ADP-ribosylation factor interacting protein 2 (ARFIP2)

ADP-ribosylation factor interacting protein 2 (ARFIP2), also known as Arfaptin-2 or POR1, is a BAR domain–containing adaptor/scaffold protein with key roles in membrane curvature sensing and induction, intracellular trafficking, and signal transduction[1][2]. ARFIP2 is crucial at the trans-Golgi network, where it interacts with small GTPases (including Arl1 and Rac1), regulates actin cytoskeleton organization, and coordinates vesicle formation and cargo secretion[1]. In hepatocellular carcinoma, high ARFIP2 expression promotes tumor cell proliferation, migration, and invasion by inducing EMT and inhibiting autophagy, in part through the PI3K/Akt signaling pathway[2]. ARFIP2 is also implicated in neuroprotection in Huntington’s disease, regulating protein aggregation and proteasome activity through Akt-dependent phosphorylation[1][2]. Its varied cellular roles highlight it as a prognostic marker and an emerging therapeutic target in cancer and potentially in neurodegenerative diseases[2][1][3].

Other names

Arfaptin-2POR1Partner of RAC1ADP ribosylation factor interacting protein 2Partner of RAC1 (arfaptin 2)

Not directly targeted by approved drugs, but ARFIP2 modulates the PI3K/Akt signaling pathway, affecting EMT, autophagy, and cell proliferation[2].