Component

PTEN (human phosphatase and tensin homolog)

PTEN (human phosphatase and tensin homolog). Species, exposure and limitations are retained in each linked claim.

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

Read recorded mechanisms Open recursive mind map

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 it acts on

  1. Human PTEN removed the 3-phosphate from PI(3,4,5)P3, forming PI(4,5)P2.

    PTEN (human phosphatase and tensin homolog) → Phosphatidylinositol 3,4,5-trisphosphate (PIP3) source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/9593664.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248", "start_char": 0, "end_char": 1012, "text_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248"}
    experimental_model
    Phosphatase assays and human cell expression
    exposure
    Wild-type versus catalytic-mutant PTEN
    limitations
    Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human protein and HEK293 cells
    plain_language
    A phosphatase reverses a signaling-lipid phosphorylation step.
    primary_references
    [ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375
    tissue_or_cell_type
    Purified enzyme and cultured cells

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 717–728

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Phosphatase assays and human cell expression · source_derived_draft · unverified_draft

    ### ino-pten-pip3 Human PTEN removed the 3-phosphate from PI(3,4,5)P3, forming PI(4,5)P2. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A phosphatase reverses a signaling-lipid phosphorylation step. organism: Human protein and HEK293 cells tissue_or_cell_type: Purified enzyme and cultured cells experimental_model: Phosphatase assays and human cell expression limitations: Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN. exposure: Wild-type versus catalytic-mutant PTEN evidence_span: {"source_cache": "artifacts/inositol-research/9593664.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248", "start_char": 0, "end_char": 1012, "text_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248"} [ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375
    Complete structured claim and evidence

  2. PTEN also showed 3-phosphatase activity toward soluble inositol 1,3,4,5-tetrakisphosphate.

    PTEN (human phosphatase and tensin homolog) → Inositol 1,3,4,5-tetrakisphosphate source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/inositol-research/9593664.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248", "start_char": 0, "end_char": 1012, "text_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248"}
    experimental_model
    Phosphatase assays and human cell expression
    exposure
    Wild-type versus catalytic-mutant PTEN
    limitations
    Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN.
    nutrient_topic
    Inositol research collection; topical membership is not evidence of a direct dietary effect. · Inositol (stereoisomer family)
    organism
    Human protein and HEK293 cells
    plain_language
    A related phosphate-removal reaction was observed on a soluble molecule.
    primary_references
    [ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375
    tissue_or_cell_type
    Purified enzyme and cultured cells

    Inositol: synthesis, signaling, mineral interactions and conditional deficiency (2026-09-17) · lines 730–741

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Phosphatase assays and human cell expression · source_derived_draft · unverified_draft

    ### ino-pten-soluble PTEN also showed 3-phosphatase activity toward soluble inositol 1,3,4,5-tetrakisphosphate. Condition category: normal nutrient_topic: Inositol research collection; topical membership is not evidence of a direct dietary effect. plain_language: A related phosphate-removal reaction was observed on a soluble molecule. organism: Human protein and HEK293 cells tissue_or_cell_type: Purified enzyme and cultured cells experimental_model: Phosphatase assays and human cell expression limitations: Cellular overexpression and enzymology do not imply that inositol supplements activate PTEN. exposure: Wild-type versus catalytic-mutant PTEN evidence_span: {"source_cache": "artifacts/inositol-research/9593664.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248", "start_char": 0, "end_char": 1012, "text_sha256": "118dd3dacb2fa7be09cb0258dd0f6de1193cf2553142c94a5750d82c5f00a248"} [ino-p9593664] The tumor suppressor, PTEN/MMAC1, dephosphorylates the lipid second messenger, phosphatidylinositol 3,4,5-trisphosphate. (1998). https://pubmed.ncbi.nlm.nih.gov/9593664/ DOI: 10.1074/jbc.273.22.13375
    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