ARF1 (ADP-ribosylation factor 1) is a protein in the ARF gene family that is responsible for vesicular trafficking within the cell through its activation of phospholipase D. It is found in the cells golgi apparatus and its main function is intra-Golgi transport within the cell. Arf1 is a GTP-binding protein and is known to activate ArfGEF (guanine nucleotide exchange factor) which is a cholera toxin catalytic subunit. Arf1 also modulates budding and uncoating within the Golgi complex. When Arf1 is deactivated, the entire Golgi complex is redistributed to the endoplasmic reticulum, which shows that it plays a major role in protein trafficking in the cell.
ARF1 is found on the 1q47 chromosome region, and has been involved in several interesting studies. In a recent study (1), it is suggested that BFA (Brefeldin A) interaction with ArfGEF has a cytotoxic effect on cells and could possibly be a new treatment for certain cancers. The focus of this study was to find the inhibitors of the Arf1-ArfGEF interaction that show antitumor behavior, but that are very chemically different from the protein BFA, since BFA has a very poor bioavailability and has not progressed very far in drug development. To do this, they studied 39 different cell lines and compared them to a drug sensitivity data base, and through a series of experiments, concluded that AMF targets Arf1 activation, inhibits the Golgi system, and suggests that it may be a novel drug treatment in cancer therapies.
Shannon Cain
Professional Research Assistant
University of Colorado Denver
