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Papers In Press, published online ahead of print January 19, 2005
J. Biol. Chem, 10.1074/jbc.M408638200
Submitted on July 29, 2004
Revised on January 19, 2005
Accepted on January 19, 2005

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

Biochemistry and Molecular Biology, University of Barcelona, Barcelona E-08028

Corresponding Author: restevez{at}pcb.ub.es

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 sulphydryl-specific reagent N-ethyl maleimide (NEM), but not the one with high affinity. Mutation in LAT4 of the SLC43 conserved serine 297 to alanine abolishes sensitivity to NEM. 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.


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