{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nUVRAG functions as an essential component of the class III phosphatidylinositol 3‐kinase machinery that orchestrates both autophagy and membrane trafficking. Originally identified as the mammalian counterpart of yeast Vps38, UVRAG assembles with Beclin 1 and VPS34 into distinct complexes that govern autophagosome initiation versus endosomal and lysosomal fusion. Structural studies demonstrate that UVRAG promotes the conversion of unstable Beclin 1 homodimers into active heterodimers, thereby stimulating lipid kinase activity and facilitating downstream events such as autophagosome maturation, receptor degradation, and reticulophagy. Regulation by nutrient‐sensitive kinases (e.g. mTORC1), as well as by ubiquitination/deubiquitination cascades, further refines UVRAG’s role in these membrane‐remodeling processes, with additional modulation observed during viral infection and Golgi‐derived membrane dynamics."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "10"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its pivotal role in autophagy, UVRAG exerts significant tumor‐suppressive functions by maintaining genomic stability and proper cell division. It facilitates nonhomologous end joining for DNA double‐strand break repair and ensures centrosome integrity, thereby preventing aneuploidy. In parallel, UVRAG interacts with apoptosis regulators such as Bax – limiting its translocation to mitochondria and tempering cell death induced by genotoxic or therapeutic stress. Moreover, frameshift mutations and decreased expression of UVRAG have been detected in various cancers, impairing its ability to regulate receptor turnover, cytokinesis, and nucleotide excision repair; these defects contribute to tumor progression and treatment resistance."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "11", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nUVRAG expression and function are further fine‐tuned by a network of microRNAs and post‐translational modifications that impact cellular outcomes in diverse disease contexts. For example, targeting by miR‐183, miR‐125b, miR‐216b, and miR‐1183 modulates UVRAG levels, thereby affecting autophagic flux, apoptotic sensitivity, and drug response in colorectal cancer, melanoma, and autoimmune conditions. In addition, UVRAG participates in specialized processes such as melanogenesis via stabilization of BLOC‐1 complexes and in viral entry through its collaboration with endosomal tethering and SNARE proteins. Its interaction with adaptor proteins like Grb2 further underscores a multifaceted role in coordinating vesicular trafficking and stress responses across various cell types."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "23", "end_ref": "31"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Chengyu Liang, Jong-soo Lee, Kyung-soo Inn, et al. 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