Arf-GAP with dual PH domain-containing protein 1 (ADAP1)

Arf-GAP with dual PH domain-containing protein 1 (ADAP1) is an enzyme that acts as a GTPase-activating protein (GAP) primarily for the small GTPase ARF6. It features an N-terminal ArfGAP domain, followed by two pleckstrin homology (PH) domains that bind phosphoinositides, allowing ADAP1 to function as a scaffold and regulator of cytoskeletal dynamics, vesicular trafficking, and intracellular signaling. Highly expressed in neurons, ADAP1 is critical for neuronal differentiation, polarity, dendrite branching, and axon specification, working in complex with motor proteins such as KIF13B. Its dysregulation has been implicated in neurodegeneration (notably Alzheimer’s disease, where amyloid β upregulates ADAP1), cancer progression, immune regulation (including HIV latency escape in T cells), cardiovascular remodeling, and increased susceptibility to certain inflammatory diseases. No direct drugs or inhibitors are clinically available that target ADAP1 specifically, and while it is a central cellular regulator, it is not currently considered a classical therapeutic drug target[1][2][3][4][5][6][7].

Other names

Centaurin-alpha-1CENTA1GCS1Lp42IP4ArfGAP with dual PH domains 1centaurin-α1CentA1putative MAPK-activating protein PM25