{"id":"15cd2d8a-fbfb-50bf-b571-cc241838cafc","stable_key":"research:lrp8-variant-binds-selenop","predicate":"binds","statement":"An ApoER2 variant containing its O-linked glycosylation domain bound SELENOP with high affinity in the tested system.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"literature_reviewed:direct_experimental","direction":"neutral","is_public":true,"mechanism_event_id":"a4ce4195-6d5f-516e-a8a5-1481a2f6c6a4","mechanism_event_label":"A receptor variant improved SELENOP binding.","subject":{"id":"8d16c6b3-0027-5eba-83b7-74cbd8f8968f","slug":"lrp8-o-linked-domain-variant","display_name":"LRP8 variant containing the O-linked glycosylation domain","entity_type_key":"protein_state"},"object":{"id":"c7fbd153-6444-50b2-a8be-6936e352a11c","slug":"selenop","display_name":"SELENOP","entity_type_key":"protein"},"evidence_count":1,"mechanism_event":{"id":"a4ce4195-6d5f-516e-a8a5-1481a2f6c6a4","stable_key":"research:lrp8-variant-binds-selenop","event_type":"binding","label":"A receptor variant improved SELENOP binding.","description":"An ApoER2 variant containing its O-linked glycosylation domain bound SELENOP with high affinity in the tested system.","status":"active","compartment":{"slug":"plasma-membrane","display_name":"Plasma membrane"},"participants":[{"entity":{"id":"8d16c6b3-0027-5eba-83b7-74cbd8f8968f","slug":"lrp8-o-linked-domain-variant","display_name":"LRP8 variant containing the O-linked glycosylation domain","entity_type_key":"protein_state"},"role":"receptor","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"f47ee853-9252-56f4-8e2a-48ede17ed3a3","slug":"lrp8","display_name":"ApoER2 / LRP8","entity_type_key":"protein"},"role":"parent-protein","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"c7fbd153-6444-50b2-a8be-6936e352a11c","slug":"selenop","display_name":"SELENOP","entity_type_key":"protein"},"role":"ligand","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"cell_type","value_text":"Jurkat","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Receptor-variant assays","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"Do not generalize to all LRP8 variants.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"organism","value_text":"human","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"71bb3475-af37-50c1-ba43-650054105186","evidence_kind":"curated_literature_summary","locator":"lines 546-556","start_line":546,"end_line":556,"excerpt":"## lrp8-variant-binds-selenop\n\nA receptor variant improved SELENOP binding.\n\nAn ApoER2 variant containing its O-linked glycosylation domain bound SELENOP with high affinity in the tested system.\n\nOrganism: human\nCell type: Jurkat\nExperimental model: Receptor-variant assays\nLimitations: Do not generalize to all LRP8 variants.\nPrimary reference: [An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase](https://pubmed.ncbi.nlm.nih.gov/37406814/)","model_system":"Receptor-variant assays","directness":"author_interpretation","verification_status":"secondary_verified","notes":"Curated summary; inspect the linked primary papers for original methods and results.","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"4f892f13-06ea-5199-a33c-a703f35c80ae","stable_key":"selenium-research-2026-09-17","title":"Selenium: literature corrections and mechanism additions","document_type":"curated_literature_review","citation_label":"Metabolic Ledger literature curation, 17 September 2026; primary papers linked individually","file_path":"","sha256":"0b818b10c1c7120e5caf7f4d4019d7bd025d745692e424f515d3ef903c9ab7f3","revision_id":"80984e03-5f0f-5877-8094-afef7637444e","review_status":"secondary_verified","notes":"Secondary curated summaries of primary experiments, with explicit models and limitations. Not archived primary full text."}}],"relations":[],"conflicts":[],"corrections":[],"research":{"topic":"selenium-transport","plain_language":"A receptor variant improved SELENOP binding.","evidence_scope":"direct_experimental","papers":[{"key":"mizuno-2023-lrp8-routing","title":"An efficient selenium transport pathway of selenoprotein P utilizing a high-affinity ApoER2 receptor variant and being independent of selenocysteine lyase","url":"https://pubmed.ncbi.nlm.nih.gov/37406814/","doi":"10.1016/j.jbc.2023.105009","year":2023,"model":"Human Jurkat and RD cells","summary":"Receptor variants and vesicle processing differ between cell lines; SCLY dependence is not universal."}]}}