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The ATP‐binding cassette (ABC) transporter Bpt1p mediates vacuolar sequestration of glutathione conjugates in yeast
Author(s) -
Klein Markus,
Mamnun Yasmine M.,
Eggmann Thomas,
Schüller Christoph,
Wolfger Hubert,
Martinoia Enrico,
Kuchler Karl
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02767-9
Subject(s) - atp binding cassette transporter , glutathione , detoxification (alternative medicine) , xenobiotic , transporter , biochemistry , yeast , vanadate , vacuole , chemistry , microbiology and biotechnology , biology , cytoplasm , enzyme , gene , medicine , alternative medicine , pathology
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.