{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nSorting nexin 27 (SNX27) is a multifunctional endosomal adaptor protein uniquely characterized by the presence of a PDZ domain in addition to its phosphoinositide‐binding (PX) domain. SNX27 couples PDZ‐binding motifs present in many transmembrane receptors and transporters to the retromer and WASH complexes, thereby facilitating selective endosome‐to–plasma membrane recycling and preventing lysosomal degradation. Structural and proteomic studies have elucidated that the SNX27 PDZ domain directly engages with cargo motifs—as well as with retromer subunits such as VPS26—to enhance cargo affinity via cooperative binding determinants, including acidic residues and phosphorylation‐dependent switches. This core function underpins its role as a major hub in maintaining cell surface receptor levels and cellular nutrient homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "7"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its central recycling role, SNX27 modulates diverse signaling pathways and cellular processes in multiple cell types. In neurons, SNX27‐mediated recycling of receptors—including NMDA receptor subunits and proteins critical for synapse organization—contributes to synaptic plasticity and cognitive function. In T lymphocytes, SNX27 governs the polarized delivery of signaling molecules and transporters at the immunological synapse by interacting with effectors such as diacylglycerol kinase ζ and β‑Pix, thereby fine‐tuning receptor signaling, cell motility, and metabolic reprogramming. Furthermore, by controlling the surface levels of transporters like GLUT1 and ASCT2, SNX27 influences nutrient uptake and mTOR activation, while its regulation of ion channels such as Kir3 channels underscores a broader impact on membrane excitability and cell function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "19"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of SNX27 function has emerged as an important contributor to human disease and specialized cellular responses. SNX27 deficiency or altered cargo interactions have been implicated in neurodegenerative and neurodevelopmental disorders by perturbing glutamate receptor trafficking and compromising synaptic integrity. In addition, pathogens and viral oncoproteins exploit SNX27’s adaptor functions: for instance, HPV E6 proteins disrupt SNX27 binding to key partners, thereby modulating intracellular receptor turnover and enhancing cell proliferation, while SNX27 also plays a role in controlling the surface availability of receptors such as ACE2, thus influencing viral entry pathways. Moreover, SNX27 regulates receptor recycling in glial cells—impacting pathways such as GPR17‐mediated oligodendrocyte differentiation—and its structural versatility is underscored by recent crystallographic studies of its PX domain. 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