Abstract
We previously demonstrated that glycine transporters GlyT1 and GlyT2 are differentially affected by toxic benzophenanthridine alkaloids. Using a combination of homology modeling, knowledge of the sensitivity of sanguinarine to sulfhydryl reagents and site directed mutagenesis we show here that the increased sensitivity of human GlyT1c to sanguinarine is abolished by the mutation of only cysteine 475. Inhibition requires the membrane permeable alkaloid alkanolamine, which is consistent with the intracellular location of the targeted cysteine.
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