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Cooperation of Two mRNA-Binding Proteins Drives Metabolic Adaptation to Iron Deficiency
Open accessAbstract
Iron (Fe) is an essential cofactor for a wide range of cellular processes. We have previously demonstrated in yeast that Cth2 is expressed during Fe deficiency and promotes degradation of a battery of mRNAs leading to reprogramming of Fe-dependent metabolism and Fe storage. We report here that the Cth2-homologous protein Cth1 is transiently expressed during Fe deprivation and participates in the response to Fe deficiency through the degradation of mRNAs primarily involved in mitochondrially localized activities including respiration and amino acid biosynthesis. In parallel, wild-type cells, but not cth1Deltacth2Delta cells, accumulate mRNAs encoding proteins that function in glucose import and storage and store high levels of glycogen. In addition, Fe deficiency leads to phosphorylation of Snf1, an AMP-activated protein kinase family member required for the cellular response to glucose starvation. These studies demonstrate a metabolic reprogramming as a consequence of Fe starvation that is dependent on the coordinated activities of two mRNA-binding proteins.
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“Under iron limitation, yeast cells lacking the iron-regulated RNA-binding protein Cth2 display high mRNA levels of multiple ERG genes including those of the first steps of the late stage of synthesis (ERG1, ERG7, ERG11 and DAP1) [116,118].”
From Regulation of Ergosterol Biosynthesis in Saccharomyces cerevisiae (2020) · cites this paper as [118]
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Cited by
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Metalloproteins and metal sensing
Waldron, K. J., Rutherford, J. C., Ford, D., & Robinson, N. J. (2009) · Nature · doi:10.1038/nature08300 · Cited by 1,269
“The factors also control metabolic switching; for example, the transcription factors Aft1 and Aft2 indirectly (through Cth1 and Cth2 (also known as Tis11)) reduce the stability of transcripts encoding iron-dependent enzymes when iron is in poor suppl”
BackgroundThe role of mitochondria in cellular iron–sulfur protein biogenesis and iron metabolism
Lill, R., Hoffmann, B., Molik, S., Pierik, A. J., Rietzschel, N., Stehling, O., Uzarska, M. A., Webert, H., Wilbrecht, C., & Mühlenhoff, U. (2012) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2012.05.009 · Cited by 513
“Moreover, the levels of CCC1 mRNA are diminished by Cth1 – Cth2-dependent mRNA decay [195] (Fig.”
InfluentialRegulation of Ergosterol Biosynthesis in Saccharomyces cerevisiae
Jordá, T., & Puig, S. (2020) · Genes · doi:10.3390/genes11070795 · Cited by 489
Self-citationThe elemental role of iron in DNA synthesis and repair
Puig, S., Ramos-Alonso, L., Romero, A. M., & Martínez‐Pastor, M. T. (2017) · Metallomics · doi:10.1039/c7mt00116a · Cited by 379
Jan, A., Maruyama, K., Todaka, D., Kidokoro, S., Abo, M., Yoshimura, E., Shinozaki, K., Nakashima, K., & Yamaguchi‐Shinozaki, K. (2013) · PLANT PHYSIOLOGY · doi:10.1104/pp.112.205385 · Cited by 312
“In humans, TZFs control the expression of cytokines, whereas in yeast (Saccharomyces cerevisiae), TZF homologs (Cth1 and Cth2) promote the reprogramming of iron-dependent metabolism and iron storage through the control of target mRNA half-lives (Blackshear et al., 2005; Puig et al., 2008).”
Background
Metadata
- Authors
- Puig, S., Vergara, S. V., & Thiele, D. J.
- Affiliations
- Universitat de València (ES)
- Duke Medical Center (US)
- Corresponding author
- Puig, Sergi
- Thiele, Dennis J.
- Venue
- Cell Metabolism
- Publisher
- Elsevier BV
- Published
- 2008-06
- Volume
- 7
- Issue
- 6
- Pages
- 555-564
- ISSN
- 1550-4131 (ISSN-L)
- PMC
- PMC2459314
- OpenAlex
- W2041968919
- Cited by
- 135
- References
- 38
- Citations by year
- 2026: 3 · 2025: 4 · 2024: 8 · 2023: 4 · 2022: 7 · 2021: 8 · 2020: 6 · 2019: 3 · 2018: 11 · 2017: 8 · 2016: 8 · 2015: 4 · 2014: 7 · 2013: 12 · 2012: 13
- FWCI
- 5.84
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell Metabolism (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- University of Pittsburgh
- National Institutes of Health
- U.S. Public Health Service (FDK081304A)
- National Institute of General Medical Sciences (GM 41840, R01GM041840)
- National Institute of Diabetes and Digestive and Kidney Diseases (F31DK081304)
- Topics
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › RNA Research and Splicing
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Keywords
- iron deficiency, mRNA-binding proteins, mRNA degradation, metabolic reprogramming, Snf1, AMPK, glycogen storage, mitochondrial respiration, amino acid biosynthesis, Saccharomyces cerevisiae, iron starvation response
- MeSH terms
- Iron Deficiencies, Adaptation, Physiological, DNA-Binding Proteins, Metabolism, Phosphorylation, RNA, Messenger, Saccharomyces cerevisiae, Transcription Factors, RNA-Binding Proteins, Protein Serine-Threonine Kinases, Saccharomyces cerevisiae Proteins, Tristetraprolin
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