Donata Wawrzycka

TL;DR: It is shown by direct transport assays that arsenite uptake is mediated by Fps1p, and the first report describing a eukaryotic uptake mechanism for arsenite and antimonite and its involvement in metalloid tolerance is described.

TL;DR: The finding that the phosphorylation state of aSyn on S129 can alter the ability of cells to clear aSyn inclusions provides important insight into the role that this posttranslational modification may have in the pathogenesis of PD and other synucleinopathies, opening novel avenues for investigating the molecular basis of these disorders and for the development of therapeutic strategies.

TL;DR: Recent advances in understanding of arsenic and antimony transport pathways in eukaryotes are reviewed, including a dual role of aquaglyceroporins in uptake and efflux of metalloids, elucidation of arsenic transport mechanism by the yeast Acr3 transporter and its role in arsenic hyperaccumulation in ferns, identification of vacuolar transporters of arsenic-phytochelatin complexes in plants.

TL;DR: It is shown that the yeast Acr3p mediates not only high-level resistance to arsenite but also moderate tolerance to antimonite, and possesses a dual arsenite and antimonites specificity.

TL;DR: A systematic mutational analysis of all nine cysteine residues present in the Saccharomyces cerevisiae Acr3p found that mutagenesis of highly conserved Cys151 resulted in a complete loss of metalloid transport function and interaction of As(III) with multiple thiol groups in the yeast AcR3p may facilitate As( III) translocation across the plasma membrane.