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

Author(s)

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

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. Π2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.

Organisation(s)

Department of Social and Cultural Anthropology, Department of Biochemistry and Cell Biology, Department of Microbiology, Immunobiology and Genetics

External organisation(s)

Universität Zürich (UZH), Vienna BioCenter , Université de Neuchâtel

Journal

FEBS Letters

Volume

520

Pages

63-67

No. of pages

5

ISSN

0014-5793

Publication date

2002

Peer reviewed

Yes

Austrian Fields of Science 2012

1060 Biology

Portal url

https://ucrisportal.univie.ac.at/en/publications/79cbc5f9-3c70-4291-89fb-4367d5bb2b25