Palacı́n, Manuel, Raúl Estévez, Joan Bertran, and Antonio Zorzano. Molecular Biology of
Mammalian Plasma Membrane Amino Acid Transporters. Physiol. Rev. 78: 969–1054, 1998 …

Devés, R., and CAR Boyd. Transporters for Cationic Amino Acids in Animal Cells: Discovery,
Structure, and Function. Physiol. Rev. 78: 487–545, 1998.—The structure and function of the …

Cystinuria is a classic heritable aminoaciduria that involves the defective transepithelial
transport of cystine and dibasic amino acids in the kidney and intestine. Six missense …

Glycoprotein-associated amino acid transporters (gpaAT) are permease-related proteins
that require heterodimerization to express their function. So far, four vertebrate gpaATs have …

Heterodimeric amino acid transporters are comprised of two subunits, a polytopic membrane
protein (light chain) and an associated type II membrane protein (heavy chain). The heavy …

Cystinuria (MIM 220100) is a common recessive disorder of renal reabsorption of cystine
and dibasic amino acids. Mutations in SLC3A1, encoding rBAT, cause cystinuria type I (ref …

We have identified a new human cDNA (y+ L amino acid transporter-1 (y+ LAT-1)) that
induces system y+ L transport activity with 4F2hc (the surface antigen 4F2 heavy chain) in …

The heteromeric amino acid transporters (HATs) are composed of two polypeptides: a heavy
subunit (HSHAT) and a light subunit (LSHAT) linked by a disulfide bridge. HSHATs are N …

The heteromeric amino acid transporters (HATs) are composed of a light and a heavy
subunit linked by a disulfide bridge. The heavy subunits are the SLC3 members (rBAT and …

Members of the newly discovered glycoprotein-associated amino acid transporter family
(gpaAT-family) share a similar primary structure with> 40% identity, a predicted 12 …