Molecular physiology of the insect K-activated amino acid transporter 1 (KAAT1) and cation-anion activated amino acid transporter/channel 1 (CAATCH1) in the light of the structure of the homologous protein LeuT

被引：15
|
作者：
Castagna, M. [1 ]
Bossi, E. [2 ,3 ]
Sacchi, V. F. [1 ]
机构：
[1] Univ Milan, Sch Pharm, Inst Gen Physiol & Biol Chem G Esposito, I-20134 Milan, Italy
[2] Univ Insubria, Dept Biotechnol & Mol Sci, Varese, Italy
[3] Univ Insubria, Ctr Neurosci, Varese, Italy
来源：
INSECT MOLECULAR BIOLOGY | 2009年 / 18卷 / 03期
关键词：
Cotransporters; homology modelling; SLC6; NSS family; KAAT1; CAATCH1; amino acid transport; ION-BINDING; SUBSTRATE SELECTIVITY; SEROTONIN TRANSPORTER; TRANSMEMBRANE DOMAIN; OLIGOMERIC STRUCTURE; NEUROTRANSMITTER; PH; PERMEATION; MECHANISM; SODIUM;
D O I：
10.1111/j.1365-2583.2009.00881.x
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
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.
引用
收藏
页码：265 / 279
页数：15
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