Disease relevance of PDR16

• Deletion of PDR16 resulted in hypersensitivity of yeast to azole inhibitors of ergosterol biosynthesis [1].

High impact information on PDR16

• The azole sensitivity of the PDR16-deleted strain may be the result of imbalanced ergosterol synthesis [1].
• Collectively, our results indicate that PDR16 and PDR17 control levels of various lipids in various compartments of the cell and thereby provide a mechanism for multidrug resistance unrecognized so far [1].
• The Saccharomyces cerevisiae open reading frame YNL231C was recently found to be controlled by the multiple drug resistance regulator Pdr1p [1].
• PDR16-mediated azole resistance in Candida albicans [2].
• To address this question, we deleted both alleles of PDR16 in an AR clinical strain overexpressing the three genes, using the mycophenolic acid resistance flipper strategy [2].

Biological context of PDR16

• Our results show that the homozygous pdr16Delta/pdr16Delta mutant is approximately twofold less resistant to azoles than the parental strain whereas reintroducing a copy of PDR16 in the mutant restored azole resistance, demonstrating that this gene contributes to the AR phenotype of the cells [2].

Anatomical context of PDR16

• Sfh1p was detected in the nucleus and Sfh3p in lipid particles and in microsomes [3].

References