The solute carrier family 38 (SLC38) of probable sodium-coupled neutral amino acid transporter comprises 11 members in the human genome and closely related mammalian genomes. They are widely found in plants, animals, yeast, fungi, bacteria, archaea, unicellular eukaryotic protists, and slime molds. The SLC38 family belongs to the amino acid-polyamine-organocation family of transporters. All transporters in this family are Na+ dependent and mediate the efflux of small neutral amino acids. Therefore, they are particularly expressed in actively growing cells, or in cells undergoing significant amino acid metabolisms, such as kidney, liver, and brain. The SLC38 transporters are present in membranes that face intercellular space or blood vessels, but not in the apical membrane of absorptive epithelia. In the placenta, they play an important role in the transfer of amino acids to the fetus.
Fig.1 Proposed roles of SLC38 transporters in the liver. (Bröer, 2014)
SLC38 family transporters are highly regulated by stimuli such as amino acid depletion, osmolarity, hormones, and cell growth. Expression of SLC38 transporters during cell growth is essential because they allow the amino acids to enter the cells, whereas many other amino acid transporters are obligatory antiporters. They have been proposed as transceptors independent of their transport function. Transporters of the SLC38 family provide potential to treat disease states. Inhibition of SNAT2 could prevent ER stress in pancreatic beta cells, and inhibition of SNAT5 could be beneficial for myc-driven cancers. Development of specific inhibitors would be greatly facilitated by improving the structure of mammalian members of the SLC38 family.
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