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ADP-ribosylation factor 3 (ARF3) is a member of the ARF family of small guanine nucleotide-binding proteins within the Ras superfamily. Like other ARF proteins, ARF3 functions as a molecular switch, cycling between GDP-bound (inactive) and GTP-bound (active) forms to regulate membrane dynamics. It is centrally involved in vesicle budding, cargo sorting, and membrane trafficking, especially within the Golgi apparatus, where it modulates the assembly of vesicle coat proteins (such as COP-I and adaptin complexes). ARF3, together with its homologs, coordinates critical aspects of protein trafficking, organelle structure, and signal transduction in eukaryotic cells[1][3][4][5][7][8]. While direct pharmacological targeting has not been established, its involvement in fundamental cellular logistics ties ARF3 to diverse diseases characterized by defective membrane trafficking, including certain cancers and congenital disorders[4][6].
Not applicable; no specific drugs target ARF3 in a clinical context as of the latest data
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