{"id":"f75da1cc-0cd5-54af-a62a-ffa611db1ccf","stable_key":"e0ea2d6a-7429-5e9f-b774-41e5e3288da3:e-sig-alpha-pkc-ps-association","predicate":"enhances","statement":"Adding 1 mol% alpha-tocopherol enhanced isolated PKC alpha C2-domain association with phosphatidylserine-containing lipid surfaces by surface plasmon resonance. Tocopherol without phosphatidylserine did not support binding.","claim_class":"mechanistic","status":"source_derived_draft","evidence_grade":"ungraded","direction":"positive","is_public":true,"mechanism_event_id":"d7c46e44-318c-5894-812b-677fe6bd723d","mechanism_event_label":"Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine.","subject":{"id":"ae6048a7-d112-5d3a-8e7c-ad5a152642f9","slug":"rrr-alpha-tocopherol","display_name":"RRR-alpha-tocopherol","entity_type_key":"small_molecule"},"object":{"id":"6e1d6bb0-5403-5d17-8dc2-87ce356b60e4","slug":"pkca-c2-ps-membrane-association","display_name":"PKC alpha C2-domain association with phosphatidylserine membranes","entity_type_key":"cellular_process"},"evidence_count":1,"mechanism_event":{"id":"d7c46e44-318c-5894-812b-677fe6bd723d","stable_key":"e0ea2d6a-7429-5e9f-b774-41e5e3288da3:e-sig-alpha-pkc-ps-association-event","event_type":"biochemical_relationship","label":"Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine.","description":"Adding 1 mol% alpha-tocopherol enhanced isolated PKC alpha C2-domain association with phosphatidylserine-containing lipid surfaces by surface plasmon resonance. Tocopherol without phosphatidylserine did not support binding.","status":"provisional","compartment":null,"participants":[{"entity":{"id":"0e2dd859-6135-556e-938f-d177f1e8c1ad","slug":"phosphatidylserine","display_name":"Phosphatidylserine","entity_type_key":"lipid"},"role":"required membrane lipid","stoichiometry":null,"state_label":"","sequence_order":0,"notes":""},{"entity":{"id":"ae6048a7-d112-5d3a-8e7c-ad5a152642f9","slug":"rrr-alpha-tocopherol","display_name":"RRR-alpha-tocopherol","entity_type_key":"small_molecule"},"role":"subject","stoichiometry":null,"state_label":"","sequence_order":1,"notes":""},{"entity":{"id":"6e1d6bb0-5403-5d17-8dc2-87ce356b60e4","slug":"pkca-c2-ps-membrane-association","display_name":"PKC alpha C2-domain association with phosphatidylserine membranes","entity_type_key":"cellular_process"},"role":"target","stoichiometry":null,"state_label":"","sequence_order":2,"notes":""}]},"contexts":[{"dimension":"cross_nutrient","value_text":"false","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"experimental_model","value_text":"Surface plasmon resonance with recombinant C2 domain and lipid vesicles","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"exposure","value_text":"Base lipid composition 70:20:10 mol%; alpha-tocopherol at 1 mol% replacing POPC; no-PS control had 10 mol% tocopherol.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"limitations","value_text":"A membrane association endpoint is distinct from kinase activation. No direct C2-domain binding to free tocopherol is claimed.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"nutrient_topic","value_text":"Vitamin E research collection; topical membership is not evidence of a direct dietary effect.","comparator":null,"unit":null,"notes":"","entity":{"slug":"vitamin-e","display_name":"Vitamin E","entity_type_key":"chemical_species"}},{"dimension":"organism","value_text":"Recombinant construct; species not independently stated","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"plain_language","value_text":"Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine.","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"primary_references","value_text":"[mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318","comparator":null,"unit":null,"notes":"","entity":null},{"dimension":"tissue_or_cell_type","value_text":"Artificial POPC/POPE/POPS membrane","comparator":null,"unit":null,"notes":"","entity":null}],"evidence":[{"id":"5902c4cf-bdd5-5bd4-b2ce-6a69f7bb40f0","evidence_kind":"source_excerpt","locator":"Lines 998-1009","start_line":998,"end_line":1009,"excerpt":"### e-sig-alpha-pkc-ps-association\nAdding 1 mol% alpha-tocopherol enhanced isolated PKC alpha C2-domain association with phosphatidylserine-containing lipid surfaces by surface plasmon resonance. Tocopherol without phosphatidylserine did not support binding.\nCondition category: normal\nnutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect.\nplain_language: Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine.\norganism: Recombinant construct; species not independently stated\ntissue_or_cell_type: Artificial POPC/POPE/POPS membrane\nexperimental_model: Surface plasmon resonance with recombinant C2 domain and lipid vesicles\nlimitations: A membrane association endpoint is distinct from kinase activation. No direct C2-domain binding to free tocopherol is claimed.\nexposure: Base lipid composition 70:20:10 mol%; alpha-tocopherol at 1 mol% replacing POPC; no-PS control had 10 mol% tocopherol.\ncross_nutrient: false\n[mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318","model_system":"Surface plasmon resonance with recombinant C2 domain and lipid vesicles","directness":"author_interpretation","verification_status":"source_derived_draft","notes":"Exact curation-document quotation, not publisher quotation. Study references: [mccary2012] Vitamin E isoforms directly bind PKCα and differentially regulate activation of PKCα. (2012). https://pubmed.ncbi.nlm.nih.gov/21933153/ DOI: 10.1042/bj20111318","relationship":"supports","weight":1.0,"link_notes":"","source":{"id":"3ac41dba-4727-5116-a556-ac3bbb0dc41c","stable_key":"import-e0ea2d6a-7429-5e9f-b774-41e5e3288da3","title":"Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17)","document_type":"imported_text","citation_label":"AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text.","file_path":"","sha256":"a90b6565e092c6a2da07f74cf758792c2cf63b40746260c8ff12bd64322c36f4","revision_id":"956793d1-23e4-5397-9291-25c1732a8e02","review_status":"unverified_draft","notes":""}}],"relations":[],"conflicts":[],"corrections":[],"research":null}