Different functional roles of arginine residues 39 and 61 and tyrosine residue 98 in transport and channel mode of the glutamate transporter EAAC1
文献类型：期刊论文
| 作者 | Zhu, YN; Vasilets, LA; Fei, J; Guo, LH; Schwarz, W |
| 刊名 | BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES
 |
| 出版日期 | 2004 |
| 卷号 | 1665期号:1页码:20-28 |
| 关键词 | Xenopus oocyte glutamate uptake EAAC1-mediated current |
| 通讯作者 | Fei, J (reprint author), Max Planck Inst Biophys, Maire Curie Str 15, D-60439 Frankfurt, Germany.,jfei@sibs.ac.cn ; schwarz@mpibp-frankfurt.mpg.de |
| 英文摘要 | The excitatory amino acid transporter EAAC1 is an electrogenic Na+- and K+-gradient-driven transporter. In addition, the transporter mediates in the presence of Na+ and glutamate an anion conductance uncoupled from the transport of the glutamate. The first two N-terminal domains, important for forming the conductance mode, are extracellularly bordered by positively charged arginine residues, R39 and R61, being completely conserved throughout the transporter family. Also the conserved tyrosine residue Y98 could be important for Cl- conductance. We have investigated, by measurements of glutamate uptake and glutamate-induced currents, the effects of mutation of the arginines and the tyrosine to alanine. The mutation R39A hardly affects transport and channel mode. The mutation R61A, on the other hand, reduces the activity of transport but stimulates the channel conductance. In addition, the apparent K, values for glutamate uptake and for the glutamate-activated current are reduced. Glutamate stimulation of current seems to be associated with a voltage-dependent step, and the apparent valence of charge moved during binding is reduced in the R61A mutant. The mutation Y98A leads to reduced function with reduced apparent K-m value for glutamate, and with strong reduction of the selectivity ration between NO3- and Cl-_ of the conductance mode. (C) 2004 Elsevier B.V. All rights reserved. |
| 学科主题 | Biochemistry & Molecular Biology; Biophysics |
| 类目[WOS] | Biochemistry & Molecular Biology ; Biophysics |
| 关键词[WOS] | AMINO-ACID TRANSPORTER ; CHLORIDE CHANNEL ; XENOPUS-LAEVIS ; RAT-BRAIN ; EXPRESSION ; CURRENTS ; OOCYTES ; CONDUCTANCE ; MUTATION ; FLUXES |
| 收录类别 | SCI |
| 语种 | 英语 |
| WOS记录号 | WOS:000224462900003 |
| 版本 | 出版稿 |
| 源URL | [http://202.127.25.143/handle/331003/2194]  |
| 专题 | 上海生化细胞研究所_上海生科院生化细胞研究所 |
| 推荐引用方式 GB/T 7714 | Zhu, YN,Vasilets, LA,Fei, J,et al. Different functional roles of arginine residues 39 and 61 and tyrosine residue 98 in transport and channel mode of the glutamate transporter EAAC1[J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,2004,1665(1):20-28. |
| APA | Zhu, YN,Vasilets, LA,Fei, J,Guo, LH,&Schwarz, W.(2004).Different functional roles of arginine residues 39 and 61 and tyrosine residue 98 in transport and channel mode of the glutamate transporter EAAC1.BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES,1665(1),20-28. |
| MLA | Zhu, YN,et al."Different functional roles of arginine residues 39 and 61 and tyrosine residue 98 in transport and channel mode of the glutamate transporter EAAC1".BIOCHIMICA ET BIOPHYSICA ACTA-BIOMEMBRANES 1665.1(2004):20-28. |
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