Sorting nexin-9 (SNX9)

Sorting nexin-9 is a multifunctional adaptor protein encoded by the *SNX9* gene in humans[1][2][3]. It is a member of the sorting nexin family, characterized by the presence of a phosphoinositide-binding Phox (PX) domain and a Bin-Amphiphysin-Rvs (BAR) domain, which are essential for sensing and inducing membrane curvature[1][5][7]. SNX9 plays a central role in clathrin-mediated endocytosis, acting as a scaffold that recruits dynamin, clathrin, and adaptor complexes such as AP-2 to sites of vesicle formation at the plasma membrane[1][5][7][8]. Its Src homology 3 (SH3) domain mediates interactions with proteins including dynamin and N-WASP, thereby linking vesicle trafficking to actin cytoskeleton remodeling[4][7]. SNX9 is also involved in several cellular processes beyond endocytosis, such as regulation of cell migration, cytokinesis, and angiogenesis, partly by participating in actin polymerization and recycling adhesion receptors[1][6]. In the context of disease, altered SNX9 activity and expression have been linked to enhanced metastasis in cancer, chronic inflammation, and modulation of immune status[6][4]. There are currently no known drugs directly targeting SNX9, and it is not a primary therapeutic target like a receptor or enzyme.

Other names

SNX9Sorting nexin 9Sorting nexin-9SH3PX1