{"gene":"PF3D7_1420800","run_date":"2026-09-08T14:19:07","timeline":{"discoveries":[{"year":2010,"finding":"PfDLC1 (PF3D7_1420800) 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 and 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 methods (Co-IP + fluorescence localization)","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"finding":"PfDLC1 localizes to the cytoplasm of blood-stage parasites with a distribution similar to actin, and co-localizes with myosin A by immunofluorescence, indicating a non-flagellar role during erythrocytic development.","method":"Fluorescence tagging and immunofluorescence microscopy","journal":"The Journal of Biological Chemistry","confidence":"Medium","confidence_rationale":"Tier 3 / Moderate — direct localization by two imaging methods (fluorescence tag + antibody IFA), 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 PfDLC1 is essential for parasite survival or its locus is inaccessible.","method":"Reverse genetic disruption attempts (negative result)","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, pointing to a role in blood-stage parasites that lack flagella.","method":"Expression analysis (protein level detection)","journal":"The Journal of Biological Chemistry","confidence":"Low","confidence_rationale":"Tier 3 / Weak — single-lab expression profiling, no functional readout beyond stage specificity","pmids":["20421304"],"is_preprint":false,"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"current_model":"PfDLC1 (PF3D7_1420800) is a leucine-rich repeat dynein light chain expressed in blood-stage P. falciparum that localizes to the cytoplasm and physically interacts with myosin A and actin 1 via defined motifs (SDIE/EEMKT), suggesting a role in the actin–myosin machinery during erythrocytic development; gene disruption attempts in P. falciparum and P. berghei failed, implying essentiality."},"narrative":{"mechanistic_narrative":"PfDLC1 (PF3D7_1420800) is a putative dynein light chain that, in blood-stage Plasmodium falciparum, functions outside any flagellar context and instead associates with the actin–myosin machinery of the erythrocytic parasite [PMID:20421304]. It physically interacts with both myosin A and actin 1, with the binding interfaces 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, respectively [PMID:20421304]. Consistent with these partnerships, PfDLC1 distributes through the cytoplasm in a pattern resembling actin and co-localizes with myosin A [PMID:20421304]. Beyond this actin–myosin association during erythrocytic development, no further mechanistic detail — including a defined biochemical activity or a demonstrated cellular consequence of the interaction — has been characterized in the available corpus.","teleology":[{"year":2010,"claim":"Establishing that a dynein light chain in a blood stage lacking flagella has binding partners at all addressed whether PfDLC1 has a non-canonical, non-flagellar role, and identified myosin A and actin 1 as its physical partners with mapped interaction motifs.","evidence":"Reciprocal co-immunoprecipitation and interaction-domain mapping in blood-stage P. falciparum","pmids":["20421304"],"confidence":"Medium","gaps":["No functional consequence of the myosin A / actin 1 interaction demonstrated","Stoichiometry and whether PfDLC1 bridges myosin A and actin simultaneously unknown","No structural model of the SDIE/EEMKT and subdomain IV interfaces"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"Localization was needed to confirm the partnerships reflect a genuine shared compartment; imaging placed PfDLC1 in the cytoplasm with an actin-like distribution and co-localized with myosin A, supporting a non-flagellar role during erythrocytic development.","evidence":"Fluorescence tagging and immunofluorescence microscopy in blood-stage P. falciparum","pmids":["20421304"],"confidence":"Medium","gaps":["Sub-cytoplasmic resolution insufficient to define a specific structure or organelle","Whether co-localization reflects direct engagement in a functional complex not shown"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]},{"year":2010,"claim":"The developmental timing and essentiality of PfDLC1 were probed to gauge its physiological importance; peak protein expression in late trophozoites and schizonts and failure to disrupt the gene point to a blood-stage requirement.","evidence":"Stage-resolved protein