| Modification Notes |
The ADP-ribosylation factor (ARF) protein family are structurally and functionally conserved members of the Ras superfamily of regulatory GTP-binding proteins. ARFs influence vesicle trafficking and signal transduction in eukaryotic cells. ARF-dependent regulatory mechanisms include the coordination of spectrin interactions with Golgi membranes and the association of Actin to the Golgi via Rho family-dependent G-protein localization and WASP/Arp2/3 complexes. Additionally, ARFs play a central role in maintenance of organelle integrity, assembly of coat proteins and activation of phospholipase D (PC-PLD). ZNF289 (zinc finger protein 289), also known as ARFGAP2 (ADP-ribosylation factor GTPase activating protein 2), IRZ, Zfp289 or Nbla10535, functions as a GTPase-activating protein (GAP) for ARF family proteins. Localizing to the cytoplasmic side of the Golgi apparatus, ZNF289 contains one ARF-GAP domain and is found associated with COP-I-coated vesicles. |