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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
Vagaries of conditional gene targeting
Schmidt‐Supprian, M., & Rajewsky, K. (2007) · Nature Immunology · doi:10.1038/ni0707-665 · Cited by 422
Meyron‐Holtz, E. G., Ghosh, M. C., Iwai, K., LaVaute, T., Brazzolotto, X., Berger, U. V., Land, W., Ollivierre‐Wilson, H., Grinberg, A., Love, P., et al. (2004) · The EMBO Journal · doi:10.1038/sj.emboj.7600041 · Cited by 408
Iron–sulfur cluster biogenesis and human disease
Rouault, T. A., & Tong, W. H. (2008) · Trends in Genetics · doi:10.1016/j.tig.2008.05.008 · Cited by 391
Paradkar, P. N., Zumbrennen, K. B., Paw, B. H., Ward, D. M., & Kaplan, J. (2008) · Molecular and Cellular Biology · doi:10.1128/mcb.01685-08 · Cited by 362
Tong, W.-H., & Rouault, T. A. (2006) · Cell Metabolism · doi:10.1016/j.cmet.2006.02.003 · Cited by 294
Molecular control of vertebrate iron homeostasis by iron regulatory proteins
Wallander, M. L., Leibold, E. A., & Eisenstein, R. S. (2006) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2006.05.004 · Cited by 287
Guernsey, D. L., Jiang, H., Campagna, D. R., Evans, S. C., Ferguson, M., Kellogg, M. D., Lachance, M., Matsuoka, M., Nightingale, M., Rideout, A., et al. (2009) · Nature Genetics · doi:10.1038/ng.359 · Cited by 244 · cited 1×
“, the Grx5, Slc25A38, or Abcb7 genes (Guernsey et al., 2009; Levi andRovida, 2009;Rouault andTong, 2008;Sheftel and Lill, 2009).”
Galy, B., Ferring–Appel, D., Miñana, B., Bell, O., Janser, H., Muckenthaler, M. U., Schümann, K., & Hentze, M. W. (2005) · Blood · doi:10.1182/blood-2005-04-1365 · Cited by 224
Self-citationHuang, M. L.-H., Becker, E. M., Whitnall, M., Rahmanto, Y. S., Ponka, P., & Richardson, D. R. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0906784106 · Cited by 212
The role of iron in mitochondrial function
Levi, S., & Rovida, E. (2008) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2008.09.008 · Cited by 202
Galy, B., Ferring-Appel, D., Kaden, S., Gröne, H.-J., & Hentze, M. W. (2008) · Cell Metabolism · doi:10.1016/j.cmet.2007.10.006 · Cited by 195
Self-citationGraham, R. M. (2007) · World Journal of Gastroenterology · doi:10.3748/wjg.v13.i35.4725 · Cited by 184
Delaby, C., Pilard, N., Puy, H., & Canonne-Hergaux, F. (2008) · Biochemical Journal · doi:10.1042/bj20071474 · Cited by 144
Self-citationSmith, S., Ghosh, M. C., Ollivierre, H., Tong, W. H., & Rouault, T. A. (2006) · Blood Cells Molecules and Diseases · doi:10.1016/j.bcmd.2005.12.006 · Cited by 123
Bioenergetics in Glutaryl-Coenzyme A Dehydrogenase Deficiency
Sauer, S., Okun, J., Schwab, M., Crnic, L. R., Hoffmann, G., Goodman, S., Koeller, D., & Kolker, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m502845200 · Cited by 120
Self-citationEnlargement of Mitochondrial Compartment in Iron and Copper Deficiency
Dallman, P. R., & Goodman, J. R. (1970) · Blood · doi:10.1182/blood.v35.4.496.496 · Cited by 119
Atamna, H., Walter, P. B., & Ames, B. N. (2002) · Archives of Biochemistry and Biophysics · doi:10.1006/abbi.2001.2671 · Cited by 118
Chen, O. S., Schalinske, K. L., & Eisenstein Richard, S. (1997) · Journal of Nutrition · doi:10.1093/jn/127.2.238 · Cited by 110
Molybdenum cofactor-deficient mice resemble the phenotype of human patients
Lee, H. (2002) · Human Molecular Genetics · doi:10.1093/hmg/11.26.3309 · Cited by 70
Lyoumi, S., Abitbol, M., Andrieu, V., Hénin, D., Robert, E., Schmitt, C., Gouya, L., de Verneuil, H., Deybach, J., Montagutelli, X., et al. (2006) · Blood · doi:10.1182/blood-2006-04-014142 · Cited by 63
Self-citationGeneration of conditional alleles of the murine iron regulatory protein (IRP)‐1 and ‐2 genes
Galy, B., Ferring–Appel, D., & Hentze, M. W. (2005) · genesis · doi:10.1002/gene.20169 · Cited by 54
Self-citationSheftel, A. D., & Lill, R. (2008) · Annals of Medicine · doi:10.1080/07853890802322229 · Cited by 49
Gender Disparity of Hepatic Lipid Homoeostasis Regulated by the Circadian Clock
Yang, X., Zhang, Y.-K. J., Esterly, N., Klaassen, C. D., & Wan, Y.-J. Y. (2009) · The Journal of Biochemistry · doi:10.1093/jb/mvp018 · Cited by 38
Getting around lethality with inducible Cre-mediated excision
Garcia, E. L., & Mills, A. A. (2002) · Seminars in Cell and Developmental Biology · doi:10.1016/s1084-9521(02)00019-8 · Cited by 37
Davies, R., Schuurman, A., Barker, C. R., Clothier, B., Chernova, T., Higginson, F. M., Judah, D. J., Dinsdale, D. D., Edwards, R., Greaves, P., et al. (2005) · American Journal Of Pathology · doi:10.1016/s0002-9440(10)62325-5 · Cited by 35
Dietary iron deficiency in the rat. I. Abnormalities in energy metabolism of the hepatic tissue
Masini, A., Salvioli, G., Cremonesi, P., Botti, B., Gallesi, D., & Ceccarelli, D. (1994) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/0005-2728(94)90020-5 · Cited by 24
Ubiquitous postnatal LoxP recombination using a doxycycline auto-inducible Cre transgene (DAI-Cre)
Holzenberger, M., Zaoui, R., Leneuve, P., Hamard, G., & Bouc, Y. L. (2000) · genesis · doi:10.1002/(sici)1526-968x(200002)26:2 · Cited by 23
Lyoumi, S., Schmitt, C., Touitou, Y., Puy, H., & Djeridane, Y. (2008) · Chronobiology International · doi:10.1080/07420520802548242 · Cited by 12
Self-citationSwick, R. A., Cheeke, P. R., & Buhler, D. R. (1982) · Journal of Animal Science · doi:10.2527/jas1982.5561425x · Cited by 5
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Wang, J., & Pantopoulos, K. (2011) · Biochemical Journal · doi:10.1042/bj20101825 · Cited by 986
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Galy, B., Conrad, M., & Muckenthaler, M. U. (2023) · Nature Reviews Molecular Cell Biology · doi:10.1038/s41580-023-00648-1 · Cited by 843
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Pantopoulos, K., Porwal, S. K., Tartakoff, A., & Devireddy, L. (2012) · Biochemistry · doi:10.1021/bi300752r · Cited by 598
Regulation of iron transport and the role of transferrin
Gkouvatsos, K., Papanikolaou, G., & Pantopoulos, K. (2012) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2011.10.013 · Cited by 518
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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