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CutA divalent cation tolerance homolog (CUTA) is a multifunctional protein in humans, originally characterized from its bacterial homologue, which has well-established roles in copper and divalent cation tolerance. In mammals, CUTA is involved in protein localization, particularly facilitating the cell-surface expression of acetylcholinesterase essential for neuronal signal transmission, and modulates the trafficking and processing of β-site APP cleaving enzyme 1 (BACE1), attenuating β-amyloid generation implicated in Alzheimer’s disease pathogenesis. Additionally, CUTA acts as a terminal RNA nucleotidyltransferase, adding non-templated nucleotides to mRNA 3′ ends, thus promoting transcript decapping and degradation—a central function in post-transcriptional gene regulation. CUTA binds copper ions and participates in metal homeostasis across diverse organisms, forming trimeric assemblies that aggregate reversibly in the presence of metals. Variants or altered abundance of CUTA have been linked with neurological disorders and other traits, although it is not considered a direct therapeutic target or biomarker at present.
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