{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nVPS35 is a core component of the retromer complex that orchestrates the retrieval and recycling of transmembrane proteins from endosomes back to the trans‐Golgi network and plasma membrane. Acting as a scaffold within the cargo‐recognition trimer (with VPS26 and VPS29), VPS35 adopts a horseshoe‑shaped α‑helical solenoid structure that organizes multiple binding interfaces for cargo proteins, sorting nexins, and regulatory factors such as Rab7 and the actin‐nucleating WASH complex. This assembly underlies fundamental processes including the endosome‐to‑Golgi transport of receptors like the cation‑independent mannose‑6‑phosphate receptor and DMT1, as well as trafficking linked to mitochondria‐derived vesicles."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "9"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nPerturbations of VPS35 function—most notably through pathogenic missense mutations such as D620N—are implicated in neurodegenerative disorders, particularly Parkinson’s disease. In affected neurons, VPS35 mutations disrupt its association with regulators (for example, the WASH complex), impairing the formation of transport carriers and leading to altered endosomal morphology. Such defects compromise the recycling and trafficking of critical cargoes, result in abnormal dopamine receptor and mitochondrial protein handling, and enhance LRRK2 kinase activity, thereby contributing to mitochondrial fragmentation, defective autophagy, and ultimately neurodegeneration. Genetic and cellular analyses in patient‐derived cells, animal models, and even Drosophila have underscored that VPS35 dysfunction not only perturbs endosome–TGN trafficking but also adversely affects synaptic transmission and receptor recycling, thereby amplifying neuronal vulnerability."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "10", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its classical role in endosomal recycling, VPS35 exerts diverse functions in other cellular contexts. It regulates the trafficking of viral envelope glycoproteins—as exemplified by its role in HIV‐1 Env incorporation into virions—and modulates signaling pathways via interactions with Ras and type‑I interferon receptors, thereby influencing MAPK and JAK/STAT signals. Moreover, altered VPS35 expression and mutations have been linked to oncogenic processes in hepatocellular carcinoma and to motor neuron degeneration in amyotrophic lateral sclerosis, underscoring its broader relevance to cellular homeostasis and disease pathogenesis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "37", "end_ref": "43"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Raul Rojas, Satoshi Kametaka, Carol R Haft, et al. 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