Abstract:
:To investigate the structural determinants underlying transport by the glutamate transporter EAAT1, we mutated each of 24 highly conserved residues (P392 to Q415) to cysteine. A majority of these substituted cysteines react with the sulfhydryl-modifying reagent MTSEA, suggesting that they reside in an aqueous environment. The impermeant reagents MTSES and MTSET react with residues at each end of the domain (A395C and A414C), supporting a model that places these residues near the extracellular surface. Substrates and inhibitors block the reaction between MTS derivatives and A395C, and the cosubstrate, sodium, slows reaction of MTSEA with Y405C and E406C. From these results, we propose that this domain forms a reentrant membrane loop at the cell surface and may comprise part of the translocation pore for substrates and cotransported ions.
journal_name
Neuronjournal_title
Neuronauthors
Seal RP,Amara SGdoi
10.1016/s0896-6273(00)80666-2subject
Has Abstractpub_date
1998-12-01 00:00:00pages
1487-98issue
6eissn
0896-6273issn
1097-4199pii
S0896-6273(00)80666-2journal_volume
21pub_type
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