ADP-ribosylation factor (ARF) and ARF-like proteins are a family of highly conserved Ras-related GTPases. They share the unique structural device ‘interswitch toggle’, allowing communication from the N-terminus to the nucleotide binding site. These proteins, originally identified as cofactors in the cholera toxin-catalyzed ADP ribosylation of Gs subunits, have been found in all eukaryotes tested so far and are widely expressed in most mammalian tissues. They serve regulatory roles in vesicular traffic, lipid metabolism, microtubule dynamics, and development. Activated ARF stimulates phospholipase D to produce phosphatidic acid. This stimulation and the formation of its product are important in intracellular vesicle formation and trafficking.
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