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AGP2  -  Agp2p

Saccharomyces cerevisiae S288c

Synonyms: General amino acid permease AGP2, YBR1007, YBR132C
 
 
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Disease relevance of AGP2

  • Deletion of AGP2 dramatically reduces the initial velocity of spermidine and putrescine uptake and confers strong resistance to the toxicity of exogenous polyamines, and transformation with an AGP2 expression vector restored polyamine transport in agp2delta mutants [1].
 

High impact information on AGP2

 

Biological context of AGP2

 

Anatomical context of AGP2

 

Associations of AGP2 with chemical compounds

  • Both Agp2p and Agp3p are low affinity permeases for leucine (Kmapp 0.2-0.5 mM) and are expressed at lower levels than other permeases on all media tested [6].
  • In the ssk1delta stelldelta double-mutant strain, the expression of AGP2 and the uptake of carnitine were greatly reduced compared to the wild-type strain [5].
  • The expression of AGP2 was down-regulated by osmotic stresses, including NaCl, sorbitol, and KCI [5].
  • YBR1007 shows strong similarities to amino-acid permeases, in particular the high-affinity proline permeases of S. cerevisiae and A. nidulans [4].
 

Other interactions of AGP2

  • The gene AGP2 and the ORF YFL055w (here named AGP3) are classified as members of the yeast amino acid permease gene family [6].
  • Transcription of AGP2 and AGP3 is very low but is increased in cells lacking other functional general amino acid permeases (Gap1p or Agp1p) [6].
  • Carnitine uptake by AGP2 in yeast Saccharomyces cerevisiae is dependent on Hog1 MAP kinase pathway [5].
  • Deletion of FES1 or AGP2 resulted in reduced polyamine uptake [7].

References

  1. AGP2 encodes the major permease for high affinity polyamine import in Saccharomyces cerevisiae. Aouida, M., Leduc, A., Poulin, R., Ramotar, D. J. Biol. Chem. (2005) [Pubmed]
  2. Molecular characterization of carnitine-dependent transport of acetyl-CoA from peroxisomes to mitochondria in Saccharomyces cerevisiae and identification of a plasma membrane carnitine transporter, Agp2p. van Roermund, C.W., Hettema, E.H., van den Berg, M., Tabak, H.F., Wanders, R.J. EMBO J. (1999) [Pubmed]
  3. A genome-wide screen in Saccharomyces cerevisiae reveals altered transport as a mechanism of resistance to the anticancer drug bleomycin. Aouida, M., Pagé, N., Leduc, A., Peter, M., Ramotar, D. Cancer Res. (2004) [Pubmed]
  4. An analysis of the sequence of part of the right arm of chromosome II of S. cerevisiae reveals new genes encoding an amino-acid permease and a carboxypeptidase. Nasr, F., Bécam, A.M., Grzybowska, E., Zagulski, M., Slonimski, P.P., Herbert, C.J. Curr. Genet. (1994) [Pubmed]
  5. Carnitine uptake by AGP2 in yeast Saccharomyces cerevisiae is dependent on Hog1 MAP kinase pathway. Lee, J., Lee, B., Shin, D., Kwak, S.S., Bahk, J.D., Lim, C.O., Yun, D.J. Mol. Cells (2002) [Pubmed]
  6. Yeast Agp2p and Agp3p function as amino acid permeases in poor nutrient conditions. Schreve, J.L., Garrett, J.M. Biochem. Biophys. Res. Commun. (2004) [Pubmed]
  7. Mechanism of polyamine tolerance in yeast: novel regulators and insights. Porat, Z., Wender, N., Erez, O., Kahana, C. Cell. Mol. Life Sci. (2005) [Pubmed]
 
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