| First Author | Li J | Year | 2000 |
| Journal | Biochim Biophys Acta | Volume | 1467 |
| Issue | 2 | Pages | 338-46 |
| PubMed ID | 11030592 | Mgi Jnum | J:297525 |
| Mgi Id | MGI:6478859 | Doi | 10.1016/s0005-2736(00)00232-7 |
| Citation | Li J, et al. (2000) Functional significance of N- and C-terminus of the amino acid transporters EAAC1 and ASCT1: characterization of chimeric transporters. Biochim Biophys Acta 1467(2):338-46 |
| abstractText | 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. |
