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J. Biol. Chem., Vol. 280, Issue 12, 12002-12011, March 25, 2005

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Identification of LAT4, a Novel Amino Acid Transporter with System L Activity^*

Susanna Bodoy, Lorena Martín, Antonio Zorzano, Manuel Palacín, Raúl Estévez¶||, and Joan Bertran¶

From the Department of Biochemistry and Molecular Biology, University of Barcelona, Avda Diagonal 645, Barcelona E-08028 and Parc Científic de Barcelona, Josep Samitier 1-5, Barcelona E-08028, Spain

System L amino acid transporters mediate the movement of bulky neutral amino acids across cell membranes. Until now three proteins that induce system L activity have been identified: LAT1, LAT2, and LAT3. The former two proteins belong to the solute carrier family 7 (SLC7), whereas the latter belongs to SLC43. In the present study we present a new cDNA, designated LAT4, which also mediates system L activity when expressed in Xenopus laevis oocytes. Human LAT4 exhibits 57% identity to human LAT3. Like LAT3, the amino acid transport activity induced by LAT4 is sodium-, chloride- and pH-independent, is not trans-stimulated, and shows two kinetic components. The low affinity component of LAT4 induced activity is sensitive to the sulfhydryl-specific reagent N-ethylmaleimide but not that with high affinity. Mutation in LAT4 of the SLC43 conserved serine 297 to alanine abolishes sensitivity to N-ethylmaleimide. LAT4 activity is detected at the basolateral membrane of PCT kidney cells. In situ hybridization experiments show that LAT4 mRNA is restricted to the epithelial cells of the distal tubule and the collecting duct in the kidney. In the intestine, LAT4 is mainly present in the cells of the crypt.

Received for publication, July 29, 2004 , and in revised form, December 30, 2004.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBank^TM/EBI Data Bank with accession number(s)BK005642 (human LAT4) and BK005643 (mouse LAT4)

^* This study was supported in part by the Instituto de Salud Carlos III (networks G03/054 and C03/08), by the Comissionat per a Universitats I Recerca, and by the Spanish Ministry of Science and Technology (Grant SAF03-08940-C02-01) and by the European Commission Grant EUGINDAT LSHM-CT-2003-502852 (to M. P.). 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.

Recipient of a fellowship from the Parc Científic de Barcelona.

Recipient of a fellowship from the Comissió Interdepartmental de Recerca i Innovació Technològica.

^¶ Researchers from the Programa Ramón y Cajal of the Spanish Ministry of Science and Technology. Contributed equally to this study.

^|| To whom correspondence may be addressed. Tel.: 34-93-4034700; Fax: 34-93-4034717; E-mail: restevez{at}pcb.ub.es.** To whom correspondence may be addressed. Tel.: 34-93-4034700; Fax: 34-93-4034717; E-mail: jbertran{at}ub.edu.

^** To whom correspondence may be addressed. Tel.: 34-93-4034700; Fax: 34-93-4034717; E-mail: jbertran{at}ub.edu.

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