{"id":"b1c5400e-3ef7-5803-a2c2-0903d6fef421","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:basolateral-lysine-exchange","predicate":"transports","statement":"SLC7A7-SLC3A2 exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids with sodium.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"context_dependent","is_public":true,"mechanism_event_id":"6e3dd51a-57e9-5eb3-99da-77b7743f1922","mechanism_event_label":"This route helps lysine leave epithelial cells toward blood.","subject":{"id":"67810399-d835-5aef-acbe-46596e0644ac","slug":"slc7a7-slc3a2-complex","display_name":"y+LAT1-4F2hc complex","entity_type_key":"protein_complex"},"object":{"id":"5fff6664-209e-5c35-b88e-ac15c1c5fbc0","slug":"l-lysine","display_name":"L-Lysine","entity_type_key":"small_molecule"},"evidence_count":1,"mechanism_event":{"id":"6e3dd51a-57e9-5eb3-99da-77b7743f1922","stable_key":"c3df3634-4c3a-5099-a5d9-e4f6344c1084:basolateral-lysine-exchange-event","event_type":"biochemical_relationship","label":"This route helps lysine leave epithelial cells toward blood.","description":"SLC7A7-SLC3A2 exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids with sodium.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"57fab5cc-28ef-5271-a0b2-fd26e0b8b6c8","slug":"slc7a7","display_name":"y+LAT1 / SLC7A7","entity_type_key":"protein"},"role":"transporter","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"1ca4b4d5-616a-54d3-8244-0dc151b1bcfe","slug":"slc3a2","display_name":"4F2hc / SLC3A2","entity_type_key":"protein"},"role":"partner","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"5fff6664-209e-5c35-b88e-ac15c1c5fbc0","slug":"l-lysine","display_name":"L-Lysine","entity_type_key":"small_molecule"},"role":"transported_substrate","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""},{"entity":{"id":"f707c753-cc8c-5f06-90be-bb3d73c60a18","slug":"leucine","display_name":"L-Leucine","entity_type_key":"small_molecule"},"role":"counter_substrate","stoichiometry":null,"state_label":"","sequence_order":3,"notes":""},{"entity":{"id":"38de8704-84db-5770-ac1d-242cd787e798","slug":"sodium-ion","display_name":"Sodium ion","entity_type_key":"ion"},"role":"coupled_ion","stoichiometry":null,"state_label":"","sequence_order":4,"notes":""},{"entity":{"id":"67810399-d835-5aef-acbe-46596e0644ac","slug":"slc7a7-slc3a2-complex","display_name":"y+LAT1-4F2hc complex","entity_type_key":"protein_complex"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":5,"notes":""}]},"contexts":[{"dimension":"experimental_model","value_text":"Human/mouse heterodimer expression and exchange assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Neutral-substrate transport is sodium-dependent; lysine binding itself should not be mislabeled a sodium cotransport step.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"Homo sapiens","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"This route helps lysine leave epithelial cells toward blood.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[pfeiffer1999yl] Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. (1999). https://pubmed.ncbi.nlm.nih.gov/9878049/ DOI: 10.1093/emboj/18.1.49","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Basolateral intestinal and renal epithelial membranes","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"transport_effect","value_text":"lowers","comparator":null,"unit":null,"notes":"Exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids, so lysine leaves the cell.","entity":null},{"dimension":"transport_pool","value_text":"the enterocyte interior","comparator":null,"unit":null,"notes":"Exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids, so lysine leaves the cell.","entity":null}],"evidence":[{"id":"6cadef0b-846e-57bb-9305-e7a0d736a9d9","evidence_kind":"source_excerpt","locator":"Lines 34-42","start_line":34,"end_line":42,"excerpt":"### basolateral-lysine-exchange\nSLC7A7-SLC3A2 exchanges intracellular cationic amino acids including lysine for extracellular neutral amino acids with sodium.\nPlain language: This route helps lysine leave epithelial cells toward blood.\nCondition category: normal\norganism: Homo sapiens\ntissue_or_cell_type: Basolateral intestinal and renal epithelial membranes\nexperimental_model: Human/mouse heterodimer expression and exchange assays\nlimitations: Neutral-substrate transport is sodium-dependent; lysine binding itself should not be mislabeled a sodium cotransport step.\n[pfeiffer1999yl] Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. (1999). https://pubmed.ncbi.nlm.nih.gov/9878049/ DOI: 10.1093/emboj/18.1.49","model_system":"Human/mouse heterodimer expression and exchange assays","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact quote from the accompanying curation document, not from publisher text. Original study references: [pfeiffer1999yl] Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family. (1999). https://pubmed.ncbi.nlm.nih.gov/9878049/ DOI: 10.1093/emboj/18.1.49","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"7633bde7-dcc9-5086-91c6-a45eb96857f3","stable_key":"import-c3df3634-4c3a-5099-a5d9-e4f6344c1084","title":"L-Lysine: mechanism-first literature curation (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. 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