{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSorting nexin 9 (SNX9) is emerging as a multifunctional adaptor protein that plays a central role in clathrin‐mediated endocytosis. It directly binds to key endocytic factors such as dynamin, clathrin, and the adaptor protein complex AP‑2, thereby promoting the assembly of endocytic complexes at clathrin‐coated pits. In the cytosol, SNX9 forms a complex with dynamin and other accessory proteins, with its recruitment to membranes being tightly regulated by interactions and post‐translational modifications. This dynamic association helps trigger the membrane scission steps that complete vesicle formation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSNX9’s membrane‐remodeling functions are primarily mediated by its tandem Phox homology (PX) and Bin‑Amphiphysin‑Rvs (BAR) domains. These domains confer the ability to sense and induce membrane curvature, molding lipid bilayers into narrow tubules. In vitro and in vivo studies show that SNX9 can tubulate membranes and that its activity is modulated by phosphoinositides, while structural studies have revealed both a flexible and a more rigid BAR conformation. These molecular features not only underpin its role in vesicle formation but also dictate its capacity to recruit proteins such as N‑WASP that drive actin polymerization."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "14"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its classical role in endocytosis, SNX9 is a key player in coupling membrane trafficking with actin cytoskeletal dynamics in immune signaling. In T cells, SNX9 is recruited to clathrin‐coated structures containing costimulatory receptors such as CD28 and interacts with actin‐regulating proteins like WASp; these interactions promote receptor internalization, actin remodeling, and downstream cytokine production. Such functions have been linked to the modulation of T cell activation and even the prevention of exhaustion in adoptively transferred T cells."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "15", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nSNX9 also contributes to other cellular processes beyond classical endocytosis. It plays a role during mitosis and cytokinesis—helping to stabilize kinetochore fiber architecture—and regulates the recycling of adhesion receptors in endothelial cells, thereby influencing cell migration and angiogenesis. Moreover, SNX9 localizes to invadopodia in cancer cells where it modulates extracellular matrix degradation, and its expression levels may serve as an indicator of altered immune status during chronic inflammation."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its individual functions, SNX9 engages in highly specific protein–protein interactions that fine‑tune its activities. It is subject to regulatory mechanisms involving dimerization (with specificity influenced by related sorting nexins such as SNX33), ubiquitylation by E3 ligases like Itch, and cooperative regulation of receptor internalization—as seen in the trafficking of ADAM9 and podocin in podocytes. These interactions underscore SNX9’s role as an integrative scaffold linking membrane curvature, vesicle trafficking, and signal transduction."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "26"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nFinally, SNX9 is exploited by pathogenic as well as physiologically relevant signaling processes. Certain bacterial effectors (e.g. EspF from enteropathogenic Escherichia coli) hijack SNX9 to induce membrane tubulation that facilitates host cell invasion, while in the context of receptor stimulation, SNX9‐mediated membrane deformation is key to propagating signals at the immunological synapse."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "27"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Qiong Lin, Charles G Lo, Richard A Cerione, et al. 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