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Uptake and intracellular fate of nona‐arginine peptide in yeast

Cell‐penetrating peptides (CPPs) which are capable of crossing biological membranes are important tools for the delivery of cargo in modern day science and medicine. Mammalian cells are commonly used as model systems to study the uptake mechanism of several CPPs. In contrast, there are very few reports describing the mode of internalization of CPPs in fungal cells. Despite these studies, our understanding of the mechanism of translocation of CPPs in yeast is ambiguous. In this work, we evaluated the uptake of carboxyfluorescein‐labeled nona‐arginine (CF‐R9) CPP into the model yeast Saccharomyces cerevisiae. Translocation of R9 was concentration and time‐dependent and did not largely affect the viability of the cells. Endocytosis was the preferred mode of uptake when the cells were grown at 30 °C. A significant effect on the translocation of R9 was observed in cells treated with chemicals that inhibit energy‐dependent uptake and endocytosis. A substantial reduction in the uptake of the peptide was also observed in mutant cells lacking End3p, an essential protein for endocytosis. Interestingly, as proposed for other cell types, significant direct uptake was not observed in our experimental conditions. To our knowledge, this study for the first time reports the mechanism of translocation of R9 in yeast cells.