Abstract:
:We have investigated the possible role of selected negatively-charged amino acids of the sodium and chloride-coupled GABA transporter GAT-1 on sodium binding. These residues located adjacent to putative transmembrane domains and which are conserved throughout the large superfamily of neurotransmitter transporters were changed by site-directed mutagenesis. The functional consequences were that one of the residues, glutamate-101, was critical for transport. Its replacement by aspartate left only 1% of the activity, and no activity could be detected when it was replaced by other residues. Expression levels and targeting to the plasma membrane of the mutant transporters appeared normal. Transient sodium currents were not observed in the mutants, and increased sodium concentrations did not affect the percentage of wild type transport of the E101D mutant. It is concluded that residue glutamate-101 is critical for one or more of the conformational changes of GAT-1 during its transport cycle.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Keshet GI,Bendahan A,Su H,Mager S,Lester HA,Kanner BIdoi
10.1016/0014-5793(95)00859-8subject
Has Abstractpub_date
1995-08-28 00:00:00pages
39-42issue
1eissn
0014-5793issn
1873-3468pii
0014-5793(95)00859-8journal_volume
371pub_type
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