The DOI matches its Crossref record; 12 of the 12 references it cites were found in a registry or an index.
The Role of Mitochondria in Cellular Iron-Sulfur Protein Biogenesis: Mechanisms, Connected Processes, and Diseases
Open accessAbstract
Iron-sulfur (Fe/S) clusters belong to the most ancient protein cofactors in life, and fulfill functions in electron transport, enzyme catalysis, homeostatic regulation, and sulfur activation. The synthesis of Fe/S clusters and their insertion into apoproteins requires almost 30 proteins in the mitochondria and cytosol of eukaryotic cells. This review summarizes our current biochemical knowledge of mitochondrial Fe/S protein maturation. Because this pathway is essential for various extramitochondrial processes, we then explain how mitochondria contribute to the mechanism of cytosolic and nuclear Fe/S protein biogenesis, and to other connected processes including nuclear DNA replication and repair, telomere maintenance, and transcription. We next describe how the efficiency of mitochondria to assemble Fe/S proteins is used to regulate cellular iron homeostasis. Finally, we briefly summarize a number of mitochondrial "Fe/S diseases" in which various biogenesis components are functionally impaired owing to genetic mutations. The thorough understanding of the diverse biochemical disease phenotypes helps with testing the current working model for the molecular mechanism of Fe/S protein biogenesis and its connected processes.
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Cites
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Structure, function, and formation of biological iron-sulfur clusters
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Grx5 Is a Mitochondrial Glutaredoxin Required for the Activity of Iron/Sulfur Enzymes
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Self-citationDeficiency of glutaredoxin 5 reveals Fe-S clusters are required for vertebrate haem synthesis.
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Cited by
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Battaglia, A. M., Chirillo, R., Aversa, I., Sacco, A., Costanzo, F., & Biamonte, F. (2020) · Cells · doi:10.3390/cells9061505 · Cited by 561
Cysteinyl-tRNA synthetase governs cysteine polysulfidation and mitochondrial bioenergetics
Akaike, T., Ida, T., Wei, F.-Y., Nishida, M., Kumagai, Y., Alam, M. M., Ihara, H., Sawa, T., Matsunaga, T., Kasamatsu, S., et al. (2017) · Nature Communications · doi:10.1038/s41467-017-01311-y · Cited by 544
The genetics and pathology of mitochondrial disease
Alston, C. L., Rocha, M. C., Lax, N. Z., Turnbull, D. M., & Taylor, R. W. (2017) · The Journal of Pathology · doi:10.1002/path.4809 · Cited by 451
Mitochondrial iron–sulfur protein biogenesis and human disease
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Self-citationMaturation of cytosolic and nuclear iron–sulfur proteins
Netz, D. J. A., Mascarenhas, J., Stehling, O., Pierik, A. J., & Lill, R. (2014) · Trends in Cell Biology · doi:10.1016/j.tcb.2013.11.005 · Cited by 184
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Metadata
- Authors
- Stehling, O., & Lill, R.
- Venue
- Cold Spring Harbor Perspectives in Biology
- Publisher
- Cold Spring Harbor Laboratory
- Published
- 2013-08-01
- Volume
- 5
- Issue
- 8
- Pages
- a011312-a011312
- ISSN
- 1943-0264 (ISSN-L)
- OpenAlex
- W2105427103
- Cited by
- 227
- References
- 12
- Type
- posted content
- Language
- en
- Open access
- bronze
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