The ADP-ribosylation factor 1 (ARFA1) was first identified as a cellular activity required for cholera toxin to ADP-ribosylate the Gs heterotrimeric G protein and exert its toxic effect (Kahn and Gilman 1986; O’Neal et al. 2005). This ADP-ribosylation factor (ARF) activity is shared by several closely related proteins, which were later numbered ARF1–ARF6, although ARF2 (a close relative of ARF1) is present in mice and rats but not in humans (Boman and Kahn 1995). However, the endogenous roles of ARF1–6 do not involve ADP-ribosylation, but rather participation in membrane traffic and organization of the cytoskeleton.
Regulation of ARF1 Activity
ARF1 is a member of the Ras superfamily, which can be divided into five major families: ARF, Rab, Ran, Ras, and Rho (Wennerberg et al. 2005). The members of the ARF family are sometimes called GTPases, but they cannot hydrolyze GTP in the absence of a GTPase-activating protein (GAP) and...
- Boulay PL, Cotton M, Melancon P, Claing A. ADP-ribosylation factor 1 controls the activation of the phosphatidylinositol 3-kinase pathway to regulate epidermal growth factor-dependent growth and migration of breast cancer cells. J Biol Chem. 2008;283:36425–34.PubMedPubMedCentralCrossRefGoogle Scholar
- Krndija D, Munzberg C, Maass U, Hafner M, Adler G, Kestler HA, Seufferlein T, Oswald F, Wichert G. The phosphatase of regenerating liver 3 (PRL-3) promotes cell migration through arf-activity-dependent stimulation of integrin alpha5 recycling. J Cell Sci. 2012;125:3883–92.PubMedCrossRefGoogle Scholar