Component
Human MRS2 homopentamer
Five human MRS2 subunits surrounding a central channel pore.
2 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.
Other things that act on it
Enzymes, hormones, genes, and other components with a recorded effect. These are not nutrients, so they do not count toward the arrows above. Each finding names the chapter that recorded it.
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.
What acts on it
Cryo-EM resolved human MRS2 as a homopentamer surrounding a central pore.
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)
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
The events it takes part in
A mechanism often involves more than two components. These are the full events, with every participant and its role.
Situations it appears in
Low-supply and faulty-machinery situations recorded in the chapters where this component plays a part.
In the sources
Preserved passages that mention this component, quoted exactly. Open one to read it in context.
Open hypotheses
Proposed ideas that involve this component. They are labeled as hypotheses and do not change any recorded statement.
This is a research prototype built from draft material. It is not medical advice, and its statements still await verification against the original studies.