ADP-ribosylation factor interacting protein 1 (ARFIP1)

ADP-ribosylation factor interacting protein 1 (ARFIP1), also known as Arfaptin-1, is a BAR domain–containing protein that coordinates membrane trafficking events within cells[2][1][5]. ARFIP1 has the ability to bind phosphatidylinositol-4-phosphate and interact with activated ADP-ribosylation factors (ARFs), localizing primarily to the trans-Golgi network, Golgi membrane, and cytosol[1][2][7]. Its main role is regulating the formation and release of secretory granules—such as insulin granules in pancreatic beta cells—by forming a scaffold at the granule neck, controlling ARF-dependent vesicular fission, and modulating vesicle traffic[1][2][5]. ARFIP1 is phosphorylated by protein kinase D, which inactivates its scaffold function to permit granule release[2]. It is also involved in the negative regulation of retrograde transport and can inhibit ARF activation of downstream enzymes, thus fine-tuning intracellular vesicle sorting and secretion[2]. ARFIP1 has not been established as a direct therapeutic target, and there are currently no known small molecules or drugs specifically targeting this protein[1][5][2].

Other names

ARFIP1Arfaptin-1HSU52521ADP ribosylation factor interacting protein 1arfaptin 1