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Iron Regulatory Proteins Secure Mitochondrial Iron Sufficiency and Function
Open accessAbstract
Mitochondria supply cells with ATP, heme, and iron sulfur clusters (ISC), and mitochondrial energy metabolism involves both heme- and ISC-dependent enzymes. Here, we show that mitochondrial iron supply and function require iron regulatory proteins (IRP), cytosolic RNA-binding proteins that control mRNA translation and stability. Mice lacking both IRP1 and IRP2 in their hepatocytes suffer from mitochondrial iron deficiency and dysfunction associated with alterations of the ISC and heme biosynthetic pathways, leading to liver failure and death. These results uncover a major role of the IRPs in cell biology: to ensure adequate iron supply to the mitochondrion for proper function of this critical organelle.
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“Earlier work investigating mice with complete IRP deficiency in hepatocytes or duodenal enterocytes, respectively, had shown early post-natal death in both cases, reflecting essential functions of the IRPs for organismal survival (Galy et al., 2008, 2010).”
From Iron Regulatory Proteins Mediate Host Resistance to Salmonella Infection (2015) · cites this paper as Galy et al., 2010
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Cites
Regulation of Iron Metabolism by Hepcidin
Nemeth, E., & Ganz, T. (2006) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.26.061505.111303 · Cited by 756 · cited 1×
“At the systemic level, the hepatic ‘‘iron hormone’’ hepcidin (Hamp) has emerged as the key regulator of blood iron levels (Nemeth and Ganz, 2006).”
BackgroundPuy, H., Gouya, L., & Deybach, J. (2010) · The Lancet · doi:10.1016/s0140-6736(09)61925-5 · Cited by 727
Self-citationMuckenthaler, M. U., Galy, B., & Hentze, M. W. (2008) · Annual Review of Nutrition · doi:10.1146/annurev.nutr.28.061807.155521 · Cited by 701
Self-citationMitoferrin is essential for erythroid iron assimilation
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., et al. (2006) · Nature · doi:10.1038/nature04512 · Cited by 624
Forging a field: the golden age of iron biology.
Andrews, N. C. (2008) · Blood · doi:10.1182/blood-2007-12-077388 · Cited by 623
Zip14 (Slc39a14) mediates non-transferrin-bound iron uptake into cells
Liuzzi, J. P., Aydemir, F., Nam, H., Knutson, M. D., & Cousins, R. J. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0606424103 · Cited by 577
LaVaute, T., Smith, S., Cooperman, S., Iwai, K., Land, W., Meyron-Holtz, E., Drake, S. K., Miller, G., Abu-Asab, M., Tsokos, M., et al. (2001) · Nature Genetics · doi:10.1038/84859 · Cited by 509
Biosynthesis of heme in mammals
Ajioka, R. S., Phillips, J. D., & Kushner, J. P. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.005 · Cited by 493
Biochemical Basis for the Manifestations of Iron Deficiency
Dallman, P. R. (1986) · Annual Review of Nutrition · doi:10.1146/annurev.nu.06.070186.000305 · Cited by 447
Mantena, S. K., King, A. L., Andringa, K. K., Eccleston, H. B., & Bailey, S. M. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.12.029 · Cited by 429
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Self-citationRegulation of cellular iron metabolism
Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
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Bonadonna, M., Altamura, S., Tybl, E., Palais, G., Qatato, M., Polycarpou‐Schwarz, M., Schneider, M., Kalk, C., Rüdiger, W., Ertl, A., et al. (2022) · Science Advances · doi:10.1126/sciadv.abq4469 · Cited by 68
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Styś, A., Galy, B., Starzyński, R. R., Smuda, E., Drapier, J., Lipiński, P., & Bouton, C. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.231902 · Cited by 64
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Self-citationLemire, J. A., Mailloux, R. J., Darwich, R., Auger, C., & Appanna, V. D. (2011) · Toxicology Letters · doi:10.1016/j.toxlet.2011.03.019 · Cited by 46
Li, H., Zhao, H., Hao, S., Shang, L., Wu, J., Song, C., Meyron‐Holtz, E. G., Qiao, T., & Li, K. (2018) · Scientific Reports · doi:10.1038/s41598-018-23175-y · Cited by 45
Peoc’h, K., Nicolas, G., Schmitt, C., Mirmiran, A., Daher, R., Lefèbvre, T., Gouya, L., Karim, Z., & Puy, H. (2019) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2019.01.015 · Cited by 43
