Arf-GAP domain and FG repeat-containing protein 2 (AGFG2)

Arf-GAP domain and FG repeat-containing protein 2 (AGFG2) is a mammalian member of the ArfGAP protein family, containing a zinc-finger Arf-GAP domain, several phenylalanine-glycine (FG) repeats, and asparagine-proline-phenylalanine (NPF) motifs[3]. AGFG2 regulates vesicular trafficking, particularly by facilitating the stimulation-dependent exocytosis of von Willebrand factor (vWF) from Weibel–Palade bodies in endothelial cells upon exposure to phorbol ester or histamine[1][2][3]. It interacts with Eps15 homology (EH) domains and plays a role in the Rev export pathway, which mediates the nucleocytoplasmic transfer of proteins and RNAs[3]. AGFG2 is also highly expressed in the salivary gland and may contribute to exocytosis in other secretory cells. It has been identified as a host factor that influences HIV-1 progression, suggesting potential broader relevance in viral replication or immune response modulation[1][2][3].

Other names

AGFG2HRBLRABRHIV-1 Rev-binding protein-like proteinRev/Rex activation domain-binding protein relatedarf-GAP domain and FG repeat-containing protein 2nucleoporin