Component

Human mitochondrial MRS2

Human inner-mitochondrial-membrane channel protein.

3 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 it acts on

  1. MRS2 overexpression increased Mg uptake into HEK293F-derived mitochondria.

    Experimental context and source evidence
    evidence-system
    Isolated mitochondria from MRS2-overexpressing cells
    experimental_model
    Isolated mitochondria from MRS2-overexpressing cells
    limitations
    Uptake assay is not an intervention on dietary magnesium.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Human
    plain_language
    More MRS2 increased magnesium entry into the mitochondrial compartment.
    primary_references
    [human-mrs2-2023-permeation] Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel (2023). https://www.nature.com/articles/s41467-023-40516-2 DOI: 10.1038/s41467-023-40516-2
    tissue
    HEK293F-derived mitochondria
    tissue_or_cell_type
    HEK293F-derived mitochondria
    transport_direction
    Intermembrane-space side toward matrix.

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 1221–1233

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Isolated mitochondria from MRS2-overexpressing cells · source_derived_draft · unverified_draft

    ### human-mrs2-magnesium-uptake MRS2 overexpression increased Mg uptake into HEK293F-derived mitochondria. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: More MRS2 increased magnesium entry into the mitochondrial compartment. organism: Human tissue_or_cell_type: HEK293F-derived mitochondria experimental_model: Isolated mitochondria from MRS2-overexpressing cells limitations: Uptake assay is not an intervention on dietary magnesium. transport_direction: Intermembrane-space side toward matrix. evidence-system: Isolated mitochondria from MRS2-overexpressing cells tissue: HEK293F-derived mitochondria [human-mrs2-2023-permeation] Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel (2023). https://www.nature.com/articles/s41467-023-40516-2 DOI: 10.1038/s41467-023-40516-2
    Complete structured claim and evidence
  2. Cryo-EM resolved human MRS2 as a homopentamer surrounding a central pore.

    Human mitochondrial MRS2 → Human MRS2 homopentamer source_derived_draftungraded
    Experimental context and source evidence
    evidence-system
    Purified recombinant human MRS2 cryo-EM
    experimental_model
    Purified recombinant human MRS2 cryo-EM
    limitations
    Structure alone does not establish every gating transition or physiological selectivity.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Human protein
    plain_language
    Five MRS2 subunits form the mitochondrial ion-conduction architecture.
    primary_references
    [human-mrs2-2023-permeation] Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel (2023). https://www.nature.com/articles/s41467-023-40516-2 DOI: 10.1038/s41467-023-40516-2
    tissue
    Protein purified from HEK293F expression
    tissue_or_cell_type
    Protein purified from HEK293F expression

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 1208–1219

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Purified recombinant human MRS2 cryo-EM · source_derived_draft · unverified_draft

    ### human-mrs2-pentamer Cryo-EM resolved human MRS2 as a homopentamer surrounding a central pore. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: Five MRS2 subunits form the mitochondrial ion-conduction architecture. organism: Human protein tissue_or_cell_type: Protein purified from HEK293F expression experimental_model: Purified recombinant human MRS2 cryo-EM limitations: Structure alone does not establish every gating transition or physiological selectivity. evidence-system: Purified recombinant human MRS2 cryo-EM tissue: Protein purified from HEK293F expression [human-mrs2-2023-permeation] Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel (2023). https://www.nature.com/articles/s41467-023-40516-2 DOI: 10.1038/s41467-023-40516-2
    Complete structured claim and evidence

Where it participates (unsigned role)

  1. Dissipating membrane potential reduced Mg uptake in the human MRS2 mitochondrial assay.

    Experimental context and source evidence
    evidence-system
    FCCP or valinomycin exposure of isolated mitochondria
    experimental_model
    FCCP or valinomycin exposure of isolated mitochondria
    limitations
    Pharmacological potential collapse can affect other mitochondrial properties; does not imply direct ATP hydrolysis by MRS2.
    nutrient_topic
    Magnesium research collection; topical membership is not evidence of a direct dietary effect. · Magnesium
    organism
    Human
    plain_language
    The inner membrane electrical gradient helps drive magnesium into mitochondria.
    primary_references
    [human-mrs2-2023-permeation] Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel (2023). https://www.nature.com/articles/s41467-023-40516-2 DOI: 10.1038/s41467-023-40516-2
    tissue
    HEK293F-derived mitochondria
    tissue_or_cell_type
    HEK293F-derived mitochondria

    Magnesium: cross-nutrient mechanisms and deficiency (2026-09-17) · lines 1235–1246

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · FCCP or valinomycin exposure of isolated mitochondria · source_derived_draft · unverified_draft

    ### mitochondrial-potential-supports-mrs2-uptake Dissipating membrane potential reduced Mg uptake in the human MRS2 mitochondrial assay. Condition category: normal nutrient_topic: Magnesium research collection; topical membership is not evidence of a direct dietary effect. plain_language: The inner membrane electrical gradient helps drive magnesium into mitochondria. organism: Human tissue_or_cell_type: HEK293F-derived mitochondria experimental_model: FCCP or valinomycin exposure of isolated mitochondria limitations: Pharmacological potential collapse can affect other mitochondrial properties; does not imply direct ATP hydrolysis by MRS2. evidence-system: FCCP or valinomycin exposure of isolated mitochondria tissue: HEK293F-derived mitochondria [human-mrs2-2023-permeation] Molecular basis of Mg2+ permeation through the human mitochondrial Mrs2 channel (2023). https://www.nature.com/articles/s41467-023-40516-2 DOI: 10.1038/s41467-023-40516-2
    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