Alzheimer’s disease is the most prevalent neurodegenerative disorder. A hallmark of the disease is the abnormal accumulation of the Tau protein into aggregates in neurons in affected regions of the brain. This characteristic feature is also found in other neurodegenerative diseases which are collectively known as tauopathies. In normal conditions, Tau binds dynamically to microtubules aiding in their assembly and stability, dependent on the phosphorylation state of the protein. In disease-affected neurons, hyperphosphorylation leads to the accumulation of the Tau protein into aggregates, which have been seen to colocalise with other disease proteins in neurodegeneration. One such protein is α-synuclein, the main constituent of aggregates in Parkinson’s disease. We have genetically modified the model organism Dictyostelium discoideum to express human Tau protein alone and in combination with alpha-synuclein. D. discoideum is a well characterised model organism for studying human diseases, including neurodegeneration and its cellular processes are comparable to our own. Our results indicate that tau interacts with tubulin and can be phosphorylated in D. discoideum. DuolinkTM immunofluorescence experiments suggest that Tau interacts with tubulin throughout the cell in D. discoideum, and with the α-synuclein protein at the cortex. The expression of tau has no effect on growth rates on plates but causes a moderate phototaxis defect. When Tau is co-expressed with α-synuclein it rescues a previously seen α-synuclein-mediated growth defect and produces a more severe defect in phototaxis than with tau alone. Through direct measurements of mitochondrial respiration tau is seen to impair ATP synthesis, α-synuclein increases mitochondrial respiration and the co-expression of the two proteins leads to normally functioning mitochondria. This indicates an interaction between the two proteins. Together these results suggest that D. discoideum could be a viable simple model system for the study of tauopathies and interactions of human proteins involved in neurodegeneration.