<Review>Molecular biology of L-type amino acid transporters

概要

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Amino acid membrane transport systems have been identified and classified since the 1960s. In the 1990s, the cDNA of solute carrier 7 (SLC7) for humans and a number of animal models were cloned, and the primary structures and properties have been clarified in recent years. SLC7 consists of eleven transporters (y^+LAT1, y^+LAT2, Asc-1, LAT1, LAT2, xCT, BAT1, CAT1, CATS, CAT2, and CAT4), and the L-type amino acid transporter (LAT) subfamily is involved in neutral amino acid transport. Some members in this subfamily are involved in the function of the blood-brain barrier, while the expression levels of some members are elevated in actively proliferating cancer cells. Multiple (12-time) transmembrane proteins in the LAT family with a molecular weight of about 40kDa (y^+LAT1, y^+LAT2, Asc-1, LAT1, LAT2, xCT and BAT1) form heterodimers with a single transmembrane chaperone-like protein with a molecular weight of about 8OkDa (4F2hc and rBAT) to express transport functions. These transporters are the first of their kind found to require a heterodimeric form to express function. This discovery should assist the development of strategies for research into protein-protein interactions in the post-genome era.
茨城県立医療大学の論文