ADP-ribosylation factor 5 (ARF5)

ADP-ribosylation factor 5 (ARF5) is a small GTP-binding protein in the ARF family, functioning as a molecular switch in protein trafficking, particularly within the Golgi apparatus. It cycles between inactive GDP-bound and active GTP-bound states, regulated by GEFs and GAPs. Upon activation, ARF5 recruits coat proteins, remodels membrane lipids, and helps drive the formation and uncoating of vesicles, impacting both secretory and endosomal membrane systems. The ARF GTPase family is classified into subgroups (ARF1-3 as type I, ARF4-5 as type II), with ARF5 sharing functions related to membrane association and curvature generation. ARF5 and related proteins are key for maintaining cell homeostasis, and their dysregulation is implicated in diseases related to membrane trafficking, organelle structure, and cytoskeletal dynamics[7][9][3][4][11][8]. No major spelling or conceptual errors are present with "ARF GTPase 5", but "ADP-ribosylation factor 5" (ARF5) is the standardized nomenclature. Currently, no specific drugs selectively target ARF5 in clinical use or investigation.

Other names

ARF5ADP-ribosylation factor 5

Inhibition or modulation of GEFs (guanine nucleotide exchange factors) or GAPs (GTPase activating proteins) that regulate ARF5 cycle between active (GTP-bound) and inactive (GDP-bound) forms[6][1] Modulating ARF5 affects membrane trafficking and vesicle formation processes[3][6]