Schizophrenia is a chronic mental illness, which a great number of patients around the world struggle with daily. The pathology of schizophrenia is still largely unknown, and the purpose of this thesis is to attempt to solve a piece of the schizophrenia puzzle. The role of TRIO and F-actin-binding protein 1 (TRIOBP-1) is the unsolved problem that we are seeking to resolve and, by doing so, contribute to the broader study of schizophrenia. More specifically, the formation of insoluble TRIOBP-1 aggregates is the main point of interest in my research. TRIOBP-1 is a protein that scientists have previously studied in an attempt to discover its role in the proteinopathy of schizophrenia. What this thesis is seeking to accomplish is expand upon the knowledge revolving around this protein which has already accumulated over the years. Specific data must be obtained on the mechanism of protein aggregation and the involvement of the proteasome in the protein's behaviour. My research involved two TRIOBP-1 constructs: a full-length wild type gene with no alterations and a mutant gene with a deletion between amino acids 333 and 340 as well as a deletion of the N-Terminal section (1-59). The two constructs were used to do a comparison against each other and to test how the two constructs behave when placed in different cell lines. The results showed that the mutant variant of the TRIOBP-1 with the aforementioned deletions did not aggregate into any of the cell lines that it was transfected in which proves that those are the regions responsible for aggregation of the full-length TRIOBP-1 plasmid. The impact of inhibiting the proteasome did not impact the number of insoluble protein aggregates which opened the door for further research on how TRIOBP-1 behaves when a combination of stressors is applied. These findings bring us closer to establishing which exact amino acids are prone to aggregation in TRIOBP-1 and open a new chapter in the investigation of the impact of TRIOBP-1 in the broader study of schizophrenia.