Component

Human methylthioadenosine phosphorylase / MTAP

Context-specific entity; species, compartment and exposure are stated on each claim.

3 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. MTAP loss caused methylthioadenosine accumulation in the study cancer-cell systems, identifying salvage failure as a change in the intracellular metabolite environment.

    Human methylthioadenosine phosphorylase / MTAP → 5′-Methylthioadenosine source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human cancer-cell shRNA/metabolomics and biochemical profiling.
    limitations
    Extracellular stromal clearance and in-vivo exposure can differ from isolated culture.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A product of polyamine synthesis must be recycled or removed.
    primary_references
    MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 284–290

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell shRNA/metabolomics and biochemical profiling. · source_derived_draft · unverified_draft

    ## methionine-mtap-salvage A product of polyamine synthesis must be recycled or removed. MTAP loss caused methylthioadenosine accumulation in the study cancer-cell systems, identifying salvage failure as a change in the intracellular metabolite environment. Model: Human cancer-cell shRNA/metabolomics and biochemical profiling. Limitations: Extracellular stromal clearance and in-vivo exposure can differ from isolated culture. Evidence access: Primary abstract MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. MAT2A depletion preferentially reduced growth and PRMT5 methylation activity in MTAP-deleted cells.

    Human methionine adenosyltransferase 2A / MAT2A → Human protein arginine methyltransferase 5 / PRMT5 source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human cancer-cell genetic depletion experiments.
    limitations
    This genetic interaction is not proof of efficacy for methionine restriction or a particular drug in patients.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Loss of a recycling enzyme can make cells more sensitive to reduced donor synthesis.
    primary_references
    MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 300–306

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell genetic depletion experiments. · source_derived_draft · unverified_draft

    ## methionine-mat2a-prmt5-vulnerability Loss of a recycling enzyme can make cells more sensitive to reduced donor synthesis. MAT2A depletion preferentially reduced growth and PRMT5 methylation activity in MTAP-deleted cells. Model: Human cancer-cell genetic depletion experiments. Limitations: This genetic interaction is not proof of efficacy for methionine restriction or a particular drug in patients. Evidence access: Primary abstract MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    Complete structured claim and evidence

  2. Biochemical methyltransferase profiling identified MTA as a potent selective PRMT5 inhibitor; MTAP-deleted cells had reduced PRMT5 methylation activity.

    5′-Methylthioadenosine → Human protein arginine methyltransferase 5 / PRMT5 source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human cancer-cell and purified-enzyme study.
    limitations
    Selectivity applies to the tested panel and conditions; not all methyltransferases.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A recycling product can inhibit another methylation enzyme.
    primary_references
    MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 292–298

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human cancer-cell and purified-enzyme study. · source_derived_draft · unverified_draft

    ## methionine-mta-prmt5 A recycling product can inhibit another methylation enzyme. Biochemical methyltransferase profiling identified MTA as a potent selective PRMT5 inhibitor; MTAP-deleted cells had reduced PRMT5 methylation activity. Model: Human cancer-cell and purified-enzyme study. Limitations: Selectivity applies to the tested panel and conditions; not all methyltransferases. Evidence access: Primary abstract MTAP Deletions in Cancer Create Vulnerability to Targeting of the MAT2A/PRMT5/RIOK1 Axis. · 2016 · https://pubmed.ncbi.nlm.nih.gov/27068473/ · DOI 10.1016/j.celrep.2016.03.043
    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