Component

Mouse mitoferrin-1 / Slc25a37

Mouse mitoferrin-1 / Slc25a37. Species, exposure and limitations are retained in each linked claim.

4 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. Mitoferrin function was required for mitochondrial iron assimilation and heme synthesis in the tested vertebrate erythroblasts.

    Mouse mitoferrin-1 / Slc25a37 → Mitochondrial iron import source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/16511496.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234", "start_char": 0, "end_char": 1533, "text_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234"}
    experimental_model
    Zebrafish mutant, mouse stem-cell knockout and cross-species rescue
    exposure
    Mitoferrin loss and rescue
    limitations
    Species-specific loss/rescue evidence; no claim that plasma iron alone measures mitochondrial iron delivery.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Zebrafish, mice and yeast
    plain_language
    The final iron delivery step for heme synthesis is across the mitochondrial membrane.
    primary_references
    [iron-p16511496] Mitoferrin is essential for erythroid iron assimilation. (2006). https://pubmed.ncbi.nlm.nih.gov/16511496/ DOI: 10.1038/nature04512
    tissue_or_cell_type
    Developing erythroblasts and mitochondria

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 459–470

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Zebrafish mutant, mouse stem-cell knockout and cross-species rescue · source_derived_draft · unverified_draft

    ### iron-mitoferrin-import Mitoferrin function was required for mitochondrial iron assimilation and heme synthesis in the tested vertebrate erythroblasts. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: The final iron delivery step for heme synthesis is across the mitochondrial membrane. organism: Zebrafish, mice and yeast tissue_or_cell_type: Developing erythroblasts and mitochondria experimental_model: Zebrafish mutant, mouse stem-cell knockout and cross-species rescue limitations: Species-specific loss/rescue evidence; no claim that plasma iron alone measures mitochondrial iron delivery. exposure: Mitoferrin loss and rescue evidence_span: {"source_cache": "artifacts/iron-research/16511496.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234", "start_char": 0, "end_char": 1533, "text_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234"} [iron-p16511496] Mitoferrin is essential for erythroid iron assimilation. (2006). https://pubmed.ncbi.nlm.nih.gov/16511496/ DOI: 10.1038/nature04512
    Complete structured claim and evidence

  2. Mfrn-null mouse embryonic-stem-cell-derived erythroblasts arrested maturation and had severely impaired incorporation of iron-55 into heme.

    Mouse mitoferrin-1 / Slc25a37 → Erythroid heme synthesis source_derived_draftungraded
    Experimental context and source evidence
    availability_state
    machinery_impairment Imported condition classification; unverified.
    evidence_span
    {"source_cache": "artifacts/iron-research/16511496.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234", "start_char": 0, "end_char": 1533, "text_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234"}
    experimental_model
    Zebrafish mutant, mouse stem-cell knockout and cross-species rescue
    exposure
    Mitoferrin loss and rescue
    limitations
    Species-specific loss/rescue evidence; no claim that plasma iron alone measures mitochondrial iron delivery.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Zebrafish, mice and yeast
    plain_language
    Plenty of iron elsewhere would not replace this missing mitochondrial transport step.
    primary_references
    [iron-p16511496] Mitoferrin is essential for erythroid iron assimilation. (2006). https://pubmed.ncbi.nlm.nih.gov/16511496/ DOI: 10.1038/nature04512
    tissue_or_cell_type
    Developing erythroblasts and mitochondria
    trigger_kind
    machinery_impairment Imported condition classification; unverified.

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 472–483

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Zebrafish mutant, mouse stem-cell knockout and cross-species rescue · source_derived_draft · unverified_draft

    ### iron-mitoferrin-loss Mfrn-null mouse embryonic-stem-cell-derived erythroblasts arrested maturation and had severely impaired incorporation of iron-55 into heme. Condition category: machinery_impairment nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Plenty of iron elsewhere would not replace this missing mitochondrial transport step. organism: Zebrafish, mice and yeast tissue_or_cell_type: Developing erythroblasts and mitochondria experimental_model: Zebrafish mutant, mouse stem-cell knockout and cross-species rescue limitations: Species-specific loss/rescue evidence; no claim that plasma iron alone measures mitochondrial iron delivery. exposure: Mitoferrin loss and rescue evidence_span: {"source_cache": "artifacts/iron-research/16511496.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234", "start_char": 0, "end_char": 1533, "text_sha256": "cb2b06715c001133d1f1173d5084a2689170fa9a0e14f3b7b0a0cb5a7b6a5234"} [iron-p16511496] Mitoferrin is essential for erythroid iron assimilation. (2006). https://pubmed.ncbi.nlm.nih.gov/16511496/ DOI: 10.1038/nature04512
    Complete structured claim and evidence

