Structure and function of cationic amino acid transporters (CATs)

• Published in: The Journal of membrane biology Vol. 213; no. 2; pp. 67 - 77
• Main Authors: Closs, E I, Boissel, J-P, Habermeier, A, Rotmann, A
• Format: Journal Article
• Language: English
• Published: United States Springer Nature B.V 01-09-2006
• Subjects: Amino Acid Transport Systems, Basic - chemistry; Amino Acid Transport Systems, Basic - classification; Amino Acid Transport Systems, Basic - genetics; Amino Acid Transport Systems, Basic - metabolism; Amino acids; Animals; Binding Sites - genetics; Gene Expression Regulation; Humans; Ion Transport; Models, Biological; Models, Molecular; Molecular biology; Molecular Structure; Mutation; Pharmacology; Proteins; Signal Transduction; Subcellular Fractions - metabolism
• ISSN: 0022-2631; 1432-1424
• DOI: 10.1007/s00232-006-0875-7

The CAT proteins (CAT for cationic amino acid transporter) are amongst the first mammalian amino acid transporters identified on the molecular level and seem to be the major entry path for cationic amino acids in most cells. However, CAT proteins mediate also efflux of their substrates and thus may also deplete cells from cationic amino acids under certain circumstances. The CAT proteins form a subfamily of the solute carrier family 7 (SLC7) that consists of four confirmed transport proteins for cationic amino acids: CAT-1 (SLC7A1), CAT-2A (SLC7A2A), CAT-2B (SLC7A2B), and CAT-3 (SLC7A3). SLC7A4 and SLC7A14 are two related proteins with yet unknown function. One focus of this review lies on structural and functional differences between the different CAT isoforms. The expression of the CAT proteins is highly regulated on the level of transcription, mRNA stability, translation and subcellular localization. Recent advances toward a better understanding of these mechanisms provide a second focus of this review.