Dsk1 is the Schizosaccharomyces pombe functional homolog of human SRPK1, an SR protein kinase that regulates localization and function of SR protein splicing factors involved in transcription, alternative splicing, and mRNA export. It has been shown that a Dsk1 deletion strain of S. pombe is sensitive to exposure to butylated hydroxyanisole (BHA), a phenol derivative commonly used as a food preservative. Little is known about how BHA interacts with cells on a functional level, although it has been shown to be cytotoxic and tumorigenic. The aims of this thesis are to study the effect of BHA on eukaryotic cells and the possible involvement of Dsk1 protein kinase in the cellular response network to BHA through the use of fluorescence microscopy. The results showed that in BHA-treated cells, Dsk1 exhibits reduced nuclear localization and increased incidence of cytoplasmic clusters as well as a series of changes in cellular morphology. These observations imply that the function of Dsk1 is altered in response to BHA, consistent with genomic data collected by the Tang Lab. Thus, this study provides a basis for a series of future studies that will reveal in more detail how BHA affects fission yeast cells, and potentially gene or protein functional homologs in human cells.