ASRGL1 (asparaginase and isoaspartyl peptidase 1) is a dual-function enzyme that catalyzes the hydrolysis of L-asparagine to L-aspartic acid and ammonia, while also cleaving isoaspartyl dipeptides that can alter protein folding 1. The enzyme requires autocatalytic processing between G167 and T168 for activation, with oligomerization being critical for this process and enzymatic activity 1. ASRGL1 plays essential roles in neuronal function and retinal health, as it prevents TDP-43 protein aggregation by cleaving isoaspartates that make TDP-43 prone to misfolding 2. Loss of ASRGL1 function causes autosomal recessive retinal degeneration, with the G178R mutation leading to photoreceptor loss and progressive vision impairment 34. In disease contexts, ASRGL1 expression is diminished in ALS brain samples, contributing to TDP-43 proteinopathy and neurodegeneration 2. Conversely, ASRGL1 is overexpressed in various cancers including hepatocellular carcinoma, nasopharyngeal carcinoma, and endometrial cancer, where it promotes cell proliferation, invasion, and poor prognosis through cell cycle regulation and metabolic reprogramming 567. These findings highlight ASRGL1's dual role as both a neuroprotective enzyme and a potential oncogene depending on cellular context.