{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nOPTN functions as a central autophagy receptor in selective autophagy pathways—most notably in mitophagy and the clearance of pathogenic protein aggregates. Upon mitochondrial damage, PINK1‐mediated phosphorylation and parkin‐dependent ubiquitination generate signals that recruit OPTN to the outer mitochondrial membrane. There, its ubiquitin‐binding and LC3‐interacting regions facilitate the assembly of core autophagy machinery (including ULK1, DFCP1, WIPI1, and ATG complexes), thereby promoting the formation and maturation of autophagosomes. In parallel, OPTN is essential for the clearance of ubiquitinated protein inclusions, a process that is tightly regulated by phosphorylation events (for example by TBK1) and is impaired by disease‐associated mutations affecting its ubiquitin recognition."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "15"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its role in autophagy, OPTN acts as an important negative regulator of inflammatory signaling. By binding K63‐linked polyubiquitin chains, it competes with proteins like NEMO in receptor complexes and aids in the recruitment of deubiquitinating enzymes (for example, CYLD), thereby dampening TNFα–induced NF‑κB activation. Phosphorylation of OPTN further modulates these interactions, and mutations that disturb its post‑translational modification (or its inherent binding capacity) result in a failure to properly suppress pro‐inflammatory signaling."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "16", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn addition to its functions in autophagy and inflammatory control, OPTN plays a crucial role in vesicular trafficking and Golgi maintenance. It acts as an adaptor linking motor proteins such as myosin VI to secretory vesicles, thereby regulating endocytic recycling and the fusion of vesicles with the plasma membrane. Furthermore, OPTN has been implicated in cell cycle regulation through interactions that modulate kinases like Plk1, highlighting its multifaceted contribution to overall cellular homeostasis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "24"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinically, mutations and sequence variations in the OPTN gene have been linked to a spectrum of neurodegenerative and ocular disorders—including primary open‐angle glaucoma, normal tension glaucoma, amyotrophic lateral sclerosis, and frontotemporal dementia—where defective OPTN function contributes to impaired autophagic clearance, dysregulated inflammatory responses, and disrupted vesicular trafficking. 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