{"id":"3f15e7d9-c759-5c4b-a3d1-435a822719ea","stable_key":"1acdb1e8-2159-5c7f-b39f-0153ff8024ae:taurine-mto1-proteostress","predicate":"loss_induces","statement":"Mto1-deficient experimental cells and mice showed defective mitochondrial translation with mistargeting and aggregation of nuclear-encoded mitochondrial proteins; chemical chaperones reduced cytotoxicity.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"e884d07a-6ff2-5b16-b110-1457c20a2dd7","mechanism_event_label":"Failure of mitochondrial translation can disturb protein handling beyond mitochondria.","subject":{"id":"8c8a20fb-f734-5beb-980d-cf03c6dc28bb","slug":"mouse-mto1","display_name":"Mouse mitochondrial tRNA modification protein / Mto1","entity_type_key":"protein"},"object":{"id":"4155a2b4-0f48-5ca3-90a9-2e55fc4ab506","slug":"mouse-mto1-proteostress","display_name":"Cytoplasmic proteostress following Mto1 loss in mouse models","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"e884d07a-6ff2-5b16-b110-1457c20a2dd7","stable_key":"1acdb1e8-2159-5c7f-b39f-0153ff8024ae:taurine-mto1-proteostress-event","event_type":"observed_relationship","label":"Failure of mitochondrial translation can disturb protein handling beyond mitochondria.","description":"Mto1-deficient experimental cells and mice showed defective mitochondrial translation with mistargeting and aggregation of nuclear-encoded mitochondrial proteins; chemical chaperones reduced cytotoxicity.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"8c8a20fb-f734-5beb-980d-cf03c6dc28bb","slug":"mouse-mto1","display_name":"Mouse mitochondrial tRNA modification protein / Mto1","entity_type_key":"protein"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"4155a2b4-0f48-5ca3-90a9-2e55fc4ab506","slug":"mouse-mto1-proteostress","display_name":"Cytoplasmic proteostress following Mto1 loss in mouse models","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"dd968147-5f93-56d5-bc83-7fa01f9b0e42","slug":"mt-trna-taurinomethyluridine","display_name":"Mitochondrial tRNA 5-taurinomethyluridine / tau-m5U34","entity_type_key":"rna_modification"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"e423cd36-f183-522b-a5e4-5f9ef50eee7e","slug":"taurine","display_name":"Taurine","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""}]},"contexts":[{"dimension":"availability_state","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null},{"dimension":"evidence_access","value_text":"Primary abstract","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Mto1 deficiency in experimental cells and mice.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The rescue used chemical chaperones, not proof that taurine treats absent Mto1.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Taurine collection; molecular form, preparation, species, exposure and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"taurine","display_name":"Taurine","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Failure of mitochondrial translation can disturb protein handling beyond mitochondria.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Defective Mitochondrial tRNA Taurine Modification Activates Global Proteostress and Leads to Mitochondrial Disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29320742/ · DOI 10.1016/j.celrep.2017.12.051","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"trigger_kind","value_text":"machinery_impairment","comparator":null,"unit":null,"notes":"Imported condition classification; unverified.","entity":null}],"evidence":[{"id":"23787113-291a-53df-82dd-bdcca9c30143","evidence_kind":"source_excerpt","locator":"Lines 273-279","start_line":273,"end_line":279,"excerpt":"## taurine-mto1-proteostress\nFailure of mitochondrial translation can disturb protein handling beyond mitochondria.\nMto1-deficient experimental cells and mice showed defective mitochondrial translation with mistargeting and aggregation of nuclear-encoded mitochondrial proteins; chemical chaperones reduced cytotoxicity.\nModel: Mto1 deficiency in experimental cells and mice.\nLimitations: The rescue used chemical chaperones, not proof that taurine treats absent Mto1.\nEvidence access: Primary abstract\nDefective Mitochondrial tRNA Taurine Modification Activates Global Proteostress and Leads to Mitochondrial Disease. · 2018 · https://pubmed.ncbi.nlm.nih.gov/29320742/ · DOI 10.1016/j.celrep.2017.12.051","model_system":"Mto1 deficiency in experimental cells and mice.","directness":"reported_statement","verification_status":"source_derived_draft","notes":"Original curation paraphrase; evidence access and experimental limitations specified.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"dc8d9ab8-fdf9-5107-877c-336cf8005097","stable_key":"import-1acdb1e8-2159-5c7f-b39f-0153ff8024ae","title":"Taurine: synthesis, transport, mitochondrial decoding and nutrient interactions (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary-abstract references and experimental limitations individually identified. 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