Abstract
The norepinephrine transporter(NET) is a member of the Na+/Cl- dependent neurotransmitter transporter family and constitutes the target of several clinically important antidepressants. To delineate the critical amino acid residues and the function of C-terminal in regulating transport activity of NET, here we constructed two site mutants (V70F, F72V; V70I, F72V) and one C-terminal truncated mutant (△ 611-617). The wild type and mutants of NET were expressed in Xenopus oocytes by injection of their cRNA. We found that all of these mutants lost their transport activity. These results indicate that the amino acid residues of V70 and F72 , and the last seven amino acids of C-terminal are essential to the transport activity of NET.
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Acknowledgements
We thank Dr. Philip Wood, Dr. Ursula Eckstein-Ludwig, Mrs. Eva-Maria Gaertner, Mrs Heike Biel at Max-Plank Institute fuer Biophysik.
This research work is supported by Young Scientist Foundation from Chinese Academy of Sciences and Qi Ming Xing Foundation from Shanghai Science and Technology Committee.
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Liu, Y., Huang, F., Fei, J. et al. Val 70, Phe 72 and the last seven amino acid residues of C-terminal are essential to the function of norepinephrine transporter. Cell Res 8, 311–315 (1998). https://doi.org/10.1038/cr.1998.31
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DOI: https://doi.org/10.1038/cr.1998.31