ADP-ribosylation factor (ARF) has been implicated as a critical component in the protein secretory machinery in yeast (S. cerevisiae) and mammalian cells. The disruption of the ARF1 gene in yeast causes a defect in N-glycosylation, similar to that seen for yptl mutants, as evidenced by the formation of incompletely glycosylated invertase. The arfl−mutant shows synthetic lethality with yptl-1, sec21-1, and bet2-1, each of which has been shown to cause defects in protein secretion. In NIH 3T3, Chinese hamster ovary (CHO) and normal rat kidney (NRK) cells, immunocytochemical techniques have allowed the localization of ARF to Golgi membranes and Golgi-derived vesicles. In fact, ARF has been shown to be an abundant protein on non-clathrin-coated vesicles. The binding of ARF proteins and β-COP to Golgi membranes has been found to be rapidly and specifically blocked by the addition of brefeldin A, both in vivo and in vitro. © 1995 Elsevier Inc.
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