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ADP-ribosylation factor 4 (ARF4) is a small GTPase of the ARF family within the Ras superfamily, encoded by the *ARF4* gene in humans[1][3][5]. It mainly functions as a molecular switch, cycling between GDP- and GTP-bound states to regulate vesicular trafficking, membrane trafficking specificity, and activation of effectors such as phospholipase D[1][3][4][5]. ARF4 is upregulated in response to Golgi stress, participates in intracellular trafficking from endosomes to the trans-Golgi network, interacts with the epidermal growth factor receptor for downstream signaling, and is essential for the correct delivery of sensory receptors like rhodopsin to cilia[1][3][5]. ARF4 depletion has been shown to modulate cellular resistance to certain pathogens and to affect viral particle trafficking[3]. Although no therapeutic drugs directly targeting ARF4 have been described, its regulatory role in key trafficking and defense pathways makes it of interest for disease research, especially in cancer, infection, and disorders involving ciliary dysfunction[3][5].
Not applicable; no known targeted drugs. Modulation would theoretically impact vesicular trafficking, signal transduction, and possibly viral release and ciliary transport[3].
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