ArfGAP with GTPase domain, ankyrin repeat and PH domain-containing protein 2 (AGAP2)

ArfGAP with GTPase domain, ankyrin repeat and PH domain-containing protein 2 (AGAP2) is a multi-domain enzyme that functions as a GTPase-activating protein (GAP) primarily for the ADP-ribosylation factor (Arf) family of small GTPases, especially ARF1 and ARF5. It acts as a key regulator of intracellular trafficking, receptor recycling, and signal transduction by serving as a scaffold for protein complexes that promote endocytosis and recycling of receptors such as the β2-adrenergic receptor and the transferrin receptor. AGAP2 directly influences PI3K/Akt signaling, mediating anti-apoptotic responses, and has been shown to interact with molecules such as β-arrestins, Akt, and ERK, thereby linking membrane trafficking with key survival and mitogenic pathways. AGAP2 is overexpressed and/or amplified in multiple human cancers, where it acts as a proto-oncogene by supporting cell proliferation, invasion, and resistance to apoptosis. It is also associated with neurodevelopmental disorders, further highlighting its role in central signaling cascades.

Other names

CENTG1KIAA0167PIKEGGAP2Centaurin-gamma-1GTP-binding and GTPase-activating protein 2Phosphatidylinositol 3-kinase enhancerAGAP-2arf-GAP with GTPase, ANK repeat and PH domain-containing protein 2Arf GAP with GTP-binding protein-like, ANK repeat and PH domains 2centaurin, gamma 1phosphoinositide 3-kinase enhancer

no direct targeted therapeutics; hypothetical mechanisms would include inhibition of its GTPase-activating function or protein-protein interactions with signaling complexes