Click here to close Hello! We notice that you are using Internet Explorer, which is not supported by Xenbase and may cause the site to display incorrectly. We suggest using a current version of Chrome, FireFox, or Safari.
XB-ART-10165
Biochim Biophys Acta 2000 Aug 25;14672:338-46.
Show Gene links Show Anatomy links

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

Li J , Fei J , Huang F , Guo LH , Schwarz W .


???displayArticle.abstract???
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.

???displayArticle.pubmedLink??? 11030592
???displayArticle.link??? Biochim Biophys Acta


Species referenced: Xenopus laevis
Genes referenced: slc1a1 slc1a4