Abstract
Trans-activation response DNA-binding protein 43 (TDP-43) is a major constituent of proteinaceous inclusions characteristic of most forms of amyotrophic lateral sclerosis (ALS) and ubiquitin positive frontotemporal lobar degeneration (FTLD). Normally, TDP-43 is a nuclear protein; in the disease-state it translocates to the cytoplasm, forming pathogenic inclusions. In addition to the mislocalization and aggregation, TDP-43 undergoes phosphorylation, stress granule co-localisation and cleavage. We have characterized an ALS cell model to investigate these key pathological hallmarks of ALS at the molecular level using confocal imaging, thus laying the foundation to better understand TDP-43 aggregation.
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