The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins. ARFs influence vesicle trafficking and signal transduction in eukaryotic cells. ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with Golgi membranes and the association of actin to the Golgi via rho family-dependent G-protein localization (Rac, CDC42) and WASP/Arp2/3 complexes. Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins, and activation of phospholipase D. The ARF proteins are categorized as class I (ARF1, ARF2, and ARF3), class II (ARF4 and ARF5) and class III (ARF6); members of each class share a common gene organization. The human ARF1 gene maps to chromosome 1q42, contains 5 exons and 4 introns, and encodes a 181 amino acid protein.