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ADP-ribosylation factor 1 is a small GTP-binding protein belonging to the Ras superfamily, functioning as a key regulator of vesicular trafficking, primarily at the Golgi apparatus. ARF1 cycles between an active GTP-bound state and an inactive GDP-bound state, with conformational changes critical for its ability to recruit coat proteins (such as COPI) and adaptors that drive vesicle formation, cargo sorting, and membrane curvature. It also interacts with and activates enzymes including phospholipase D. Dysfunction of ARF1 can disrupt membrane traffic and contribute to diseases such as cancer and neurodegenerative disorders. The prototypical ARF inhibitor, Brefeldin A, disrupts ARF1’s function by preventing GDP-GTP exchange, highlighting its role as a drug target.
Inhibition of ARF1 GTPase (by Brefeldin A, leading to disruption of vesicular transport)
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