Cited by 625Iron Metabolism and DisordersMitochondrial Function and PathologyHemoglobin structure and function

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Mitoferrin is essential for erythroid iron assimilation

Shaw, George C., Cope, John J., Li, Liangtao, Corson, Kenneth, Hersey, Candace, Ackermann, Gabriele E., Gwynn, Babette, Lambert, Amy J., Wingert, Rebecca A., Traver, David, Trede, Nikolaus S., Barut, Bruce A., Zhou, Yi, Minet, Emmanuel, Donovan, Adriana, Brownlie, Alison, Balzan, Rena, Weiss, Mitchell J., Peters, Luanne L., Kaplan, Jerry, Zon, Leonard I., Paw, Barry H.·2006·Nature

DOI 10.1038/nature04512

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Abstract

Iron has a fundamental role in many metabolic processes, including electron transport, deoxyribonucleotide synthesis, oxygen transport and many essential redox reactions involving haemoproteins and Fe-S cluster proteins. Defective iron homeostasis results in either iron deficiency or iron overload. Precise regulation of iron transport in mitochondria is essential for haem biosynthesis, haemoglobin production and Fe-S cluster protein assembly during red cell development. Here we describe a zebrafish mutant, frascati (frs), that shows profound hypochromic anaemia and erythroid maturation arrest owing to defects in mitochondrial iron uptake. Through positional cloning, we show that the gene mutated in the frs mutant is a member of the vertebrate mitochondrial solute carrier family (SLC25) that we call mitoferrin (mfrn). mfrn is highly expressed in fetal and adult haematopoietic tissues of zebrafish and mouse. Erythroblasts generated from murine embryonic stem cells null for Mfrn (also known as Slc25a37) show maturation arrest with severely impaired incorporation of 55Fe into haem. Disruption of the yeast mfrn orthologues, MRS3 and MRS4, causes defects in iron metabolism and mitochondrial Fe-S cluster biogenesis. Murine Mfrn rescues the defects in frs zebrafish, and zebrafish mfrn complements the yeast mutant, indicating that the function of the gene may be highly conserved. Our data show that mfrn functions as the principal mitochondrial iron importer essential for haem biosynthesis in vertebrate erythroblasts.

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Authors: Shaw, G. C., Cope, J. J., Li, L., Corson, K., Hersey, C., Ackermann, G. E., Gwynn, B., Lambert, A. J., Wingert, R. A., Traver, D., Trede, N. S., Barut, B. A., Zhou, Y., Minet, E., Donovan, A., Brownlie, A., Balzan, R., Weiss, M. J., Peters, L. L., Kaplan, J., Zon, L. I., & Paw, B. H.
Affiliations: Brigham and Women's Hospital (US)
University of Utah (US)
Boston Children's Hospital (US)
Jackson Laboratory (US)
University of Malta (MT)
Children's Hospital of Philadelphia (US)
Corresponding author: Paw, Barry H.
ORCID: Shaw, George C.
Li, Liangtao
Gwynn, Babette
Lambert, Amy J.
Wingert, Rebecca A.
Traver, David
Trede, Nikolaus S.
Zhou, Yi
Balzan, Rena
Weiss, Mitchell J.
Peters, Luanne L.
Zon, Leonard I.
Paw, Barry H.
Venue: Nature
Publisher: Springer Science and Business Media LLC
Published: 2006-03
Volume: 440
Issue: 7080
Pages: 96-100
ISSN: 0028-0836 (ISSN-L)
1476-4687
DOI: 10.1038/nature04512
OpenAlex: W1972998779
Cited by: 624
References: 30
Citations by year: 2026: 23 · 2025: 32 · 2024: 40 · 2023: 29 · 2022: 24 · 2021: 38 · 2020: 56 · 2019: 26 · 2018: 24 · 2017: 29 · 2016: 30 · 2015: 27 · 2014: 32 · 2013: 28 · 2012: 30
FWCI: 16.48
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
Locations: Nature (publishedVersion)
PubMed (publishedVersion)
RePEc: Research Papers in Economics (submittedVersion)
The Mouseion at the JAXlibrary (Jackson Laboratory) (submittedVersion)
Funders: National Heart, Lung, and Blood Institute (P01HL032262, R01HL075714)
National Institute of Diabetes and Digestive and Kidney Diseases (R01DK070838)
Topics: Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Hemoglobin structure and function
Keywords: heme biosynthesis, erythroblasts, erythroid maturation, hypochromic anemia, SLC25A37, iron-sulfur cluster assembly, iron homeostasis, positional cloning
MeSH terms: Anemia, Animals, Cell Differentiation, Erythroblasts, Gene Expression Regulation, Genetic Complementation Test, Heme, Homeostasis, Humans, Iron, Iron-Sulfur Proteins, Mitochondria, Molecular Sequence Data, Mutation, Phylogeny, Saccharomyces cerevisiae, Stem Cells, Zebrafish, Conserved Sequence, Iron Overload, Mitochondrial Proteins, Membrane Transport Proteins, Cation Transport Proteins, Saccharomyces cerevisiae Proteins, Zebrafish Proteins, Mice

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Mitoferrin is essential for erythroid iron assimilation

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