderate — reciprocal Co-IP with domain mapping, single lab, two orthogonal approaches (Co-IP + domain mapping)\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"PfDLC1 localizes to the cytoplasm in a pattern similar to actin and co-localizes with myosin A, as shown by fluorescence tagging and immunofluorescence staining in late trophozoites and schizonts.\",\n      \"method\": \"Fluorescence tagging, immunofluorescence microscopy\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct localization by two imaging methods (fluorescence tag and immunofluorescence), single lab, co-localization with known partners\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"Attempts to disrupt the dlc1 gene by reverse genetics in both P. falciparum and P. berghei were unsuccessful (negative result), suggesting essentiality for parasite survival or inaccessibility of the locus.\",\n      \"method\": \"Reverse genetic gene disruption attempts (failed)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — negative result from a single lab; essentiality is inferred but not directly demonstrated\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"PfDLC1 protein is expressed at high levels in late trophozoites and schizonts, indicating a role in blood-stage development independent of flagella.\",\n      \"method\": \"Expression analysis (Western blot / protein detection across life stages)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single lab, single method (expression profiling), no direct functional readout\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PfDLC1 (PF3D7_0729800) is a cytoplasmic dynein light chain expressed in blood-stage P. falciparum (late trophozoites and schizonts) that physically associates with myosin A (via SDIE/EEMKT motifs in the myosin A head domain) and actin 1 (via subdomain IV), co-localizes with these motor proteins in the cytoplasm, and appears essential for parasite survival based on failed gene disruption attempts in P. falciparum and P. berghei.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PfDLC1 (PF3D7_0729800) is a putative dynein light chain of Plasmodium falciparum that associates with the actomyosin motor machinery during blood-stage development rather than with a flagellar apparatus [#0, #3]. Reciprocal co-immunoprecipitation with domain mapping places PfDLC1 in physical contact with myosin A—through the SDIE and/or EEMKT motifs in the upper 50-kDa segment of the myosin A head domain—and with actin 1 via subdomain IV [#0], and the protein co-localizes with these partners in the cytoplasm of late trophozoites and schizonts [#1]. Failed gene-disruption attempts in both P. falciparum and P. berghei are consistent with essentiality for parasite survival [#2]. Beyond these physical associations, localization, and the negative knockout result, no downstream mechanistic function, substrate, or role in a defined motor complex has been characterized for PF3D7_0729800 in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"It was unknown whether this putative dynein light chain engages any specific partner in blood-stage parasites; reciprocal Co-IP with domain mapping established direct physical association with the actomyosin motor components myosin A and actin 1 and pinpointed the interacting surfaces.\",\n      \"evidence\": \"Co-immunoprecipitation and interaction domain mapping in blood-stage P. falciparum\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Interaction shown biochemically but functional consequence for motor activity not tested\", \"Whether PfDLC1 acts as an adaptor bridging myosin A and actin 1 or binds them independently is not resolved\", \"Stoichiometry and reconstitution of any complex not established\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"To test whether the interactions occur in a shared cellular compartment, imaging showed PfDLC1 resides in the cytoplasm in an actin-like pattern and co-localizes with myosin A in late trophozoites and schizonts, placing it spatially with its partners during blood-stage development.\",\n      \"evidence\": \"Fluorescence tagging and immunofluorescence microscopy in P. falciparum late trophozoites and schizonts\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\"Co-localization does not demonstrate a functional motor complex\", \"Subcellular resolution insufficient to define specific structures\", \"No live-imaging of dynamics\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Because loss-of-function phenotype was unknown, gene-disruption was attempted; failure to disrupt dlc1 in both P. falciparum and P. berghei is consistent with essentiality, though the negative result does not directly demonstrate an essential function.\",\n      \"evidence\": \"Failed reverse-genetic gene disruption in P. falciparum and P. berghei\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"Essentiality inferred from a negative result, not demonstrated by conditional knockdown or rescue\", \"Locus inaccessibility cannot be excluded as an alternative explanation\", \"No stage-specific functional requirement defined\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}, {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The molecular function of PF3D7_0729800 within the actomyosin machinery — whether it regulates myosin A motor activity, serves as a structural adaptor, or performs a dynein-related role — remains undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\"No functional assay linking the interactions to gliding, invasion, or motor activity\", \"No conditional loss-of-function phenotype\", \"No structural model of the PfDLC1-myosin A-actin 1 association\"],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0045504\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0051015\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [\"Myosin A (P. falciparum)\", \"Actin 1 (P. falciparum)\"],\n    \"other_free_text\": [\n      \"PfDLC1 (PF3D7_0729800) is expressed at high levels in late trophozoites and schizonts, indicating a blood-stage role independent of flagella [#3].\",\n      \"Gene disruption failed in both P. falciparum and P. berghei, consistent with but not proving essentiality [#2].\",\n      \"Interaction surfaces mapped to SDIE/EEMKT motifs of the myosin A head domain and subdomain IV of actin 1 [#0].\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_0729800","tier":"IDENTITY_CHECK","verdict":"identity unverified","subtype":"names_other_cards","uniprot_band":"","rules_fired":"R12","issue":"No cited paper names this card; 1 of 1 cited papers name other catalogue genes (PF3D7_0822500). The summary may describe one of those genes."},"strains":[{"strain":"Pf3D7","gene_id":"PF3D7_0729800","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0213900","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0214700","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}