A hallmark of neurodegenerative diseases like Alzheimer's, Parkinson's and Huntington's disease is the accumulation of misfolded proteins in neuronal cells. These improperly folded proteins become toxic to the cells and can cause neuronal cell death if not properly disposed of. Disposal of proteins in a cell is also known as degradation. All cells have four pathways it can utilize to degrade proteins when they accumulate in the cell. The pathways are Macro-autophagy, Endosomal micro-autophagy, Chaperone mediated autophagy, and Proteasome degradation. Proteins degraded by these pathways are not randomly targeted to one of the four pathways. A protein is most often specifically targeted to and degraded by only one pathway. However, it is unknown what makes a specific protein a target of each of these pathways. My research aims to better understand why a specific protein would be disposed of at one pathway over another. To test this question, I have created three mice cell lines expressing three different proteins of interests each tagged with Green Fluorescent Protein (GFP). The level of fluorescence in the cell can then be measured via Flow Cytometry or Western Blot technology to indicate the amount protein in the cell. Measuring fluorescence after treatment of the cells with chemical drugs that block each of the four degradative pathways can reveal the degradative fate of these proteins. Through characterization of the degradation of these three target proteins insight can be gained into how the cells four degradation pathways chose what proteins to target. Better understanding and characterization of the pathway's cells utilize to degrade proteins can reveal potential targets for therapeutic drug treatments of neurodegenerative diseases that affect millions.