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Mitochondrial iron detoxification is a primary function of frataxin that limits oxidative damage and preserves cell longevity
Open accessAbstract
Friedreich ataxia is a severe autosomal-recessive disease characterized by neurodegeneration, cardiomyopathy and diabetes, resulting from reduced synthesis of the mitochondrial protein frataxin. Although frataxin is ubiquitously expressed, frataxin deficiency leads to a selective loss of dorsal root ganglia neurons, cardiomyocytes and pancreatic beta cells. How frataxin normally promotes survival of these particular cells is the subject of intense debate. The predominant view is that frataxin sustains mitochondrial energy production and other cellular functions by providing iron for heme synthesis and iron-sulfur cluster (ISC) assembly and repair. We have proposed that frataxin not only promotes the biogenesis of iron-containing enzymes, but also detoxifies surplus iron thereby affording a critical anti-oxidant mechanism. These two functions have been difficult to tease apart, however, and the physiologic role of iron detoxification by frataxin has not yet been demonstrated in vivo. Here, we describe mutations that specifically impair the ferroxidation or mineralization activity of yeast frataxin, which are necessary for iron detoxification but do not affect the iron chaperone function of the protein. These mutations increase the sensitivity of yeast cells to oxidative stress, shortening chronological life span and precluding survival in the absence of the anti-oxidant enzyme superoxide dismutase. Thus, the role of frataxin is not limited to promoting ISC assembly or heme synthesis. Iron detoxification is another function of frataxin relevant to anti-oxidant defense and cell longevity that could play a critical role in the metabolically demanding environment of non-dividing neuronal, cardiac and pancreatic beta cells.
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“lowering iron does increase the lifespan of Drosophila [1215] and yeast [1105].”
From Iron behaving badly: inappropriate iron chelation as a major contributor to the aetiology of vascular and other progressive inflammatory and degenerative diseases (2009) · cites this paper as [1105]
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“The mRNA of hepcidin does not contain this element (99),”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [99]
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Metadata
- Authors
- Gakh, O., Park, S., Liu, G., Macomber, L., Imlay, J. A., Ferreira, G. C., & Isaya, G.
- Affiliations
- Mayo Clinic (US)
- University of Illinois Urbana-Champaign (US)
- Corresponding author
- Gakh, Oleksandr
- Venue
- Human Molecular Genetics
- Publisher
- Oxford University Press (OUP)
- Published
- 2005-12-21
- Volume
- 15
- Issue
- 3
- Pages
- 467-479
- ISSN
- 0964-6906 (ISSN-L)
- 1460-2083
- OpenAlex
- W2115953418
- Cited by
- 184
- References
- 59
- Citations by year
- 2026: 2 · 2024: 4 · 2023: 1 · 2022: 3 · 2021: 4 · 2020: 1 · 2019: 5 · 2018: 7 · 2017: 10 · 2016: 4 · 2015: 6 · 2014: 9 · 2013: 13 · 2012: 10
- FWCI
- 7.28
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- other-oa
- Locations
- Human Molecular Genetics (publishedVersion, other-oa)
- PubMed (publishedVersion)
- HighWire Press Open Archive (submittedVersion)
- Funders
- American Cancer Society
- Friedreich's Ataxia Research Alliance
- National Institutes of Health (GM49640)
- National Institute on Aging (AG-15709, R01AG015709)
- National Institute of General Medical Sciences (R01GM049640, GM 49640)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- frataxin, Friedreich's ataxia, iron mineralization, oxidative stress, chronological lifespan, superoxide dismutase, iron chaperone, iron-sulfur cluster assembly, heme biosynthesis, cell longevity, antioxidant defense
- MeSH terms
- Frataxin, Amino Acids, Ceruloplasmin, Iron, Inactivation, Metabolic, Minerals, Mitochondria, Mutation, Saccharomyces cerevisiae, Superoxide Dismutase, Mutagenesis, Site-Directed, Oxidative Stress, Molecular Chaperones, Iron-Binding Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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