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J. Biol. Chem., Vol. 280, Issue 25, 24267-24276, June 24, 2005

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AGP2 Encodes the Major Permease for High Affinity Polyamine Import in Saccharomyces cerevisiae^*

Mustapha Aouida, Anick Leduc, Richard Poulin¶||, and Dindial Ramotar**

From the Guy-Bernier Research Center, Maisonneuve-Rosemont Hospital, Montreal, Quebec H1T 2M4, Canada and the ^¶Oncological and Molecular Endocrinology Research Center, CHUL Medical Research Center (CHUQ), Ste. Foy, Quebec G1V 4G2, Canada

Polyamines play essential functions in many aspects of cell biology. Plasma membrane transport systems for the specific uptake of polyamines exist in most eukaryotic cells but have been very recently identified at the molecular level only in the parasite Leishmania. We now report that the high affinity polyamine permease in Saccharomyces cerevisiae is identical to Agp2p, a member of the yeast amino acid transporter family that was previously identified as a carnitine transporter. 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 agp2 mutants. Yeast mutants deficient in polyamine biosynthesis required >10-fold higher concentrations of exogenous putrescine to restore cell proliferation upon deletion of the AGP2 gene. Disruption of END3, a gene required for an early step of endocytosis, increased the abundance of Agp2p, an effect that was paralleled by a marked up-regulation of spermidine transport velocity. Thus, AGP2 encodes the first eukaryotic permease that preferentially uses spermidine over putrescine as a high affinity substrate and plays a central role in the uptake of polyamines in yeast.

Received for publication, March 21, 2005 , and in revised form, April 26, 2005.

^* This work was supported in part by Canadian Institutes of Health Research Grant MT-121391 (to D. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains an additional figure.

Recipient of an internal postdoctoral fellowship.

^|| Recipient of a senior fellowship from the Fonds de la Recherche en Santé du Québec. To whom correspondence may be addressed: Oncological and Molecular Endocrinology Research Center, CHUL Medical Research Center (CHUQ), 2705 Laurier Blvd., Ste. Foy, Quebec G1V 4G2, Canada. Tel.: 418-525-4444 (ext. 46234); Fax: 418-654-2761; E-mail: richard.poulin{at}crchul.ulaval.ca.

^** Recipient of a senior fellowship from the Fonds de la Recherche en Santé du Québec. To whom correspondence may be addressed: Maisonneuve-Rosemont Hospital, Guy-Bernier Research Center, 5415, Boul. de l'Assomption, Montreal, Quebec H1T 2M4, Canada. Tel.: 514-252-3400 (ext. 4684); Fax: 514-252-3430; E-mail: dramotar.hmr{at}ssss.gouv.qc.ca.

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