Self-citationLeermakers, P. A., Remels, A. H. V., Zonneveld, M. I., Rouschop, K. M. A., Schols, A. M. W. J., & Gosker, H. R. (2020) · The FASEB Journal · doi:10.1096/fj.201901815r · Cited by 46
Weidmann, H., Bannasch, J. H., Waldeyer, C., Shrivastava, A., Appelbaum, S., Ojeda, F., Schnabel, R. B., Lackner, K. J., Blankenberg, S., Zeller, T., et al. (2020) · Journal of the American Heart Association · doi:10.1161/jaha.119.015480 · Cited by 39
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Self-citationKallianpur, A. R., Jia, P., Ellis, R. J., Zhao, Z., Bloss, C. S., Wen, W., Marra, C. M., Hulgan, T., Simpson, D. M., Morgello, S., et al. (2014) · PLoS ONE · doi:10.1371/journal.pone.0103123 · Cited by 33
Moety, G. A. F. A., Ali, A. M., Fouad, R., Ramadan, W., Belal, D. S., & Haggag, H. M. (2017) · European Journal of Obstetrics & Gynecology and Reproductive Biology · doi:10.1016/j.ejogrb.2017.01.003 · Cited by 32
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Greene, C., Sharma, N. J., Fiorica, P. N., Forrester, E. J., Smith, G. J., Gross, K. W., & KAUFFMAN, E. C. (2018) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2018.12.013 · Cited by 28
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Tuncel, A. T., Ruppert, T., Wang, B.-T., Okun, J. G., Kölker, S., Morath, M., & Sauer, S. W. (2015) · PLoS ONE · doi:10.1371/journal.pone.0128770 · Cited by 26
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RetractedGarza, K. R., Clarke, S. L., Ho, Y., Bruss, M. D., Vasanthakumar, A., Anderson, S. A., & Eisenstein, R. S. (2020) · Metallomics · doi:10.1039/d0mt00192a · Cited by 22
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Dzięgała, M., Kasztura, M., Kobak, K. A., Bania, J., Banasiak, W., Ponikowski, P. P., & Jankowska, E. A. (2016) · Molecular Medicine Reports · doi:10.3892/mmr.2016.5705 · Cited by 25
Telser, J., Volani, C., Hilbe, R., Seifert, M., Brigo, N., Paglia, G., & Weiß, G. (2019) · Microbial Cell · doi:10.15698/mic2019.12.700 · Cited by 23
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Greene, C., Attwood, K. M., Sharma, N. J., Balderman, B., Deng, R., Muhitch, J. B., Smith, G. J., Gross, K. W., Xu, B., & KAUFFMAN, E. C. (2022) · Frontiers in Oncology · doi:10.3389/fonc.2022.923043 · Cited by 23
Tapryal, N., Vishnu Vivek, G., & Mukhopadhyay, C. K. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.592519 · Cited by 22
Qian, X., Zhou, Q., Ouyang, Y., Wu, X., Sun, X. L., Wang, S., Duan, Y., Hu, Z., Hou, Y., Wang, Z., et al. (2025) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2412473122 · Cited by 25
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Haro, K. J., Sheth, A., & Scheinberg, D. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0048841 · Cited by 19
Motonishi, S., Tanaka, K., & Ozawa, T. (2018) · PLoS ONE · doi:10.1371/journal.pone.0201662 · Cited by 19
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Zhang, T., Liu, Q., Chen, Q., & Wu, H. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107767 · Cited by 14
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Metadata
- Authors
- Galy, B., Ferring-Appel, D., Sauer, S. W., Kaden, S., Lyoumi, S., Puy, H., Kölker, S., Gröne, H.-J., & Hentze, M. W.
- Affiliations
- European Molecular Biology Laboratory (DE)
- Heidelberg University (DE)
- German Cancer Research Center (DE)
- Corresponding author
- Hentze, Matthias W.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2010-08
- Volume
- 12
- Issue
- 2
- Pages
- 194-201
- ISSN
- 1550-4131 (ISSN-L)
- OpenAlex
- W1995039474
- Cited by
- 147
- References
- 39
- Citations by year
- 2026: 5 · 2025: 16 · 2024: 7 · 2023: 7 · 2022: 11 · 2021: 9 · 2020: 12 · 2019: 10 · 2018: 9 · 2017: 7 · 2016: 8 · 2015: 8 · 2014: 12 · 2013: 5 · 2012: 10
- FWCI
- 5.22
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Mitochondrial Function and Pathology
- Life Sciences › Neuroscience › Neurology › Neurological diseases and metabolism
- Keywords
- iron regulatory proteins, iron regulatory protein 1, IRP2, iron deficiency, iron-sulfur clusters, heme biosynthesis, mitochondrial dysfunction, hepatocytes, liver failure, RNA-binding proteins
- MeSH terms
- Animals, Energy Metabolism, Heme, Iron, Mice, Transgenic, Mitochondria, Liver Failure, Iron-Regulatory Proteins, Iron Regulatory Protein 1, Iron Regulatory Protein 2, Mice
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