Component

PKC alpha C2-domain association with phosphatidylserine membranes

Assay endpoint for isolated recombinant PKC alpha C2 domain binding to lipid vesicles.

1 recorded relationships. Experimental role, claim status and evidence remain attached to each record.

How nutrients influence it

Every nutrient with a recorded effect on this component, credited to the nutrient that acted rather than the chapter that recorded it. Open a nutrient to see the findings and the conditions they were measured under.

How nutrients reach it in more than one step

Chains of two or more recorded steps that end here, grouped by the nutrient they start from. Each step is a separate finding, so a chain is a route a mechanism could take, not proof that it does.

Tracing routes…

What it does

Every recorded relationship this component is part of, grouped by its role. Plain wording comes first; the technical statement follows.

Recorded relationships

What acts on it

  1. 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.

    Experimental context and source evidence
    cross_nutrient
    false
    experimental_model
    Surface plasmon resonance with recombinant C2 domain and lipid vesicles
    exposure
    Base lipid composition 70:20:10 mol%; alpha-tocopherol at 1 mol% replacing POPC; no-PS control had 10 mol% tocopherol.
    limitations
    A membrane association endpoint is distinct from kinase activation. No direct C2-domain binding to free tocopherol is claimed.
    nutrient_topic
    Vitamin E research collection; topical membership is not evidence of a direct dietary effect. · Vitamin E
    organism
    Recombinant construct; species not independently stated
    plain_language
    Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine.
    primary_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
    tissue_or_cell_type
    Artificial POPC/POPE/POPS membrane

    Vitamin E: transport, membrane protection and nutrient interactions (2026-09-17) · lines 998–1009

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Surface plasmon resonance with recombinant C2 domain and lipid vesicles · source_derived_draft · unverified_draft

    ### e-sig-alpha-pkc-ps-association 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. Condition category: normal nutrient_topic: Vitamin E research collection; topical membership is not evidence of a direct dietary effect. plain_language: Alpha-tocopherol changed how the kinase’s membrane-binding domain associated with a membrane containing phosphatidylserine. organism: Recombinant construct; species not independently stated tissue_or_cell_type: Artificial POPC/POPE/POPS membrane experimental_model: Surface plasmon resonance with recombinant C2 domain and lipid vesicles limitations: A membrane association endpoint is distinct from kinase activation. No direct C2-domain binding to free tocopherol is claimed. exposure: Base lipid composition 70:20:10 mol%; alpha-tocopherol at 1 mol% replacing POPC; no-PS control had 10 mol% tocopherol. cross_nutrient: false [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
    Complete structured claim and evidence

In the sources

Preserved passages that mention this component, quoted exactly. Open one to read it in context.

    This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.

    Evidence, AI assistance and curation standards