Recombinant Saccharomyces cerevisiae Pleiotropic ABC efflux transporter of multiple drugs (PDR5), partial

1. These results present new evidence, suggesting that transmembrane helix 2 plays an important role for the efflux function of Pdr5p. PMID: 27189366
2. structural and functional implications for Pdr5 PMID: 27543784
3. High-Copy Overexpression Screening Reveals PDR5 as the Main Doxorubicin Resistance Gene in Yeast. PMID: 26690737
4. Pdr5 analyses are applicable to mammalian asymmetric ABC multidrug transporters, including transporter promiscuity, function of non-catalytic ATP-binding site, description of a transmission interface, and discovery that Pdr5 is a molecular diode. Review. PMID: 25886173
5. Novel phenotype of an S1368A mutant that lies in the putative drug-binding pocket of the yeast multidrug transporter Pdr5. PMID: 25112867
6. We describe here the first attempts to restore complete symmetry in an asymmetric ABC transporter and to study its effects, which might be relevant to the entire class of asymmetric ABC transporters. PMID: 24733388
7. Mutations adjacent to the end of transmembrane helices 6 and 7 independently affect drug efflux capacity of Pdr5p. PMID: 24333836
8. The deviant ATP-binding site of the multidrug efflux pump Pdr5 plays an active role in the transport cycle. PMID: 24019526
9. These results indicate that the S1360F mutation within the transmembrane domain interferes drastically with the ability of the nucleotide-binding domains to hydrolyze ATP by interfering with interdomain crosstalk. PMID: 23464591
10. A mutation in intracellular loop 4 affects the drug-efflux activity of the yeast multidrug resistance ABC transporter Pdr5p. PMID: 22238618
11. activity of Pdr5 in a strain with wild-type PDR1 allele was shown to drop sharply on glucose depletion from the medium and then again at the end of the diauxic shift when the cells are adapted to growth on respiratory substrates. PMID: 15471577
12. Thus, it was found that enniatins are potent and specific inhibitors for Pdr5p, with less toxicities than that of FK506. PMID: 15707993
13. membrane Pdr5p levels diminished rapidly during incubation with high calcium in a manner dependent on calcineurin PMID: 15849433
14. These results suggest that Pdr5 requires a properly folded nucleotide-binding domain for trafficking to the plasma membrane. PMID: 17302805
15. Using purified plasma membrane vesicles, we demonstrate that Pdr5p can use GTP to fuel substrate transport. We propose that Pdr5p increases its multidrug transport substrate specificity by using more than one nucleotide as an energy source. PMID: 17956128
16. provide important insights into the molecular mechanism of Pdr5 and suggest that not solely the transmembrane domains dictate substrate selection PMID: 18356296
17. drug sensitivity of mutant Pdr5 is attributable to the uncoupling of NTPase activity and transport PMID: 18842589

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KEGG: sce:YOR153W

STRING: 4932.YOR153W