ADP-ribosylation factor 6 (ARF6)

ADP-ribosylation factor 6 (ARF6) is a member of the ARF family of small GTPases within the Ras superfamily, functioning as a guanine nucleotide-binding protein that regulates multiple cellular processes. ARF6 is best known for its roles in controlling membrane trafficking—specifically endocytosis, exocytosis, recycling of plasma membrane proteins, and actin cytoskeleton reorganization[1][2]. It operates through a cycle regulated by guanine nucleotide exchange factors (GEFs) and GTPase-activating proteins (GAPs), switching between active (GTP-bound) and inactive (GDP-bound) forms[6]. ARF6 modulates vital signaling pathways, is localized mainly to the plasma membrane, and has well-established involvement in cancer cell invasion, metastasis, and developmental and vascular processes[6]. While ARF6 is considered a promising therapeutic target, direct drug development is in early stages and existing inhibitors are primarily research tools[3]. Key references: ARF6 is classified as a small GTPase, specifically of the ADP-ribosylation factor family (Ras superfamily), and regulates vesicular trafficking, endocytosis, membrane lipid remodeling, and actin dynamics[1][2][6]. Disease role is prominent in cancer (tumor growth, metastasis), vascular instability, and developmental disorders[6]. No approved drugs directly target ARF6, but it is under investigation as a molecular target in oncology and other diseases[3].

Other names

ADP ribosylation factor 6ARF6ADP-ribosylation factor 6ADP-ribosylation factor 6 (human)ARF6 GTPase

Inhibitors and targeting molecules act primarily by blocking ARF6 GTP/GDP exchange or interfering with effector binding[3].