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Agp2, a Member of the Yeast Amino Acid Permease Family, Positively Regulates Polyamine Transport at the Transcriptional Level


Mustapha Aouida​, Marta Rubio Texeira, Johan M. Thevelein, Richard Poulin  and Dindial Ramotar. AGP2 Encodes a Multifunctional Transceptor that Positively Regulates Polyamine Transport.  PLoS One. 2013 Jun 3;8(6):e65717. doi: 10.1371/journal.pone.0065717. Print 2013


Mustapha Aouida, Marta Rubio Texeira, Johan M. Thevelein, Richard Poulin, Dindial Ramotar


sensor, polyamine transporters, toxicity, transcription factors, microarray analysis, gene expression profiler




Agp2 is a plasma membrane protein of the Saccharomyces cerevisiae amino acid transporter family, involved in high-affinity uptake of various substrates including L-carnitine and polyamines. The discovery of two high affinity polyamine permeases, Dur3 and Sam3, prompted us to investigate whether Agp2 directly transports polyamines or acts instead as a regulator. Herein, we show that neither dur3D nor sam3D single mutant is defective in polyamine transport, while the dur3D sam3D double mutant exhibits a sharp decrease in polyamine uptake and an increased resistance to polyamine toxicity similar to the agp2D mutant. Studies of Agp2 localization indicate that in the double mutant dur3D sam3D, Agp2-GFP remains plasma membrane-localized, even though transport of polyamines is strongly reduced. We further demonstrate that Agp2 controls the expression of several transporter genes including DUR3 and SAM3, the carnitine transporter HNM1 and several hexose, nucleoside and vitamin permease genes, in addition to SKY1 encoding a SR kinase that positively regulates low-affinity polyamine uptake. Furthermore, gene expression analysis clearly suggests that Agp2 is a strong positive regulator of additional biological processes. Collectively, our data suggest that Agp2 might respond to environmental cues and thus regulate the expression of several genes including those involved in polyamine transport.