ArfGAP with coiled-coil, ankyrin repeat and PH domains 1 (ACAP1)

ArfGAP with coiled-coil, ankyrin repeat and PH domains 1 (ACAP1) is a GTPase-activating protein (GAP) that acts primarily on ADP-ribosylation factor 6 (ARF6), a small GTPase involved in membrane trafficking. ACAP1 is a key component of a clathrin-mediated complex essential for endocytic recycling, especially the regulated recycling of β1-integrin to the plasma membrane. Structurally, it contains GAP, coiled-coil, ankyrin repeat, BAR, and PH domains; the PH domain is critical for membrane deformation, and the BAR domain mediates dimerization and higher-order assembly. Phosphorylation, specifically by Akt, regulates ACAP1’s cargo-binding and autoinhibition. ACAP1 orchestrates membrane remodeling through lattice assembly, fostering transport carrier generation for endosomal recycling. Although primarily studied in cell biology, mutations in ACAP1 have been associated with myoclonic epilepsy in juvenile patients, suggesting relevance in disease. Currently, ACAP1 is not a direct drug target, and no established biomarkers or safety concerns for therapeutic modulation exist

Other names

CENTB1KIAA0050Cnt-b1Centaurin-beta-1ACAP1arf-GAP with coiled-coil, ANK repeat and PH domain-containing protein 1Arf GAP with coiled-coil, ANK repeat and PH domains 1centaurin-beta-1cnt-b1

Not directly targeted by drugs Potential indirect modulation via regulation of ARF6 signaling and Akt-mediated phosphorylation