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J. Biol. Chem., Vol. 279, Issue 4, 2754-2760, January 23, 2004

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The Proton/Amino Acid Cotransporter PAT2 Is Expressed in Neurons with a Different Subcellular Localization than Its Paralog PAT1^*

Isabel Rubio-Aliaga¶, Michael Boll¶, Daniela M. Vogt Weisenhorn||, Martin Foltz, Gabor Kottra, and Hannelore Daniel**

From the Molecular Nutrition Unit, Technical University of Munich, Hochfeldweg 2, D-85350 Freising-Weihenstephan, Germany and the ^||National Research Center, Institute of Developmental Genetics, Ingostädter Landstrasse 1, D-85764 Neuherberg, Germany

The new member of the mammalian amino acid/auxin permease family, PAT2, has been cloned recently and represents an electrogenic proton/amino acid symporter. PAT2 and its paralog, PAT1/LYAAT-1, are transporters for small amino acids such as glycine, alanine, and proline. Our immunodetection studies revealed that the PAT2 protein is expressed in spinal cord and brain. It is found in neuronal cell bodies in the anterior horn in spinal cord and in brain stem, cerebellum, hippocampus, hypothalamus, rhinencephalon, cerebral cortex, and olfactory bulb in the brain. PAT2 is expressed in neurons positive for the N-methyl-D-aspartate subtype glutamate receptor subunit NR1. PAT2 is not found in lysosomes, unlike its paralog PAT1, but is present in the endoplasmic reticulum and recycling endosomes in neurons. PAT2 has a high external proton affinity causing half-maximal transport activation already at a pH of 8.3, suggesting that its activity is most likely not altered by physiological pH changes. Transport of amino acids by PAT2 activity is dependent on membrane potential and can occur bidirectionally; membrane depolarization causes net glycine outward currents. Our data suggest that PAT2 contributes to neuronal transport and sequestration of amino acids such as glycine, alanine, and/or proline, whereby the transport direction is dependent on the sum of the driving forces such as substrate concentration, pH gradient, and membrane potential.

Received for publication, May 28, 2003 , and in revised form, September 24, 2003.

^* This research was supported by Deutsche Forschungsgemeinschaft (FSG) Grant BO 1857/1 (to M. B.). 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.

Present address: Division of Hematology, Children's Hospital, Harvard Medical School, 300 Longwood Ave., Boston, MA 02115.

^¶ These authors contributed equally to this work.

^** To whom correspondence should be addressed. Tel.: 49-8161-713400; Fax: 49-8161-713999; E-mail: daniel{at}wzw.tum.de.

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