Abolition of substrate-dependent currents by tyrosine mutation in the transmembrane domain of glutamate transporter.
Abolition of substrate-dependent currents by tyrosine mutation in the transmembrane domain of glutamate transporter.
复制标题
通过谷氨酸转运蛋白跨膜结构域中的酪氨酸突变消除底物依赖性电流。
DOI：
10.1016/s0014-5793(97)00155-5
复制
发表时间：
1997
期刊：
影响因子：
3.5
通讯作者：
Chiu,SY
中科院分区：
文献类型：
--
作者：
Choi,I;Chiu,SY
By site-directed mutagenesis we examined the roles of tyrosine residues (Tyr127) in the putative transmembrane domain of rat glutamate transporter (GLAST). When expressed in Xenopus oocytes, Y127F mutant protein, which was localized in plasma membranes of oocytes, completely abolished glutamate uptake currents but did not affect the intrinsic substrate-independent currents. Coexpression of wild type and mutant transporters supports that the Y127F mutation did not elicit glutamate efflux. The efflux of glutamate by wild type or Y127F mutant transporters was measured under the condition of ion perturbation where transporters run in the reverse direction. ©1997 Federation of European Biochemical Societies.
