Castagna M, Bossi E, Sacchi V F
Institute of General Physiology and Biological Chemistry 'G. Esposito', University of Milan, Milano, Italy.
Insect Mol Biol. 2009 Jun;18(3):265-79. doi: 10.1111/j.1365-2583.2009.00881.x. Epub 2009 Apr 6.
K-activated amino acid transporter 1 (KAAT1) and cation-anion-activated amino acid transporter/channel 1 (CAATCH1) are amino acid cotransporters, belonging to the Na/Cl-dependent neurotransmitter transporter family (also called SLC6/NSS), that have been cloned from Manduca sexta midgut. They have been thoroughly studied by expression in Xenopus laevis oocytes, and structure/function analyses have made it possible to identify the structural determinants of their cation and amino acid selectivity. About 40 mutants of these proteins have been studied by measuring amino acid uptake and current/voltage relationships. The results obtained since the cloning of KAAT1 and CAATCH1 are here discussed in the light of the 3D model of the first crystallized member of the family, the leucine transporter LeuT.
钾激活氨基酸转运体1（KAAT1）和阳离子-阴离子激活氨基酸转运体/通道1（CAATCH1）是氨基酸共转运体，属于Na/Cl依赖性神经递质转运体家族（也称为SLC6/NSS），已从烟草天蛾中肠克隆得到。通过在非洲爪蟾卵母细胞中表达对它们进行了深入研究，结构/功能分析使得鉴定其阳离子和氨基酸选择性的结构决定因素成为可能。通过测量氨基酸摄取和电流/电压关系，已对这些蛋白质的约40个突变体进行了研究。鉴于该家族第一个结晶成员亮氨酸转运体LeuT的三维模型，在此讨论自KAAT1和CAATCH1克隆以来所获得的结果。
