Disease relevance of AQY1

• Perhaps as a result, there was no difference between the virulence of C. albicans wild-type and aqy1 null strains in a murine model for systemic candidiasis [1].

High impact information on AQY1

• Here, we show that expression of AQY1 is stimulated during sporulation and that the Aqy1 protein is detectable exclusively in spore membranes [2].
• Taken together, we demonstrate a functional role of an aquaporin in gametogenesis, as well as in the formation of durable structures such as spores, a role that may have wider biological and medical implications [2].
• The Saccharomyces cerevisiae genome database contains two ORFs with homology to aquaporins, AQY1 and AQY2 [3].
• Comparison of these strains revealed that the aquaporin null cells were more aggregated and their surface was more hydrophobic [3].
• As a result, the aquaporin null cells were more flocculent and more efficient at haploid invasive growth [3].

Biological context of AQY1

• The Candida albicans genome database contains one ORF with homology to aquaporins, AQY1 [1].
• Oocytes injected with wild-type AQY1 cRNAs exhibit high Pf values, whereas oocytes injected with AQY1 cRNAs from laboratory strains exhibit low Pf values and have reduced levels of Aqy1p due to two amino acid substitutions [4].
• Genomewide gene expression analysis and Northern analysis of different freeze-resistant and freeze-sensitive strains have now revealed a correlation between freeze resistance and the aquaporin genes AQY1 and AQY2 [5].
• However, unlike Saccharomyces, there was no effect on the cell surface hydrophobicity, flocculation or cell aggregation in aqy1 null C. albicans cells [1].
• Phenotypes of aquaporin mutants in genetically altered mice [6].

Anatomical context of AQY1

• AQY1 from laboratory and wild-type strains of Saccharomyces were expressed in Xenopus oocytes to determine the coefficients of osmotic water permeability (Pf) [4].
• Aquaporin water channel proteins mediate the transport of water across cell membranes in numerous species [4].
• Pf measurements in yeast spheroplasts confirmed the presence of functional water channels in Sigma1278b and a pharmacological study indicated that this strain contains at least a second functional aquaporin [7].

Associations of AQY1 with chemical compounds

• We showed that the defect in the yeast glycerol plasma membrane transporter is complemented by a plant cDNA encoding the aquaporin BobTIP1;1 which is localized in the vacuolar membrane of the complemented yeast cells [8].
• We have now obtained direct evidence that selected aquaporin homologues from plants and mammals have the capacity to channel H(2)O(2) across membranes [9].

Analytical, diagnostic and therapeutic context of AQY1

• To further explain the phosphorylation of PvTIP3;1, we overexpressed this aquaporin in the methylotrophic yeast Pichia pastoris and purified the hexahistidine-tagged protein by immobilized metal affinity chromatography [10].

References