The ATP-binding cassette (ABC) transporter Bpt1p mediates vacuolar sequestration of glutathione conjugates in yeast

Markus Klein, Yasmine M. Mamnun, Thomas Eggmann, Christoph Schüller, Enrico Martinoia, Karl Kuchler

Publications: Contribution to journalArticlePeer Reviewed

Abstract

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. Œ 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
Original languageEnglish
Pages (from-to)63-67
Number of pages5
JournalFEBS Letters
Volume520
Issue number1-3
Publication statusPublished - 2002

Austrian Fields of Science 2012

  • 1060 Biology

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