Arf-GAP with SH3 domain, ankyrin repeat and PH domain-containing protein 1 (ASAP1)

ASAP1 (Arf-GAP with SH3 domain, ankyrin repeat and PH domain-containing protein 1) is a multidomain protein functioning as a GTPase-activating protein for ADP-ribosylation factors (Arfs), key regulators of membrane trafficking and cytoskeletal dynamics. ASAP1 contains BAR, PH, zinc finger, ankyrin repeat, proline-rich, and SH3 domains, allowing it to act as a hub integrating signals from the actin cytoskeleton and the plasma membrane. It directly binds F-actin, organizes actin bundles, and stabilizes them, affecting cell adhesion, migration, and invasion. ASAP1 localizes to focal adhesions, invadopodia, and similar structures central to cell motility and is implicated in cancer metastasis due to its role in enhancing cell invasiveness and migration. While ASAP1 is considered a promising research target for therapeutic development—particularly in oncology—there are currently no approved drugs targeting ASAP1 directly

Other names

ASAP1DDEF1KIAA1249PAG2ARF GTPase-activating protein 1DEF-1Differentiation-enhancing factor 1PAPZG14PCENTB4130 kDa phosphatidylinositol 4,5-bisphosphate-dependent ARF1 GTPase-activating proteinADP-ribosylation factor-directed GTPase-activating protein 1Development and differentiation-enhancing factor 1PIP2-dependent ARF1 GAPcentaurin beta 4AMAP1

No drugs directly target ASAP1 in clinical use; however, inhibition of ASAP1 or disruption of its protein-protein interactions could hypothetically modulate ARF signaling, cytoskeletal dynamics, or cell migration