The DOI matches its Crossref record; 45 of the 45 references it cites were found in a registry or an index.
A permease-oxidase complex involved in high-affinity iron uptake in yeast.
Abstract
Iron must cross biological membranes to reach essential intracellular enzymes. Two proteins in the plasma membrane of yeast--a multicopper oxidase, encoded by the FET3 gene, and a permease, encoded by the FTR1 gene--were shown to mediate high-affinity iron uptake. FET3 expression was required for FTR1 protein to be transported to the plasma membrane. FTR1 expression was required for apo-FET3 protein to be loaded with copper and thus acquire oxidase activity. FTR1 protein also played a direct role in iron transport. Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport.
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“This situation is somewhat analogous to iron transport in yeast, where the ferrous iron permease FTR1 (functionally analogous but structurally unrelated to DMT1) requires the multicopper ferroxidase FET3 for correct localization on the cell surface.85,86”
From Forging a field: the golden age of iron biology. (2008) · cites this paper as [86]
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Cited by
Sorted by citations
Multicopper oxidases and oxygenases
Solomon, E. I., Sundaram, U. M., & Machonkin, T. E. (1996) · Chemical Reviews · doi:10.1021/cr950046o · Cited by 3,664
Siderophore-Based Iron Acquisition and Pathogen Control
Miethke, M., & Marahiel, M. A. (2007) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.00012-07 · Cited by 1,774
Copper Active Sites in Biology
Solomon, E. I., Heppner, D. E., Johnston, E. M., Ginsbach, J. W., Cirera, J., Qayyum, M. F., Kieber‐Emmons, M. T., Kjaergaard, C. H., Hadt, R. G., & Tian, L. (2014) · Chemical Reviews · doi:10.1021/cr400327t · Cited by 1,803
Positional cloning of zebrafish ferroportin1 identifies a conserved vertebrate iron exporter
Donovan, A., Brownlie, A., Zhou, Y., Shepard, J., Pratt, S. J., Moynihan, J., Paw, B. H., Drejer, A., Barut, B., Zapata, A., et al. (2000) · Nature · doi:10.1038/35001596 · Cited by 1,667
The ZIP family of metal transporters
Guerinot, M. L. (2000) · Biochimica et Biophysica Acta (BBA) - Biomembranes · doi:10.1016/s0005-2736(00)00138-3 · Cited by 1,200
Metadata
- Authors
- Stearman, R., Yuan, D. S., Yamaguchi-Iwai, Y., Klausner, R. D., & Dancis, A.
- Affiliations
- National Institutes of Health (US)
- Cell Biology and Metabolism Branch, National Institutes of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.
- Corresponding author
- Dancis, Andrew
- Venue
- Science
- Published
- 1996-03-15
- Volume
- 271
- Issue
- 5255
- Pages
- 1552-1557
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- OpenAlex
- W2005806732
- Cited by
- 683
- References
- 45
- Citations by year
- 2026: 9 · 2025: 16 · 2024: 15 · 2023: 12 · 2022: 26 · 2021: 22 · 2020: 12 · 2019: 10 · 2018: 17 · 2017: 14 · 2016: 13 · 2015: 19 · 2014: 18 · 2013: 21 · 2012: 16
- FWCI
- 16.55
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Science (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
- Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
- Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Micronutrient Interactions and Effects
- Keywords
- iron absorption, multicopper oxidase, iron permease, plasma membrane transport, copper loading, yeast, conserved motifs
- MeSH terms
- Amino Acid Sequence, Binding Sites, Biological Transport, Carrier Proteins, Cell Membrane, Ceruloplasmin, Copper, Endoplasmic Reticulum, Ferric Compounds, Ferritins, Ferrous Compounds, Genes, Fungal, Golgi Apparatus, Iron, Models, Biological, Molecular Sequence Data, Multienzyme Complexes, Mutation, Oxidation-Reduction, Oxidoreductases, Saccharomyces cerevisiae, Transformation, Genetic, Open Reading Frames, Membrane Transport Proteins, Saccharomyces cerevisiae Proteins
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