Component

Human mitochondrial SAM transporter / SLC25A26

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. SLC25A26 mutations were associated with impaired CoQ10 and lipoic-acid biosynthesis in the functional study.

    Human mitochondrial SAM transporter / SLC25A26 → CoQ10 and lipoate biosynthesis in the SLC25A26 study source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human mitochondrial disease study and functional models.
    limitations
    This does not demonstrate that oral methionine, SAM, CoQ10 or lipoate repairs the transporter.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    One transport gate connects methyl-donor supply with other cofactors.
    primary_references
    Intra-mitochondrial Methylation Deficiency Due to Mutations in SLC25A26. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26522469/ · DOI 10.1016/j.ajhg.2015.09.013
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 124–130

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human mitochondrial disease study and functional models. · source_derived_draft · unverified_draft

    ## methionine-mitochondrial-cofactor-products One transport gate connects methyl-donor supply with other cofactors. SLC25A26 mutations were associated with impaired CoQ10 and lipoic-acid biosynthesis in the functional study. Model: Human mitochondrial disease study and functional models. Limitations: This does not demonstrate that oral methionine, SAM, CoQ10 or lipoate repairs the transporter. Evidence access: Primary abstract Intra-mitochondrial Methylation Deficiency Due to Mutations in SLC25A26. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26522469/ · DOI 10.1016/j.ajhg.2015.09.013
    Complete structured claim and evidence

  2. Human SLC25A26 imports cytosol-derived SAM into mitochondria for intramitochondrial methylation.

    Human mitochondrial SAM transporter / SLC25A26 → S-Adenosyl-L-methionine source_derived_draftungraded
    Experimental context and source evidence
    evidence_access
    Primary abstract
    experimental_model
    Human transporter-variant study with functional assays.
    limitations
    Transporter role and disease consequences are separately recorded.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    Making SAM outside mitochondria is not enough; it must reach the organelle.
    primary_references
    Intra-mitochondrial Methylation Deficiency Due to Mutations in SLC25A26. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26522469/ · DOI 10.1016/j.ajhg.2015.09.013
    transport_effect
    raises Recorded as import of cytosol-derived SAM into mitochondria.
    transport_pool
    the mitochondrial matrix Recorded as import of cytosol-derived SAM into mitochondria.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 108–114

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human transporter-variant study with functional assays. · source_derived_draft · unverified_draft

    ## methionine-mitochondrial-sam-entry Making SAM outside mitochondria is not enough; it must reach the organelle. Human SLC25A26 imports cytosol-derived SAM into mitochondria for intramitochondrial methylation. Model: Human transporter-variant study with functional assays. Limitations: Transporter role and disease consequences are separately recorded. Evidence access: Primary abstract Intra-mitochondrial Methylation Deficiency Due to Mutations in SLC25A26. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26522469/ · DOI 10.1016/j.ajhg.2015.09.013
    Complete structured claim and evidence

  3. Recessive SLC25A26 variants impaired mitochondrial methylation with defects in RNA stability, protein modification and translation.

    Human mitochondrial SAM transporter / SLC25A26 → Mitochondrial methylation and translation in SLC25A26 disease source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_access
    Primary abstract
    experimental_model
    Human families and cellular/functional variant studies.
    limitations
    Phenotypes varied; no general SAM or methionine supplement rescue is established.
    nutrient_topic
    L-Methionine collection; species, compartment, exposure, co-substrates and manipulation remain explicit. · L-Methionine
    plain_language
    A compartment-specific shortage can occur without proving a dietary shortage.
    primary_references
    Intra-mitochondrial Methylation Deficiency Due to Mutations in SLC25A26. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26522469/ · DOI 10.1016/j.ajhg.2015.09.013
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    L-Methionine: transport, methylation, sulfur metabolism and cross-nutrient mechanisms (2026-09-19) · lines 116–122

    AI-assisted research curation; primary references, access levels and experimental limitations individually identified. Not publisher full text. · supports · Human families and cellular/functional variant studies. · source_derived_draft · unverified_draft

    ## methionine-mitochondrial-sam-loss A compartment-specific shortage can occur without proving a dietary shortage. Recessive SLC25A26 variants impaired mitochondrial methylation with defects in RNA stability, protein modification and translation. Model: Human families and cellular/functional variant studies. Limitations: Phenotypes varied; no general SAM or methionine supplement rescue is established. Evidence access: Primary abstract Intra-mitochondrial Methylation Deficiency Due to Mutations in SLC25A26. · 2015 · https://pubmed.ncbi.nlm.nih.gov/26522469/ · DOI 10.1016/j.ajhg.2015.09.013
    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