The budding yeast Saccharomyces cerevisiae shows substantial polarity during its growth. Membranes and proteins are constantly transported to the growth sites, almost exclusively mediated by the Myosin motor Myo2p. Myo2p recognizes its cargos by interacting with different cargo-specific adaptors and its function also relies on other accessory proteins. Among them, the kinesin-like protein Smy1p was interesting due to its genetic interactions with sec2, sec4 and myo2 mutants. However, current models have problems reconciling all the previous findings. Whether Smy1p has a function in polarized secretion and how Smy1p exerts its function are largely unknown. To address these questions, different approaches were employed in this research. First, Smy1p localization was determined and I found it to rely on interactions with Myo2p. Further truncation analysis revealed a complicated localization and expression level regulation. Second, Smy1p protein depletion in myo2 conditional mutants was found to cause a massive secretion block and this method can be applied to other mutants like sec2-56, sec4-8 as well. Third, I identified over 30 smy1 mutants in different myo2 sensitized strains, studying of which will greatly increase our understanding of the mechanism underlying Smy1p's function.