ARFGAP2 (ARF GTPase activating protein 2) functions as a GTPase-activating protein that regulates vesicular trafficking at the Golgi apparatus by hydrolyzing GTP bound to ARF1 1. Unlike ARFGAP1, ARFGAP2 is specifically recruited to Golgi membranes through direct interactions with coatomer proteins, particularly via a basic stretch that binds the γ1-COP subunit, and requires coatomer for its catalytic activity 23. ARFGAP2 is essential for COPI coat assembly and proper vesicle formation, with knockdown studies showing Golgi unstacking and impaired COPI coat lattice formation 4. The protein works redundantly with ARFGAP3 and ARFGAP1 to regulate Golgi-to-ER retrograde transport, as simultaneous depletion of all three causes accumulation of Golgi proteins in the ER-Golgi intermediate compartment and blocks retrograde trafficking 5. Beyond its classical trafficking role, ARFGAP2 has emerged as a critical regulator of STING-mediated immune signaling, promoting STING proton channel activity and cytokine secretion in hematopoietic cells, thereby contributing to autoinflammatory disease pathogenesis 6. The protein also functions in podocytes to suppress Rac1 activity and protect against kidney injury 7.