TARDBP and frontotemporal dementia: 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.