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M200019200v1
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Papers In Press, published online ahead of print March 20, 2002
J. Biol. Chem, 10.1074/jbc.M200019200
Submitted on January 2, 2002
Revised on February 26, 2002
Accepted on March 19, 2002

Identification of a novel Na+-independent acidic amino acid transprter with structural similarity to the member of heterodimeric amino acid transporter family associated with unknown heavy chains

Hirotaka Matsuo, Yoshikatsu Kanai, Ju Young Kim, Arthit Chairoungdua, Do Kyung Kim, Jun Inatomi, Yasuhiro Shigeta, Hisako Ishimine, Sophapun Chaekuntode, Kittipong Tachampa, Hye Won Choi, Ellappan Babu, Jun Fukuda, and Hitoshi Endou

Department of Pharmacology and Toxicology, Kyorin University School of Medicine, Mitaka, Tokyo 181-8611

Corresponding Author: ykanai{at}kyorin-u.ac.jp

We identified a novel Na+-independent acidic amino acid transporter designated AGT1 (aspartate/glutamate transporter 1). AGT1 exhibits the highest sequence similarity (48% identity) to the Na+-independent small neutral amino acid transporter Asc-2, a member of the heterodimeric amino acid transporter family presumed to be associated with unknown heavy chains. The cysteine residue responsible for the disulfide bond formation between transporters (light chains) and heavy chain subunits of the heterodimeric amino acid transporter family is conserved for AGT1. Because AGT1 solely expressed or co-expressed with already known heavy chains 4F2hc or rBAT did not induce functional activity, we generated fusion proteins in which AGT1 was connected with 4F2hc or rBAT. The fusion proteins were sorted to the plasma membrane and expressed the Na+-independent transport activity for acidic amino acids. Distinct from Na+-independent cystine/glutamate transporter xCT structurally related to AGT1, AGT1 did not accept cystine, homocysteate and L-a-aminoadipate, and exhibited high affinity to aspartate as well as glutamate, suggesting that the negative charge recognition site in the side chain binding site of AGT1 would be closer to the a-carbon binding site compared with that of xCT. AGT1 message was predominantly expressed in kidney. In mouse kidney, AGT1 protein was present in the basolateral membrane of the proximal straight tubules and distal convoluted tubules. In the Western blot analysis, AGT1 was detected as a high molecular weight band in the nonreducing condition, whereas the band shifted to a 40-kDa band corresponding to the AGT1 monomer in the reducing condition, suggesting the association of AGT1 with other proteinvia a disulfide bond. The finding of AGT1 as well as Asc-2 has established a new subgroup of the heterodimeric amino acid transporter family which associate not with 4F2hc or rBAT but with other unknown heavy chains.


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