Vacuolar sequestration or cellular extrusion of glutathione-conjugated xenobiotics and catabolites by ATP-binding cassette (ABC) transporters is an important detoxification mechanism operating in many species. In this study, we show that the yeast ABC transporter Bpt1p, a paralogue of Ycf1p, acts as an ATP-dependent vacuolar pump for glutathione conjugates. Bpt1p, which is inhibited by vanadate and glibenclamide, accounts for one third of the total vacuolar transport of glutathione conjugates. Furthermore, immunoblot analyses show that Bpt1p levels are strongly elevated in early stationary phase, consistent with a function of Bpt1p in vacuolar detoxification.

• PMID: 12044871
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Reference Type

Journal Article | Research Support, Non-U.S. Gov't

Authors

Klein M, Mamnun YM, Eggmann T, Schüller C, Wolfger H, Martinoia E, Kuchler K

Primary Lit For

BPT1

Additional Lit For

YCF1

Review For