In the C-terminal region of the protein, the intrinsically disordered domain and a prion-like motif are located, which are regions implicated in the aggregate proteinopathy \cite{Yang_2010}. TDP-43 has a nuclear localization signal (NLS). Both the NTD and NLS are important regions for the nuclear localization of the protein as deletion results in its mislocalization from the nucleus to the cytoplasm where it forms cytoplasmic inclusions. In ALS, TDP-43 forms aberrant aggregates in both neurons and glia \cite{Fernandopulle_2019}. Within the CTD is a glycine rich region that is involved in protein-protein interactions and binding to heterogeneous nuclear ribonucleoproteins (hnRNPs) and it is in this region that most ALS mutations occur (ref). The TDP-43 NTD was found to form a homodimer in solution that helps prevent the formation of cytoplasmic aggregates and enhances its mRNA splicing functions in the cell nucleus \cite{Jiang_2017}. During cell stress TDPBP relocates to the cytoplasmic stress granules. Although TDP-43 is normally present in the nucleus during pathology it is cleaved and this cleaved form of TDP43 enters the cell cytoplasm. Cell stress granules form in the cytoplasm from mRNA and RNA binding proteins during a stress to the cell such as in the presence of toxins or high temperature. In normal physiology are dynamic structures that can assemble and then be dissembled when the stress subsides. In ALS the stress granules are persistent in motor neurons and lead to degeneration of the motor neurons.