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Gene Review

FTR1  -  high-affinity iron permease FTR1

Saccharomyces cerevisiae S288c

Synonyms: Plasma membrane iron permease, YER145C
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High impact information on FTR1

  • FET3 expression was required for FTR1 protein to be transported to the plasma membrane [1].
  • Mutations in a conserved sequence motif of FTR1 specifically blocked iron transport [1].
  • Iron-induced degradation of Fet3p-Ftr1p is significantly reduced in strains containing a deletion of a gene, VTA1, which is involved in multivesicular body (MVB) sorting in yeast [2].
  • Yeast strains defective in endocytosis (Deltaend4) show a reduced iron-induced loss of Fet3p-Ftr1p [2].
  • Strains unable to grow on iron-restricted medium contained deletions of genes that encode the structural components of the high affinity iron transport system (FET3, FTR1), the iron-sensing transcription factor AFT1 or genes required for the assembly of the transport system [3].

Biological context of FTR1

  • Suppression of the fet3 fet4 mutant phenotype by FET5 overexpression required the putative FTR1 transporter subunit of the high-affinity system [4].
  • The requirement of FTR1 for virulence in a systemic infection model and its role in transferrin iron uptake raise the possibility that transferrin is a source of iron during systemic C. albicans infections [5].
  • We examine the (59)Fe uptake kinetics for a number of complexes containing mutant forms of both Fet3p and Ftr1p and demonstrate that a residue in one protein interacts with one in the other protein along the iron trafficking pathway as would be expected in a channeling process [6].

Anatomical context of FTR1


Associations of FTR1 with chemical compounds

  • A mutation of FTR1 did not impair the use of these siderophores but did affect the uptake of ferrioxamines E and B, as well as of ferric citrate, indicating that their utilization was independent of Sit1p [9].
  • Fet3, the apparent ferroxidase, is proposed to facilitate iron uptake by catalyzing the oxidation of reductase-generated Fe(II) to Fe(III) by O2; in this model, Fe(III) is the substrate for the iron permease, encoded by FTR1 (Kaplan, J., and O'Halloran, T. V. (1996) Science 271, 1510-1512) [10].
  • Fet3p is proposed to facilitate iron uptake by catalyzing the oxidation of Fe(II) to Fe(III) by O2; in this model, Fe(III) is the substrate for the iron permease, encoded by FTR1 [11].
  • The high affinity iron uptake complex in the yeast plasma membrane (PM) consists of the ferroxidase, Fet3p, and the ferric iron permease, Ftr1p [12].
  • In turn, this might be evidence of a shielding role of the permease Ftr1, which could interact with Fet3 at the level of the aspartate-rich negatively charged region [13].

Physical interactions of FTR1

  • Siderophore-iron uptake can occur through the reduction of the complex and the subsequent uptake of iron by the high affinity iron transporter Fet3p/Ftr1p [14].

Other interactions of FTR1

  • This Ftr1p mutant supported the plasma membrane targeting of active Fet3p that is blocked in the parental ftr1delta strain [15].
  • Here, we characterize the iron transporter homologue Fth1p, which is similar to the high affinity plasma membrane iron transporter Ftr1p [16].
  • The high affinity transporters, Ftr1p and Fet3p, are primarily expressed in oxygenated cultures, whereas anaerobic conditions induce the low affinity iron transporter, Fet4p [17].
  • Supporting this is that the induction of an Aft1p target gene, FTR1, in response to iron starvation was greatly reduced in pse1-1 cells [18].
  • Epitope-tagged Arn1p was expressed in intracellular vesicles in a pattern that was indistinguishable from that of Arn3p, whereas Ftr1p, a component of the high-affinity ferrous system, was expressed on the plasma membrane [19].

Analytical, diagnostic and therapeutic context of FTR1

  • The modification of cellular iron metabolism, which involved the increased expression of high-affinity iron transport genes (FET3 and FTR1), was detected via Northern blot analysis [20].


