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ADP-ribosylation factor-like protein 1 (ARL1) is a small GTPase in the ARF family, primarily associated with the trans-Golgi network, where it acts as a molecular switch cycling between an active (GTP-bound) and inactive (GDP-bound) state[1][3][5][7]. ARL1 plays a critical role in vesicle trafficking and maintenance of Golgi structure by recruiting tethering proteins (e.g., golgins via their GRIP domains)[2][5] and interacting with other small GTPases, GEFs, and GAPs to orchestrate the precise targeting and fusion of vesicles[1][4][7]. Myristoylation of its N-terminal amphipathic helix is essential for its membrane association and function[3][5]. ARL1 is essential for viability in several eukaryotic organisms and its dysregulation disrupts Golgi architecture and membrane trafficking pathways[1][3][5]. No direct links to human disease, approved drugs, or biomarker status have been established for ARL1[5][6].
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