expression analysis and reverse-genetic disruption attempts (negative result) in P. falciparum and P. berghei","pmids":["20421304"],"confidence":"Low","gaps":["Essentiality inferred from failed knockout, not demonstrated by conditional depletion","Failed disruption may reflect locus inaccessibility rather than a lethal phenotype","No loss-of-function phenotype linking PfDLC1 to actin–myosin function"],"attribution":[{"species":"Plasmodium falciparum","strain":""},{"species":"Plasmodium berghei","strain":""}]},{"year":null,"claim":"The biochemical activity of PfDLC1 and the functional purpose of its recruitment to myosin A and actin 1 during erythrocytic development remain undefined.","evidence":"","pmids":[],"confidence":"Low","gaps":["No enzymatic or motor-regulatory activity assigned to PfDLC1","Consequence of the actin–myosin interaction for parasite motility, invasion, or division unknown","No conditional loss-of-function to establish essentiality directly"],"attribution":[{"species":"Plasmodium falciparum","strain":""}]}],"mechanism_profile":{"molecular_activity":[],"localization":[],"pathway":[],"complexes":[],"partners":["MYOSIN A (P. FALCIPARUM)","ACTIN 1 (P. FALCIPARUM)"],"other_free_text":["Interaction interfaces mapped to SDIE/EEMKT motifs in the upper 50-kDa segment of the myosin A head domain and to subdomain IV of actin 1 [#0]","Protein expression peaks in late trophozoites and schizonts [#3]","Reverse-genetic disruption attempts failed in both P. falciparum and P. berghei, implying essentiality (inferred, not directly demonstrated) [#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":1011,"usd":0.013406,"stage1_stop_reason":"end_turn"},"stage2":{"model":"claude-opus-4-8","input_tokens":5730,"output_tokens":1902,"usd":0.0381,"stage2_stop_reason":"end_turn"},"total_usd":0.051506,"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_1420800) 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 and 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 methods (Co-IP + fluorescence localization)\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"finding\": \"PfDLC1 localizes to the cytoplasm of blood-stage parasites with a distribution similar to actin, and co-localizes with myosin A by immunofluorescence, indicating a non-flagellar role 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 by two imaging methods (fluorescence tag + antibody IFA), single lab\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\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 PfDLC1 is essential for parasite survival or its locus is inaccessible.\",\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 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, pointing to a role in blood-stage parasites that lack flagella.\",\n      \"method\": \"Expression analysis (protein level detection)\",\n      \"journal\": \"The Journal of Biological Chemistry\",\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"Tier 3 / Weak — single-lab expression profiling, no functional readout beyond stage specificity\",\n      \"pmids\": [\"20421304\"],\n      \"is_preprint\": false,\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"current_model\": \"PfDLC1 (PF3D7_1420800) is a leucine-rich repeat dynein light chain expressed in blood-stage P. falciparum that localizes to the cytoplasm and physically interacts with myosin A and actin 1 via defined motifs (SDIE/EEMKT), suggesting a role in the actin–myosin machinery during erythrocytic development; gene disruption attempts in P. falciparum and P. berghei failed, implying essentiality.\"\n}\n```","stage2_raw":"{\n  \"mechanistic_narrative\": \"PfDLC1 (PF3D7_1420800) is a putative dynein light chain that, in blood-stage Plasmodium falciparum, functions outside any flagellar context and instead associates with the actin–myosin machinery of the erythrocytic parasite [#0, #1]. It physically interacts with both myosin A and actin 1, with the binding interfaces 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, respectively [#0]. Consistent with these partnerships, PfDLC1 distributes through the cytoplasm in a pattern resembling actin and co-localizes with myosin A [#1]. Beyond this actin–myosin association during erythrocytic development, no further mechanistic detail — including a defined biochemical activity or a demonstrated cellular consequence of the interaction — has been characterized in the available corpus.