The ADP-ribosylation factor (ARF) family of small GTP-binding proteins are ubiquitously expressed and involved in many cellular events such as cell adhesion, cell migration, neurite outgrowth, cell secretion, endocytosis and exocytosis, and maintenance of the platelet cytoskeleton (D’Souza-Schorey and Chavrier 2006; Ueda et al. 2013; Jang et al. 2016; Urban et al. 2016). In mammals, the ARF family consists of six members (ARFs 1–6) that differ in the localization and function. ARFs 1–5 function at the Golgi, whereas ARF6 regulates cellular events at the plasma membrane (Donaldson and Jackson 2011). ARFs belong to the Ras superfamily of GTPases and therefore act as molecular switches by cycling between inactive GDP-bound and active GTP-bound forms. They depend on Guanine Exchange Factors (GEFs) for activation and GTPase-Activating Proteins (GAPs) for inactivation (Donaldson and...
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