  1. A permease-oxidase complex involved in high-affinity iron uptake in yeast. Stearman, R., Yuan, D.S., Yamaguchi-Iwai, Y., Klausner, R.D., Dancis, A. Science (1996) [Pubmed]
  2. Post-transcriptional regulation of the yeast high affinity iron transport system. Felice, M.R., De Domenico, I., Li, L., Ward, D.M., Bartok, B., Musci, G., Kaplan, J. J. Biol. Chem. (2005) [Pubmed]
  3. Genome-wide analysis of iron-dependent growth reveals a novel yeast gene required for vacuolar acidification. Davis-Kaplan, S.R., Ward, D.M., Shiflett, S.L., Kaplan, J. J. Biol. Chem. (2004) [Pubmed]
  4. The yeast FET5 gene encodes a FET3-related multicopper oxidase implicated in iron transport. Spizzo, T., Byersdorfer, C., Duesterhoeft, S., Eide, D. Mol. Gen. Genet. (1997) [Pubmed]
  5. Iron acquisition from transferrin by Candida albicans depends on the reductive pathway. Knight, S.A., Vilaire, G., Lesuisse, E., Dancis, A. Infect. Immun. (2005) [Pubmed]
  6. Evidence for iron channeling in the Fet3p-Ftr1p high-affinity iron uptake complex in the yeast plasma membrane. Kwok, E.Y., Severance, S., Kosman, D.J. Biochemistry (2006) [Pubmed]
  7. The AFT1 transcriptional factor is differentially required for expression of high-affinity iron uptake genes in Saccharomyces cerevisiae. Casas, C., Aldea, M., Espinet, C., Gallego, C., Gil, R., Herrero, E. Yeast (1997) [Pubmed]
  8. The copper-iron connection in biology: structure of the metallo-oxidase Fet3p. Taylor, A.B., Stoj, C.S., Ziegler, L., Kosman, D.J., Hart, P.J. Proc. Natl. Acad. Sci. U.S.A. (2005) [Pubmed]
  9. The siderophore iron transporter of Candida albicans (Sit1p/Arn1p) mediates uptake of ferrichrome-type siderophores and is required for epithelial invasion. Heymann, P., Gerads, M., Schaller, M., Dromer, F., Winkelmann, G., Ernst, J.F. Infect. Immun. (2002) [Pubmed]
  10. Regulation of high affinity iron uptake in the yeast Saccharomyces cerevisiae. Role of dioxygen and Fe. Hassett, R.F., Romeo, A.M., Kosman, D.J. J. Biol. Chem. (1998) [Pubmed]
  11. Spectral and kinetic properties of the Fet3 protein from Saccharomyces cerevisiae, a multinuclear copper ferroxidase enzyme. Hassett, R.F., Yuan, D.S., Kosman, D.J. J. Biol. Chem. (1998) [Pubmed]
  12. Assembly, Activation, and Trafficking of the Fet3p{middle dot}Ftr1p High Affinity Iron Permease Complex in Saccharomyces cerevisiae. Singh, A., Severance, S., Kaur, N., Wiltsie, W., Kosman, D.J. J. Biol. Chem. (2006) [Pubmed]
  13. Specific aspartate residues in FET3 control high-affinity iron transport in Saccharomyces cerevisiae. Bonaccorsi di Patti, M.C., Felice, M.R., De Domenico, I., Lania, A., Alaleona, F., Musci, G. Yeast (2005) [Pubmed]
  14. Identification of a Candida albicans ferrichrome transporter and its characterization by expression in Saccharomyces cerevisiae. Ardon, O., Bussey, H., Philpott, C., Ward, D.M., Davis-Kaplan, S., Verroneau, S., Jiang, B., Kaplan, J. J. Biol. Chem. (2001) [Pubmed]
  15. Fre1p Cu2+ reduction and Fet3p Cu1+ oxidation modulate copper toxicity in Saccharomyces cerevisiae. Shi, X., Stoj, C., Romeo, A., Kosman, D.J., Zhu, Z. J. Biol. Chem. (2003) [Pubmed]
  16. The iron transporter Fth1p forms a complex with the Fet5 iron oxidase and resides on the vacuolar membrane. Urbanowski, J.L., Piper, R.C. J. Biol. Chem. (1999) [Pubmed]
  17. Regulation of Saccharomyces cerevisiae FET4 by oxygen and iron. Jensen, L.T., Culotta, V.C. J. Mol. Biol. (2002) [Pubmed]
  18. Pse1p mediates the nuclear import of the iron-responsive transcription factor Aft1p in Saccharomyces cerevisiae. Ueta, R., Fukunaka, A., Yamaguchi-Iwai, Y. J. Biol. Chem. (2003) [Pubmed]
  19. Siderophore-iron uptake in saccharomyces cerevisiae. Identification of ferrichrome and fusarinine transporters. Yun, C.W., Tiedeman, J.S., Moore, R.E., Philpott, C.C. J. Biol. Chem. (2000) [Pubmed]
  20. Enhanced Expression of High-affinity Iron Transporters via H-ferritin Production in Yeast. Kim, K.S., Chang, Y.J., Chung, Y.J., Park, C.U., Seo, H.Y. J. Biochem. Mol. Biol. (2007) [Pubmed]
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