ADP-ribosylation factor (ARF) family of small GTP-binding proteins are involved in vesicular transport regulation and in controlling cytoskeletal organization and cell adhesion. These proteins are best characterized as regulators of membrane traffic. The Centaurin GTPase-activating protein family comprise a subset of ARF regulatory molecules that transduce PI 3-kinase activation into coordinated control of Arf-dependent pathways. This family includes ASAP1, ACAP1, ACAP2, AGAP1, ARAP1, ARAP2, Centaurin a1 and Centaurin g3. The Centaurin a1 protein is a high affinity PtdIns(3,4,5)P3 binding protein enriched in brain. By acting as a GTPase activating protein for ADP ribosylation factor 6 (ARF6), Centaurin a1 is able to switch off ARF6 and inhibit its ability to mediate b2-adrenoceptor internalization and negatively regulate ARF6 activity by functioning as an in vivo PIP3 dependent ARF6 GAP OTTHUMP00000213337; domain, five PH domains, one Ras-associating domain, one Rho-GAP domain and one SAM (sterile a motif) domain.