TDP‐43 consists of an N‐terminal domain involved in self‐oligomerization, two RRMs, and a glycine‐rich C‐terminal region containing multiple phosphorylation sites and ALS‐/FTD‐associated mutations (Figure4A).[35] Hyperphosphorylated TDP‐43 inclusions are a common feature of various neurodegenerative diseases.[36, 37] To investigate the role of TDP‐43 domains in GAP43 splicing regulation, we co‐transfected truncated TDP‐43 constructs—TDP‐431‐383 (lacking the C‐terminus) or TDP‐4390‐414 (lacking the N‐terminus)—with pEGFP‐4a1 into HEK‐293T cells and performed RT‐PCR. Here, GAP43 is linked to frontotemporal dementia.