{"gene":"PF3D7_1147100","run_date":"2026-09-08T14:19:05","timeline":{"discoveries":[{"year":2010,"finding":"PfDLC1 (PF3D7_1147100) 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 in subdomain IV of actin 1, respectively.","method":"Co-immunoprecipitation and domain-mapping experiments","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 2 / Moderate — reciprocal Co-IP with domain mapping, single lab, two complementary methods (Co-IP plus fluorescence co-localization)","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"PfDLC1 localises to the cytoplasm in a pattern similar to actin, and co-localises with myosin A by immunofluorescence staining in blood-stage parasites, consistent with a role in the actomyosin system during erythrocytic development.","method":"Fluorescence tagging and immunofluorescence microscopy","journal":"The Journal of biological chemistry","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization experiment supported by Co-IP data from the same study, single lab","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, suggesting essentiality for parasite survival or inaccessibility of the locus.","method":"Reverse genetic disruption attempts (negative result)","journal":"The Journal of biological chemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — negative result from single-lab gene disruption attempts; essentiality is inferred, 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, stages that lack flagella, pointing to a non-flagellar role in blood-stage parasites.","method":"Expression analysis (protein detection in stage-specific samples)","journal":"The Journal of biological chemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single-lab expression study without functional follow-up beyond stage correlation","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PfDLC1 (PF3D7_1147100) is a dynein light chain expressed in blood-stage P. falciparum that localises to the cytoplasm and physically interacts with myosin A (via SDIE/EEMKT motifs in its head domain) and actin 1 (via subdomain IV), implicating it in the parasite's actomyosin machinery during erythrocytic development rather than in flagellar motility; failed gene-disruption attempts suggest it may be essential for parasite survival."},"narrative":{"mechanistic_narrative":"PfDLC1 (PF3D7_1147100) is a dynein light chain expressed in blood-stage Plasmodium falciparum that is implicated in the parasite's actomyosin system during erythrocytic development rather than in canonical flagellar dynein motility [PMID:20421304]. In blood-stage parasites it physically associates with both myosin A and actin 1, with the interactions mapped to SDIE and/or EEMKT motifs in the upper 50-kDa segment of the myosin A head domain and to subdomain IV of actin 1 [PMID:20421304]. Consistent with these interactions, PfDLC1 localises to the cytoplasm in a pattern resembling actin and co-localises with myosin A by immunofluorescence [PMID:20421304]. Beyond this actomyosin association, its precise molecular contribution to motility or invasion has not been characterized in the available corpus.","teleology":[{"year":2010,"claim":"Whether a putative dynein light chain in a blood stage that lacks flagella has any partner or role was unknown; identifying its binding partners established PfDLC1 as a component of the parasite actomyosin machinery rather than a flagellar dynein subunit.","evidence":"Reciprocal co-immunoprecipitation with domain mapping in blood-stage P. falciparum","pmids":["20421304"],"confidence":"Medium","gaps":["Functional consequence of the myosin A / actin 1 interactions not tested","Whether binding is direct or bridged by other proteins not resolved","Stoichiometry and regulation of the interaction unknown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"To test where PfDLC1 acts in the cell, localisation was examined, establishing that it resides in the cytoplasm co-distributed with actin and myosin A, supporting an actomyosin-associated role during erythrocytic development.","evidence":"Fluorescence tagging and immunofluorescence microscopy in blood-stage parasites","pmids":["20421304"],"confidence":"Medium","gaps":["Co-localisation does not demonstrate a functional requirement","Subcellular resolution relative to invasion machinery not defined"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"The developmental timing and dispensability of PfDLC1 were addressed by stage-specific expression and gene-disruption attempts, indicating peak abundance in aflagellar late blood stages and possible essentiality.","evidence":"Stage-specific protein detection and reverse-genetic disruption attempts (negative result) in P. falciparum and P. berghei","pmids":["20421304"],"confidence":"Low","gaps":["Essentiality is inferred from failed knockout, not demonstrated by conditional depletion","Locus inaccessibility cannot be excluded as the reason for disruption failure","No phenotype linked to loss of PfDLC1 function"],"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"The functional role of PfDLC1 within the actomyosin system — whether it modulates motor activity, invasion, or another process — remains undefined.","evidence":"","pmids":[],"confidence":"Low","gaps":["No conditional knockdown or complementation to establish essentiality and phenotype","No structural or biochemical reconstitution of the myosin A / actin 1 / PfDLC1 assembly","No demonstration of a mechanistic contribution to gliding motility or erythrocyte invasion"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":["Actomyosin system (myosin A / actin 1 association)"],"partners":["MYOSIN A (PFMYOA)","ACTIN 1 (PFACT1)"],"other_free_text":["Interaction mapped to SDIE/EEMKT motifs in the myosin A head upper 50-kDa segment and to subdomain IV of actin 1 [#0]","Peak protein expression in late trophozoites and schizonts, stages lacking flagella [#3]","Gene disruption unsuccessful in both P. falciparum and P. berghei, inferring possible essentiality [#2]"]}},"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":5746,"output_tokens":1805,"usd":0.036928,"stage2_stop_reason":"end_turn"},"total_usd":0.050371,"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\": 2010,\n      \"finding\": \"PfDLC1 (PF3D7_1147100) 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 in subdomain IV of actin 1, respectively.