Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 2 (APPL2)

Adaptor protein, phosphotyrosine interacting with PH domain and leucine zipper 2 (APPL2) is a multifunctional adapter protein characterized by a BAR domain (important in membrane curvature sensing), a central PH domain, and a C-terminal phosphotyrosine-binding (PTB) domain[2]. It binds small GTPases, including Rab5, and interacts with various receptors and signaling proteins to regulate cellular processes such as endosomal trafficking, cell proliferation, F-actin remodeling, and signal transduction[1][2]. In pancreatic β-cells, APPL2 is a critical regulator of glucose-stimulated insulin secretion via modulation of Rac1-mediated actin depolymerization. APPL2 also plays roles in the immune response by influencing phagocytosis and inflammatory signaling pathways, and negatively regulates adiponectin signaling and insulin sensitivity in metabolic tissues[1][2][3]. Genetic alterations or dysregulation of APPL2 activity have been linked to metabolic disorders and rare syndromic diseases, but APPL2 itself is not considered a direct pharmacological target[1][2][3].

Other names

DCC-interacting protein 13-betaDIP13BDip13-betaFLJ10659Adapter protein containing PH domain, PTB domain and leucine zipper motif 2DCC-interacting protein 13 betaadaptor protein, phosphotyrosine interaction, PH domain and leucine zipper containing 2