The DOI matches its Crossref record; 184 of the 184 references it cites were found in a registry or an index.
Iron-Sulfur Protein Biogenesis in Eukaryotes: Components and Mechanisms
Abstract
Iron-sulfur (Fe/S) clusters require a complex set of proteins to become assembled and incorporated into apoproteins in a living cell. Researchers have described three distinct assembly systems in eukaryotes that are involved in the maturation of cellular Fe/S proteins. Mitochondria are central for biogenesis. They contain the ISC—the iron-sulfur cluster assembly machinery that was inherited from a similar system of eubacteria in evolution and is involved in biogenesis of all cellular Fe/S proteins. The basic principle of mitochondrial (and bacterial) Fe/S protein maturation is the synthesis of the Fe/S cluster on a scaffold protein before the cluster is transferred to apoproteins. Biogenesis of cytosolic and nuclear Fe/S proteins is facilitated by the cytosolic iron-sulfur protein assembly (CIA) apparatus. This process requires the participation of mitochondria that export a still unknown component via the ISC export machinery, including an ABC transporter.
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“In in vitro studies in hepatoma, K562, and HeLa cells, hypoxic conditions resulted in twofold to threefold increased TfR1 mRNA expression (190, 295).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [190]
In the citing paper
“The promoter of TfR1 contains a hypoxia-responsive element (HRE) within a 100-bp sequence located upstream of the transcription start site (190).”
From Intracellular iron transport and storage: from molecular mechanisms to health implications (2008) · cites this paper as [190]
Citations
Cites
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Friedreich's Ataxia: Autosomal Recessive Disease Caused by an Intronic GAA Triplet Repeat Expansion
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Iron-sulfur clusters: nature's modular, multipurpose structures
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“For a more comprehensive summary of the complex and diverse pathways of bacterial Fe/S protein assembly, we direct the reader to recent excellent reviews (Mansy & Cowan 2004, Barras et al. 2005, Fontecave et al. 2005, Johnson et al. 2005).”
BackgroundMethodInfluentialThe WD repeat: a common architecture for diverse functions
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Regulation of Mitochondrial Iron Accumulation by Yfh1p, a Putative Homolog of Frataxin
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The mitochondrial proteins Atm1p and Nfs1p are essential for biogenesis of cytosolic Fe/S proteins
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Self-citationAssembly of Iron-Sulfur Clusters
Zheng, L., Cash, V. L., Flint, D. H., & Dean, D. R. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.21.13264 · Cited by 650
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Occurrence, Classification, and Biological Function of Hydrogenases: An Overview
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Function and biogenesis of iron-sulphur proteins
Lill, R. (2009) · Nature · doi:10.1038/nature08301 · Cited by 1,167
Self-citationHohmann-Marriott, M. F., & Blankenship, R. E. (2011) · Annual Review of Plant Biology · doi:10.1146/annurev-arplant-042110-103811 · Cited by 744
Hanschmann, E.-M., Godoy, J. R., Berndt, C., Hudemann, C., & Lillig, C. H. (2013) · Antioxidants and Redox Signaling · doi:10.1089/ars.2012.4599 · Cited by 694
Mitochondrial metabolism promotes adaptation to proteotoxic stress
Tsvetkov, P., Detappe, A., Cai, K., Keys, H. R., Brune, Z., Ying, W., Thiru, P., Reidy, M., Kugener, G., Rossen, J., et al. (2019) · Nature Chemical Biology · doi:10.1038/s41589-019-0291-9 · Cited by 645
Metadata
- Authors
- Lill, R., & Mühlenhoff, U.
- Affiliations
- Philipps University of Marburg (DE)
- Venue
- Annual Review of Cell and Developmental Biology
- Publisher
- Annual Reviews
- Published
- 2006-11-01
- Volume
- 22
- Issue
- 1
- Pages
- 457-486
- ISSN
- 1081-0706 (ISSN-L)
- 1530-8995
- OpenAlex
- W2096692378
- Cited by
- 365
- References
- 184
- Citations by year
- 2026: 2 · 2025: 10 · 2024: 8 · 2023: 12 · 2022: 5 · 2021: 11 · 2020: 16 · 2019: 16 · 2018: 11 · 2017: 19 · 2016: 16 · 2015: 15 · 2014: 18 · 2013: 20 · 2012: 21
- FWCI
- 3.45
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Annual Review of Cell and Developmental Biology (publishedVersion)
- PubMed (publishedVersion)
- Bayerische Staatsbibliothek (submittedVersion)
- Funders
- Deutsche Forschungsgemeinschaft
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Biochemistry › Metalloenzymes and iron-sulfur proteins
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Enzyme Structure and Function
- Keywords
- iron-sulfur clusters, mitochondrial iron-sulfur proteins, scaffold proteins, ABC transporters, eukaryotic evolution
- MeSH terms
- Animals, Bacteria, Eukaryotic Cells, Ferredoxin-NADP Reductase, Iron-Sulfur Proteins, Mitochondria, Saccharomyces cerevisiae
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