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Gene Review

FET4  -  Fet4p

Saccharomyces cerevisiae S288c

Synonyms: Low-affinity Fe(2+) transport protein, Low-affinity Fe(II) transport protein, YM9924.11C, YMR319C
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Disease relevance of FET4

  • First, FET4 repression by Rox1p under oxygenated conditions helps minimize metal toxicity [1].

High impact information on FET4

  • In contrast, a screen of high-copy number plasmid libraries for clones able to increase tolerance to alkaline pH revealed only two genes: FET4 (encoding a low affinity transporter for copper, iron, and zinc) and CTR1 (encoding a high affinity copper transporter) [2].
  • Second, FET4 is regulated by zinc status via the Zap1 transcription factor [3].
  • Finally, FET4 expression is regulated in response to oxygen by the Rox1 repressor [3].
  • First, we found that FET4 expression is induced in iron-limited cells by the Aft1 iron-responsive transcriptional activator [3].
  • Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen [3].

Chemical compound and disease context of FET4

  • Sensitivity towards cadmium was high in either anaerobically grown wild-type yeast or in oxygenated rox1Delta strains, and in both cases cadmium toxicity was reversed by FET4 mutations [1].

Biological context of FET4

  • This BSD2 control of ion transport occurs independently of the CTR1 and FET4 metal transport systems [4].
  • The region surrounding approximately -960 to -490 contains two consensus Rox1p binding sites and mediates Rox1p, but not iron control of FET4 [1].

Anatomical context of FET4

  • Consistent with its role as an Fe2+ transporter, FET4 is an integral membrane protein present in the plasma membrane [5].

Associations of FET4 with chemical compounds

  • The FET4 gene encodes an Fe(II) transporter required for low-affinity uptake [6].

Other interactions of FET4

  • Fet4p is not the only metal transporter that is negatively regulated by oxygen; we find that Rox1p also represses S. cerevisiae SMF3, proposed to function in vacuolar iron transport [1].
  • The high affinity transporters, Ftr1p and Fet3p, are primarily expressed in oxygenated cultures, whereas anaerobic conditions induce the low affinity iron transporter, Fet4p [1].
  • For these experiments, we utilized yeast lacking the major iron uptake pathways (FET3 and FET4) and yeast deficient in SIT1, encoding the major up-regulated iron siderophore transporter [7].
  • An sod1/fet3 double mutant showed increased sensitivity to oxygen and increased transcription of FET4, an alternative, low affinity, iron transporter [8].
  • We present evidence that FET4 is a physiologically relevant zinc transporter and this provides a rationale for its regulation by Zap1 [3].


  1. Regulation of Saccharomyces cerevisiae FET4 by oxygen and iron. Jensen, L.T., Culotta, V.C. J. Mol. Biol. (2002) [Pubmed]
  2. Copper and iron are the limiting factors for growth of the yeast Saccharomyces cerevisiae in an alkaline environment. Serrano, R., Bernal, D., Simón, E., Ariño, J. J. Biol. Chem. (2004) [Pubmed]
  3. Combinatorial control of yeast FET4 gene expression by iron, zinc, and oxygen. Waters, B.M., Eide, D.J. J. Biol. Chem. (2002) [Pubmed]
  4. Negative control of heavy metal uptake by the Saccharomyces cerevisiae BSD2 gene. Liu, X.F., Supek, F., Nelson, N., Culotta, V.C. J. Biol. Chem. (1997) [Pubmed]
  5. Characterization of the FET4 protein of yeast. Evidence for a direct role in the transport of iron. Dix, D., Bridgham, J., Broderius, M., Eide, D. J. Biol. Chem. (1997) [Pubmed]
  6. 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]
  7. Relationship between chloroquine toxicity and iron acquisition in Saccharomyces cerevisiae. Emerson, L.R., Nau, M.E., Martin, R.K., Kyle, D.E., Vahey, M., Wirth, D.F. Antimicrob. Agents Chemother. (2002) [Pubmed]
  8. Yeast lacking Cu-Zn superoxide dismutase show altered iron homeostasis. Role of oxidative stress in iron metabolism. De Freitas, J.M., Liba, A., Meneghini, R., Valentine, J.S., Gralla, E.B. J. Biol. Chem. (2000) [Pubmed]
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