{"id":"541cb731-f1e7-5313-8bc9-aa8f90d2bdb6","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-carrier-vestibule","predicate":"changes_regulatory_conformation","statement":"Calcium-associated movement of the mobile regulatory domain opened a vestibule in regulatory-domain structures; the authors proposed that this controls substrate access.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"180969e2-d2f8-5913-b455-cf3242c94070","mechanism_event_label":"Calcium binding can change access to the transport machinery.","subject":{"id":"e359bc15-e675-5d83-b0fe-1d70814e130b","slug":"calcium-ion","display_name":"Calcium ion","entity_type_key":"ion"},"object":{"id":"c2ef79cf-1fb7-52d2-b134-7a0d8de6ccbd","slug":"human-agc-regulatory-vestibule","display_name":"Regulatory vestibule of human aspartate/glutamate carriers","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"180969e2-d2f8-5913-b455-cf3242c94070","stable_key":"e37461ea-ea5d-5e2c-8091-138305f6dd70:l-aspartate-carrier-vestibule-event","event_type":"observed_relationship","label":"Calcium binding can change access to the transport machinery.","description":"Calcium-associated movement of the mobile regulatory domain opened a vestibule in regulatory-domain structures; the authors proposed that this controls substrate access.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"e359bc15-e675-5d83-b0fe-1d70814e130b","slug":"calcium-ion","display_name":"Calcium ion","entity_type_key":"ion"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"c2ef79cf-1fb7-52d2-b134-7a0d8de6ccbd","slug":"human-agc-regulatory-vestibule","display_name":"Regulatory vestibule of human aspartate/glutamate carriers","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"0a0923d3-72b7-5d6a-bf3a-5a7a3071a09b","slug":"l-aspartate","display_name":"L-Aspartate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"73632001-aec1-522c-80dd-7c5d1eda4ebe","slug":"slc25a12","display_name":"Human aralar / SLC25A12","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"5252ba8d-8e58-5fa5-abdb-7bc97ef85818","slug":"slc25a13","display_name":"Human citrin / SLC25A13","entity_type_key":"protein"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"7da684a4-2641-5bc6-93ae-8c6aa384e487","slug":"glutamate","display_name":"L-Glutamate","entity_type_key":"small_molecule"},"role":"context_participant","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"evidence_access","value_text":"Primary full text","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Human citrin/aralar domain structures and structural model.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"The substrate-access gating mechanism is structure-supported interpretation, not direct observation of an entire transport cycle.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"L-Aspartate collection; species, compartment, exposure, co-substrates and manipulation remain explicit.","comparator":null,"unit":null,"notes":"","entity":{"slug":"l-aspartate","display_name":"L-Aspartate","entity_type_key":"small_molecule"}},{"dimension":"plain_language","value_text":"Calcium binding can change access to the transport machinery.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"Calcium-induced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25410934/ · DOI 10.1038/ncomms6491","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"e7fe0824-e31c-5f2f-bcee-4fa8c0126f54","evidence_kind":"source_excerpt","locator":"Lines 114-120","start_line":114,"end_line":120,"excerpt":"## l-aspartate-carrier-vestibule\nCalcium binding can change access to the transport machinery.\nCalcium-associated movement of the mobile regulatory domain opened a vestibule in regulatory-domain structures; the authors proposed that this controls substrate access.\nModel: Human citrin/aralar domain structures and structural model.\nLimitations: The substrate-access gating mechanism is structure-supported interpretation, not direct observation of an entire transport cycle.\nEvidence access: Primary full text\nCalcium-induced conformational changes of the regulatory domain of human mitochondrial aspartate/glutamate carriers. · 2014 · https://pubmed.ncbi.nlm.nih.gov/25410934/ · DOI 10.1038/ncomms6491","model_system":"Human citrin/aralar domain structures and structural model.","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":"67970dcb-34e0-5b0a-8c86-d8c3cc183444","stable_key":"import-e37461ea-ea5d-5e2c-8091-138305f6dd70","title":"L-Aspartate: redox transfer, nitrogen partitioning and cross-nutrient mechanisms (2026-09-19)","document_type":"imported_text","citation_label":"AI-assisted research curation; primary references, access levels and experimental limitations individually identified. 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