Schizophrenia is a serious mental illness characterised by impaired perception of reality and changes in behaviour. The molecular background of schizophrenia is not yet fully known. In addition to genetic and environmental factors, protein aggregation is being researched as one of the possible causes of schizophrenia. Protein aggregation occurs when, affected by endogenous and external stresses, cellular mechanisms get disrupted, resulting in protein misfolding and protein aggregates accumulating. EHdomain containing 3 (EHD3) is a protein that has been found to aggregate in the brains of schizophrenia patients. EHD3 is a protein involved in endocytic trafficking and recycling as well as D1 receptor internalization. Full length EHD3 has been shown to aggregate in SH-SY5Y cells, while two constructs lacking the C-terminus of the protein, EHD3 amino acids 1-434 and 1-399, did not aggregate. This implied that amino acids 435-535, representing its EH domain, were required for aggregation. Also, full length EHD3 has been shown to induce EHD3 1-399 to aggregation when co-expressed. In this thesis we aimed to determine if the EH domain aggregates independently and if it would co-aggregate when co-expressed with full length EHD3. When expressed individually, EHD3 435-535 did not aggregate, implying that the EH domain is not sufficient for EHD3 aggregation by itself. When coexpressed with full length EHD3, EHD3 1-399 and EHD3 1-434 the EH domain also did not aggregate, which might imply that while the EH domain is necessary for the initialization of EHD3 aggregation, other structural regions like the helical and/or the G domain interact and recruit other molecules that make up the aggregates. Future research is needed to determine which EHD3 regions interact with the EH domain causing the protein to aggregate and co-aggregate in the cell.