\",\n      \"method\": \"Co-immunoprecipitation and domain-mapping experiments\",\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 complementary methods (Co-IP plus fluorescence co-localization)\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"PfDLC1 localises to the cytoplasm in a pattern similar to actin, and co-localises with myosin A by immunofluorescence staining in blood-stage parasites, consistent with a role in the actomyosin system during erythrocytic development.\",\n      \"method\": \"Fluorescence tagging and immunofluorescence microscopy\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"Tier 3 / Moderate — direct localization experiment supported by Co-IP data from the same study, single lab\",\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, suggesting essentiality for parasite survival or inaccessibility of the locus.\",\n      \"method\": \"Reverse genetic disruption attempts (negative result)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — negative result from single-lab gene disruption attempts; essentiality is inferred, 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, stages that lack flagella, pointing to a non-flagellar role in blood-stage parasites.\",\n      \"method\": \"Expression analysis (protein detection in stage-specific samples)\",\n      \"journal\": \"The Journal of biological chemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single-lab expression study without functional follow-up beyond stage correlation\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"current_model\": \"PfDLC1 (PF3D7_1147100) is a dynein light chain expressed in blood-stage P. falciparum that localises to the cytoplasm and physically interacts with myosin A (via SDIE/EEMKT motifs in its head domain) and actin 1 (via subdomain IV), implicating it in the parasite's actomyosin machinery during erythrocytic development rather than in flagellar motility; failed gene-disruption attempts suggest it may be essential for parasite survival.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PfDLC1 (PF3D7_1147100) is a dynein light chain expressed in blood-stage Plasmodium falciparum that is implicated in the parasite's actomyosin system during erythrocytic development rather than in canonical flagellar dynein motility [#0, #1]. In blood-stage parasites it physically associates with both myosin A and actin 1, with the interactions mapped to SDIE and/or EEMKT motifs in the upper 50-kDa segment of the myosin A head domain and to subdomain IV of actin 1 [#0]. Consistent with these interactions, PfDLC1 localises to the cytoplasm in a pattern resembling actin and co-localises with myosin A by immunofluorescence [#1]. Beyond this actomyosin association, its precise molecular contribution to motility or invasion has not been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"Whether a putative dynein light chain in a blood stage that lacks flagella has any partner or role was unknown; identifying its binding partners established PfDLC1 as a component of the parasite actomyosin machinery rather than a flagellar dynein subunit.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation with domain mapping in blood-stage P. falciparum\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Functional consequence of the myosin A / actin 1 interactions not tested\",\n        \"Whether binding is direct or bridged by other proteins not resolved\",\n        \"Stoichiometry and regulation of the interaction unknown\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"To test where PfDLC1 acts in the cell, localisation was examined, establishing that it resides in the cytoplasm co-distributed with actin and myosin A, supporting an actomyosin-associated role during erythrocytic development.\",\n      \"evidence\": \"Fluorescence tagging and immunofluorescence microscopy in blood-stage parasites\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Medium\",\n      \"gaps\": [\n        \"Co-localisation does not demonstrate a functional requirement\",\n        \"Subcellular resolution relative to invasion machinery not defined\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"The developmental timing and dispensability of PfDLC1 were addressed by stage-specific expression and gene-disruption attempts, indicating peak abundance in aflagellar late blood stages and possible essentiality.\",\n      \"evidence\": \"Stage-specific protein detection and reverse-genetic disruption attempts (negative result) in P. falciparum and P. berghei\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"Essentiality is inferred from failed knockout, not demonstrated by conditional depletion\",\n        \"Locus inaccessibility cannot be excluded as the reason for disruption failure\",\n        \"No phenotype linked to loss of PfDLC1 function\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The functional role of PfDLC1 within the actomyosin system — whether it modulates motor activity, invasion, or another process — remains undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"gaps\": [\n        \"No conditional knockdown or complementation to establish essentiality and phenotype\",\n        \"No structural or biochemical reconstitution of the myosin A / actin 1 / PfDLC1 assembly\",\n        \"No demonstration of a mechanistic contribution to gliding motility or erythrocyte invasion\"\n      ],\n      \"attribution\": [{\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [\n      {\"term_id\": \"GO:0003779\", \"supporting_discovery_ids\": [0]},\n      {\"term_id\": \"GO:0017022\", \"supporting_discovery_ids\": [0]}\n    ],\n    \"localization\": [\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [\"Actomyosin system (myosin A / actin 1 association)\"],\n    \"partners\": [\"Myosin A (PfMyoA)\", \"Actin 1 (PfAct1)\"],\n    \"other_free_text\": [\n      \"Interaction mapped to SDIE/EEMKT motifs in the myosin A head upper 50-kDa segment and to subdomain IV of actin 1 [#0]\",\n      \"Peak protein expression in late trophozoites and schizonts, stages lacking flagella [#3]\",\n      \"Gene disruption unsuccessful in both P. falciparum and P. berghei, inferring possible essentiality [#2]\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_1147100","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_1147100","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_0902000","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_0944900","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}