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

FEBS Letters

Wolfger, Hubert²  Martinoia, Enrico¹  Eggmann, Thomas¹  Klein, Markus¹  Schüller, Christoph²  Kuchler, Karl²  Mamnun, Yasmine M.² 

[1] Institut de Botanique, Laboratoire de Physiologie Végétale, University of Neuchâtel, CH-2007 Neuchâtel, Switzerland;Institute of Medical Biochemistry, University of Vienna, Vienna BioCenter, Dr. Bohr-Gasse 9/2, A-1030 Vienna, Austria

关键词: Yeast;    Vacuole;    Glutathione;    ATP-binding cassette transporter;    Detoxification;    Stationary phase;    ABC transporter;    ATP-binding cassette transporter;    DNB-GS;    S-dinitrobenzeneglutathione;    CDNB;    1-chloro-2;    4-dinitrobenzene;    CFTR;    cystic fibrosis transmembrane conductance regulator;    MRP;    multidrug resistance-related protein;    AMP-PNP;    adenosine 5′-(β;    γ-imino)triphosphate;   

DOI  :  10.1016/S0014-5793(02)02767-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown