Arf-GAP domain and FG repeat-containing protein 1 (AGFG1)

Arf-GAP domain and FG repeat-containing protein 1 (AGFG1) is a nucleoporin-related protein that regulates vesicular trafficking and nucleocytoplasmic transport in mammalian cells[1][3][4]. AGFG1 is essential for the docking and fusion of proacrosomic vesicles during sperm development; its absence causes acrosome loss and male infertility[1]. It acts as a clathrin adaptor and mediates retrieval and recycling of SNARE proteins such as VAMP7 via clathrin-coated vesicles[1]. Importantly, AGFG1 is a critical host factor for HIV-1 and Influenza A virus replication, required for the nuclear export of viral RNAs through direct interaction with the HIV-1 Rev protein[2][3]. AGFG1 localizes mainly at the perinuclear region, plasma membrane, and cytoplasm, and may play a broader role in RNA and protein transport, with evidence of interaction with adaptors such as EPS15[2][3]. AGFG1 is nonessential for general cell survival but is indispensable for specific trafficking processes and viral lifecycles.

Other names

HRBRIPRABHIV-1 Rev-binding proteinNucleoporin-like protein RIPRev-interacting proteinRev/Rex activation domain-binding proteinhRIPArfGAP with FG repeats 1

Not classically drugged, but viral proteins (notably HIV-1 Rev) bind and exploit AGFG1 for nuclear export of incompletely spliced RNAs[1][2][3][4]. Targeting the AGFG1-Rev interaction has been proposed as an antiviral strategy[2].