ArticleProceedings of the National Academy of Sciences of the United States of America2008
Structure of the membrane proximal oxidoreductase domain of human Steap3, the dominant ferrireductase of the erythroid transferrin cycle.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 61 papers.
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Who cites it
61 citing papers in PubMed, 134 citations in OpenAlex.
- Acidosis, Iron Dyshomeostasis and Inflammatory Injury.International journal of molecular sciences · 2026Review
- Regulation of mitochondrial iron homeostasis in tumor cells.Molecular medicine (Cambridge, Mass.) · 2026Review
- Crosstalk between ferroptosis and extracellular vesicles in cancer: from interaction to clinical application.Experimental hematology & oncology · 2026Review
- Targeting Ferroptosis in Sepsis: Therapeutic Potential and Mechanisms of Natural Products and Traditional Chinese Medicine.Journal of inflammation research · 2026Review
- Ferroptosis in Diabetic Cardiomyopathy and Atherosclerosis: Mechanisms and Clinical Prospects.International journal of molecular sciences · 2025Review
- STEAP3 promotes triple-negative breast cancer growth through the FGFR1-mediated activation of PI3K/AKT/mTOR signaling.iScience · 2025Article
- Article
- The Role and Mechanisms of Ubiquitin-Proteasome System-Mediated Ferroptosis in Neurological Disorders.Neuroscience bulletin · 2025Review
- Research progress of macrophage ferroptosis in inflammatory bowel disease and inflammation-cancer transformation.Frontiers in immunology · 2025Review
- Artemisinin derivatives modulate KEAP1-NRF2-xCT pathway to alleviate Sjögren's disease: insights from scRNA-seq and systems biology.Frontiers in immunology · 2025Article
- Role of autophagy and ferroptosis in the development of endometriotic cysts (Review).International journal of molecular medicine · 2024Review
- Unveiling the hidden dangers: a review of non-apoptotic programmed cell death in anesthetic-induced developmental neurotoxicity.Cell biology and toxicology · 2024Review
- Mechanism of ferroptosis regulating ischemic stroke and pharmacologically inhibiting ferroptosis in treatment of ischemic stroke.CNS neuroscience & therapeutics · 2024Review
- Sperm freezing damage: the role of regulated cell death.Cell death discovery · 2024Review
- Naodesheng Pills Ameliorate Cerebral Ischemia Reperfusion-Induced Ferroptosis via Inhibition of the ERK1/2 Signaling Pathway.Drug design, development and therapy · 2024Article
- A detailed overview of quercetin: implications for cell death and liver fibrosis mechanisms.Frontiers in pharmacology · 2024Review
- Targeting ferroptosis as a potential strategy to overcome the resistance of cisplatin in oral squamous cell carcinoma.Frontiers in pharmacology · 2024Review
- Molecular therapy of cardiac ischemia-reperfusion injury based on mitochondria and ferroptosis.Journal of molecular medicine (Berlin, Germany) · 2023Review
- Autophagy mediates an amplification loop during ferroptosis.Cell death & disease · 2023Review
- Relationship between ferroptosis and mitophagy in cardiac ischemia reperfusion injury: a mini-review.PeerJ · 2023Review
1 more citing papers are in PubMed but not listed here.
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The daily production of 200 billion erythrocytes requires 20 mg of iron, accounting for nearly 80% of the iron demand in humans. Thus, erythroid precursor cells possess an efficient mechanism for iron uptake in which iron loaded transferrin (Tf) binds to the transferrin receptor (TfR) at the cell surface. The Tf:TfR complex then enters the endosome via receptor-mediated endocytosis. Upon endosomal acidification, iron is released from Tf, reduced to Fe(2+) by Steap3, and transported across the endosomal membrane by divalent metal iron transporter 1. Steap3, the major ferrireductase in erythrocyte endosomes, is a member of a unique family of reductases. Steap3 is comprised of an N-terminal cytosolic oxidoreductase domain and a C-terminal heme-containing transmembrane domain. Cytosolic NADPH and a flavin are predicted cofactors, but the NADPH/flavin binding domain differs significantly from those in other eukaryotic reductases. Instead, Steap3 shows remarkable, although limited homology to FNO, an archaeal oxidoreductase. We have determined the crystal structure of the human Steap3 oxidoreductase domain in the absence and presence of NADPH. The structure reveals an FNO-like domain with an unexpected dimer interface and substrate binding sites that are well positioned to direct electron transfer from the cytosol to a heme moiety predicted to be fixed within the transmembrane domain. Here, we discuss possible gating mechanisms for electron transfer across the endosomal membrane.
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