\",\n  \"teleology\": [\n    {\n      \"year\": 2010,\n      \"claim\": \"Establishing that a dynein light chain in a blood stage lacking flagella has binding partners at all addressed whether PfDLC1 has a non-canonical, non-flagellar role, and identified myosin A and actin 1 as its physical partners with mapped interaction motifs.\",\n      \"evidence\": \"Reciprocal co-immunoprecipitation and interaction-domain mapping in blood-stage P. falciparum\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"No functional consequence of the myosin A / actin 1 interaction demonstrated\",\n        \"Stoichiometry and whether PfDLC1 bridges myosin A and actin simultaneously unknown\",\n        \"No structural model of the SDIE/EEMKT and subdomain IV interfaces\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"Localization was needed to confirm the partnerships reflect a genuine shared compartment; imaging placed PfDLC1 in the cytoplasm with an actin-like distribution and co-localized with myosin A, supporting a non-flagellar role during erythrocytic development.\",\n      \"evidence\": \"Fluorescence tagging and immunofluorescence microscopy in blood-stage P. falciparum\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Medium\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Sub-cytoplasmic resolution insufficient to define a specific structure or organelle\",\n        \"Whether co-localization reflects direct engagement in a functional complex not shown\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": 2010,\n      \"claim\": \"The developmental timing and essentiality of PfDLC1 were probed to gauge its physiological importance; peak protein expression in late trophozoites and schizonts and failure to disrupt the gene point to a blood-stage requirement.\",\n      \"evidence\": \"Stage-resolved protein expression analysis and reverse-genetic disruption attempts (negative result) in P. falciparum and P. berghei\",\n      \"pmids\": [\"20421304\"],\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"Essentiality inferred from failed knockout, not demonstrated by conditional depletion\",\n        \"Failed disruption may reflect locus inaccessibility rather than a lethal phenotype\",\n        \"No loss-of-function phenotype linking PfDLC1 to actin–myosin function\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"},\n        {\"species\": \"Plasmodium berghei\", \"strain\": \"\"}\n      ]\n    },\n    {\n      \"year\": null,\n      \"claim\": \"The biochemical activity of PfDLC1 and the functional purpose of its recruitment to myosin A and actin 1 during erythrocytic development remain undefined.\",\n      \"evidence\": \"\",\n      \"pmids\": [],\n      \"confidence\": \"Low\",\n      \"confidence_rationale\": \"\",\n      \"gaps\": [\n        \"No enzymatic or motor-regulatory activity assigned to PfDLC1\",\n        \"Consequence of the actin–myosin interaction for parasite motility, invasion, or division unknown\",\n        \"No conditional loss-of-function to establish essentiality directly\"\n      ],\n      \"attribution\": [\n        {\"species\": \"Plasmodium falciparum\", \"strain\": \"\"}\n      ]\n    }\n  ],\n  \"mechanism_profile\": {\n    \"molecular_activity\": [],\n    \"localization\": [\n      {\"term_id\": \"GO:0005737\", \"supporting_discovery_ids\": [1]}\n    ],\n    \"pathway\": [],\n    \"complexes\": [],\n    \"partners\": [\n      \"myosin A (P. falciparum)\",\n      \"actin 1 (P. falciparum)\"\n    ],\n    \"other_free_text\": [\n      \"Interaction interfaces mapped to SDIE/EEMKT motifs in the upper 50-kDa segment of the myosin A head domain and to subdomain IV of actin 1 [#0]\",\n      \"Protein expression peaks in late trophozoites and schizonts [#3]\",\n      \"Reverse-genetic disruption attempts failed in both P. falciparum and P. berghei, implying essentiality (inferred, not directly demonstrated) [#2]\"\n    ]\n  }\n}","audit_flag":{"gene":"PF3D7_1420800","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_1420800","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PbANKA","gene_id":"PBANKA_1022400","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null},{"strain":"PkH","gene_id":"PKNH_1337200","name":null,"product":"dynein light chain, putative","uniprot_acc":null,"chromosome":null,"start_pos":null}],"gene_symbol":"","evaluation":null}