What acts on it

  1. Abcb10 interacted with Mfrn1, enhanced its stability and promoted Mfrn1-dependent mitochondrial iron import.

    Mouse mitochondrial ABC transporter / Abcb10 → Mouse mitoferrin-1 / Slc25a37 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/19805291.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d513c833380932eae7a3667fae0e77d5bc7c03067c266e62438d8a63e3839955", "start_char": 0, "end_char": 1697, "text_sha256": "d513c833380932eae7a3667fae0e77d5bc7c03067c266e62438d8a63e3839955"}
    experimental_model
    Affinity purification, mass spectrometry and expression experiments
    exposure
    Abcb10/Mfrn1 expression during differentiation
    limitations
    Stabilization and transport were measured in cell systems, not supplementation experiments.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Mouse erythroleukemia cells and heterologous COS7 cells
    plain_language
    An interacting protein helps keep the iron importer available.
    primary_references
    [iron-p19805291] Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria. (2009). https://pubmed.ncbi.nlm.nih.gov/19805291/ DOI: 10.1073/pnas.0904519106
    tissue_or_cell_type
    Mitochondrial inner membrane

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 485–496

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Affinity purification, mass spectrometry and expression experiments · source_derived_draft · unverified_draft

    ### iron-abcb10-mitoferrin Abcb10 interacted with Mfrn1, enhanced its stability and promoted Mfrn1-dependent mitochondrial iron import. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: An interacting protein helps keep the iron importer available. organism: Mouse erythroleukemia cells and heterologous COS7 cells tissue_or_cell_type: Mitochondrial inner membrane experimental_model: Affinity purification, mass spectrometry and expression experiments limitations: Stabilization and transport were measured in cell systems, not supplementation experiments. exposure: Abcb10/Mfrn1 expression during differentiation evidence_span: {"source_cache": "artifacts/iron-research/19805291.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "d513c833380932eae7a3667fae0e77d5bc7c03067c266e62438d8a63e3839955", "start_char": 0, "end_char": 1697, "text_sha256": "d513c833380932eae7a3667fae0e77d5bc7c03067c266e62438d8a63e3839955"} [iron-p19805291] Abcb10 physically interacts with mitoferrin-1 (Slc25a37) to enhance its stability and function in the erythroid mitochondria. (2009). https://pubmed.ncbi.nlm.nih.gov/19805291/ DOI: 10.1073/pnas.0904519106
    Complete structured claim and evidence

  2. Fech interacted with both Mfrn1 and Abcb10 in the studied erythroid systems.

    Mouse ferrochelatase / Fech → Mouse mitoferrin-1 / Slc25a37 source_derived_draftungraded
    Experimental context and source evidence
    evidence_span
    {"source_cache": "artifacts/iron-research/20427704.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a4f3b1c37151557d4d888126ba888dd95391254c5e40d1c3576f0520eed7517c", "start_char": 0, "end_char": 1059, "text_sha256": "a4f3b1c37151557d4d888126ba888dd95391254c5e40d1c3576f0520eed7517c"}
    experimental_model
    Affinity purification and immunoprecipitation
    exposure
    Mfrn1, Abcb10 and Fech interaction analysis
    limitations
    Physical association supports coordination; direct substrate channeling was not separately proven.
    nutrient_topic
    Iron research collection; topical membership is not evidence of a direct dietary effect. · Iron
    organism
    Mouse erythroleukemia cells and heterologous HEK293 expression
    plain_language
    Iron import and the final heme-synthesis enzyme can be physically organized together.
    primary_references
    [iron-p20427704] Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis. (2010). https://pubmed.ncbi.nlm.nih.gov/20427704/ DOI: 10.1182/blood-2009-12-259614
    tissue_or_cell_type
    Mitochondrial heme-synthesis machinery

    Iron: absorption, trafficking, iron-dependent enzymes and nutrient interactions (2026-09-17) · lines 498–509

    AI-assisted literature curation; primary study URLs and scope retained in the document and extraction. Not publisher full text. · supports · Affinity purification and immunoprecipitation · source_derived_draft · unverified_draft

    ### iron-mitoferrin-fech-complex Fech interacted with both Mfrn1 and Abcb10 in the studied erythroid systems. Condition category: normal nutrient_topic: Iron research collection; topical membership is not evidence of a direct dietary effect. plain_language: Iron import and the final heme-synthesis enzyme can be physically organized together. organism: Mouse erythroleukemia cells and heterologous HEK293 expression tissue_or_cell_type: Mitochondrial heme-synthesis machinery experimental_model: Affinity purification and immunoprecipitation limitations: Physical association supports coordination; direct substrate channeling was not separately proven. exposure: Mfrn1, Abcb10 and Fech interaction analysis evidence_span: {"source_cache": "artifacts/iron-research/20427704.abstract.txt", "locator": "Exact primary indexed abstract; zero-based, end-exclusive Unicode character offsets", "file_sha256": "a4f3b1c37151557d4d888126ba888dd95391254c5e40d1c3576f0520eed7517c", "start_char": 0, "end_char": 1059, "text_sha256": "a4f3b1c37151557d4d888126ba888dd95391254c5e40d1c3576f0520eed7517c"} [iron-p20427704] Ferrochelatase forms an oligomeric complex with mitoferrin-1 and Abcb10 for erythroid heme biosynthesis. (2010). https://pubmed.ncbi.nlm.nih.gov/20427704/ DOI: 10.1182/blood-2009-12-259614
    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