Cited by 683Fungal and yeast genetics researchIron Metabolism and DisordersPlant Micronutrient Interactions and Effects

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A permease-oxidase complex involved in high-affinity iron uptake in yeast.

Stearman, Robert, Yuan, Daniel S., Yamaguchi-Iwai, Yuko, Klausner, Richard D., Dancis, Andrew·1996·Science

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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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Altschul, S. F., Gish, W., Miller, W., Myers, E. W., & Lipman, D. J. (1990) · Journal of Molecular Biology · doi:10.1006/jmbi.1990.9999 · Cited by 98,669
Ferrozine---a new spectrophotometric reagent for iron
Stookey, L. L. (1970) · Analytical Chemistry · doi:10.1021/ac60289a016 · Cited by 4,712
The Wilson disease gene is a putative copper transporting P–type ATPase similar to the Menkes gene
Bull, P. C., Thomas, G. R., Rommens, J. M., Forbes, J., & Cox, D. W. (1993) · Nature Genetics · doi:10.1038/ng1293-327 · Cited by 1,939
The Wilson disease gene is a copper transporting ATPase with homology to the Menkes disease gene
Tanzi, R. E., Petrukhin, K. E., Чернов, И. П., Pellequer, J., Wasco, W., Ross, B., Romano, D., Parano, E., Pavone, P., Brzustowicz, L. M., et al. (1993) · Nature Genetics · doi:10.1038/ng1293-344 · Cited by 1,367
High stored iron levels are associated with excess risk of myocardial infarction in eastern Finnish men
Salonen, J. T., Nyyssönen, K., Korpela, H., Tuomilehto, J., Seppänen, R., & Salonen, R. (1992) · Circulation · doi:10.1161/01.cir.86.3.803 · Cited by 1,284
A Saccharomyces cerevisiae genomic plasmid bank based on a centromere-containing shuttle vector
Rose, M. D., Novick, P., Thomas, J. H., Botstein, D., & Fink, G. R. (1987) · Gene · doi:10.1016/0378-1119(87)90232-0 · Cited by 1,126
Altered Brain Metabolism of Iron as a Cause of Neurodegenerative Diseases?
Gerlach, M., Ben‐Shachar, D., Riederer, P. F., & Youdim, M. B. H. (1994) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.1994.63030793.x · Cited by 704
The possible significance of the ferrous oxidase activity of ceruloplasmin in normal human serum.
Osaki, S., Johnson, D. A., & Frieden, E. (1966) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(18)96527-0 · Cited by 679
The FET3 gene of S. cerevisiae encodes a multicopper oxidase required for ferrous iron uptake.
Askwith, C., Eide, D., Van Ho, A., Bernard, P. S., Li, L., Davis-Kaplan, S., Sipe, D. M., & Kaplan, J. (1994) · Cell · doi:10.1016/0092-8674(94)90346-8 · Cited by 670
Molecular characterization of a copper transport protein in S. cerevisiae: An unexpected role for copper in iron transport
Dancis, A., Yuan, D. S., Haile, D., Askwith, C., Eide, D., Moehle, C., Kaplan, J., & Klausner, R. D. (1994) · Cell · doi:10.1016/0092-8674(94)90345-x · Cited by 659
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Show all 45 references

Research works printed but not linked: 10

Genetics Computer Group, Program Manual for the Wisconsin Package, Version 8 (1994).
BOTHWELL H. T., METABOLIC MOL BASES: 2237 (1995).
BRITTENHAM M. G., HEMATOLOGY BASIC PRI: 492 (1995).
CAMMACK R, IRON TRANSPORT STORA: 17 (1990).
CRICHTON R. R., INORGANIC BIOCH IRON: 144 (1991).
HALLIWELL B, FREE RADICALS BIOL M (1991).
HOFMANN K, BIOL CHEM HOPPESEYLE 347, 166 (1993).
LIPPARD J. S., PRINCIPLES BIOINORGA: 125 (1994).
WILLIAMS RJP, IRON TRANSPORT STORA: 2 (1990).
WINKELMANN G, IRON TRANSPORT MICRO (1987).

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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
ORCID: Stearman, Robert
Yuan, Daniel S.
Dancis, Andrew
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1996-03-15
Volume: 271
Issue: 5255
Pages: 1552-1557
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.271.5255.1552
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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A permease-oxidase complex involved in high-affinity iron uptake in yeast.

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