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New molecular components of high and low affinity iron import systems in Drosophila

Author

Listed:
  • Sattar Soltani

    (University of Alberta)

  • Minyi Yan

    (University of Alberta)

  • Qingxuan Yu

    (University of Alberta)

  • Areeg Abd Elhafiz

    (University of Alberta)

  • Erika Pfriem

    (University of Alberta)

  • Samuel M. Webb

    (SLAC National Accelerator Laboratory)

  • Thomas Kroll

    (SLAC National Accelerator Laboratory)

  • Jahir Marceliano Bahena Lopez

    (Centro de Investigación y de Estudios Avanzados (Cinvestav))

  • Fanis Missirlis

    (Centro de Investigación y de Estudios Avanzados (Cinvestav))

  • Kirst King-Jones

    (University of Alberta)

Abstract

The high abundance and molecular versatility of iron have led to its universal presence in biological systems, yet its absorption is exceptionally challenging. Animals and yeasts use divalent metal transporters to import iron, but yeasts also employ the multicopper oxidase Fet3p for high-affinity iron uptake when iron-starved. Using long-term iron depletion in Drosophila, we identified four components involved in iron absorption: Multicopper oxidase-4 (Mco4), a Fet3p ortholog, is essential for surviving iron starvation, whereas the cytochrome b561 enzymes Fire (Ferric Iron Reductase) and Fire-like, as well as cytochrome b5 protein Firewood, are required for iron absorption under normal conditions. This study reports the presence of a high-affinity iron uptake system in an animal, a cytochrome b5 electron donor for ferric iron reduction, and intestinal ferric reductases, and provides a valuable resource for further exploration of genes involved in iron homeostasis, transport, and absorption.

Suggested Citation

  • Sattar Soltani & Minyi Yan & Qingxuan Yu & Areeg Abd Elhafiz & Erika Pfriem & Samuel M. Webb & Thomas Kroll & Jahir Marceliano Bahena Lopez & Fanis Missirlis & Kirst King-Jones, 2025. "New molecular components of high and low affinity iron import systems in Drosophila," Nature Communications, Nature, vol. 16(1), pages 1-22, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-60758-6
    DOI: 10.1038/s41467-025-60758-6
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    References listed on IDEAS

    as
    1. Roland Lill, 2009. "Function and biogenesis of iron–sulphur proteins," Nature, Nature, vol. 460(7257), pages 831-838, August.
    2. Nhan Huynh & Qiuxiang Ou & Pendleton Cox & Roland Lill & Kirst King-Jones, 2019. "Glycogen branching enzyme controls cellular iron homeostasis via Iron Regulatory Protein 1 and mitoNEET," Nature Communications, Nature, vol. 10(1), pages 1-18, December.
    3. Sattar Soltani & Samuel M. Webb & Thomas Kroll & Kirst King-Jones, 2024. "Drosophila Evi5 is a critical regulator of intracellular iron transport via transferrin and ferritin interactions," Nature Communications, Nature, vol. 15(1), pages 1-20, December.
    Full references (including those not matched with items on IDEAS)

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