The ATP-binding cassette (ABC) transporter Bpt1p mediates vacuolar sequestration of glutathione conjugates in yeast.
- Klein M Institut de Botanique, Laboratoire de Physiologie Végétale, University of Neuchâtel, CH-2007 Neuchâtel, Switzerland.
- Mamnun YM
- Eggmann T
- Schüller C
- Wolfger H
- Martinoia E
- Kuchler K
- 2002-06-05
Published in:
- FEBS letters. - 2002
ATP-Binding Cassette Transporters
Adenosine Triphosphate
Biological Transport
Cadmium
Dinitrochlorobenzene
Glutathione
Green Fluorescent Proteins
Immunoblotting
Luminescent Proteins
Membrane Proteins
Microscopy, Confocal
Recombinant Fusion Proteins
Saccharomyces cerevisiae
Vacuoles
English
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.
- Language
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- English
- Open access status
- bronze
- Identifiers
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- DOI 10.1016/s0014-5793(02)02767-9
- PMID 12044871
- Persistent URL
- https://folia.unifr.ch/global/documents/239166
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