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Functional significance of N- and C-terminus of the amino acid transporters EAAC1 and ASCT1: characterization of chimeric transporters

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Li,  J.
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;
Shanghai Institute of Cell Biology, Chinese Academy of Sciences, 320 Yue Yang Lu, 200031 Shanghai, China;

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Schwarz,  Wolfgang
Department of Biophysical Chemistry, Max Planck Institute of Biophysics, Max Planck Society;

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Zitation

Li, J., Fei, J., Huang, F., Guo, L., & Schwarz, W. (2000). Functional significance of N- and C-terminus of the amino acid transporters EAAC1 and ASCT1: characterization of chimeric transporters. Biochimica et Biophysica Acta-Biomembranes, 1467(2), 338-346. doi:10.1016/S0005-2736(00)00232-7.


Zitierlink: https://hdl.handle.net/21.11116/0000-0007-DDEB-8
Zusammenfassung
To localize functionally significant domains in the amino acid transporters of mouse brain mEAAC1 and mASCT1, cRNA encoding for wild-type and chimeric transporters was injected into Xenopus oocytes. Activity of expressed transporters was investigated by measurements of uptake of 3H-labeled glutamate and serine and of glutamate- and serine-induced currents under voltage clamp. Though all transporters accept glutamate and serine as substrate, the central part of the protein (Ala94-Met418 of mEAAC1 and Ala119-Ile393 of mASCT1) determines substrate selectivity. The C-terminus rectifies the interaction with the respective substrate. A channel mode of the glutamate transporter can be activated by glutamate and serine, and the N- and C-termini of the mEAAC1 seem to be essential for the channel formation.