{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMYO5B is an unconventional type V myosin motor protein that plays a central role in the intracellular trafficking and recycling of membrane proteins. By directly interacting with specific Rab GTPases—including Rab11, Rab8, and Rab10—it helps recruit and guide discrete vesicle populations along actin filaments to appropriate docking sites at the plasma membrane. Detailed biochemical and structural studies demonstrate that the MYO5B globular tail binds cargo adaptors, organizes recycling endosomes, and even regulates critical steps such as clathrin‐independent recycling and tethering of nascent vesicles. Collectively, these studies underscore MYO5B’s essential function in orchestrating targeted vesicle transport and recycling in polarized cells."}, {"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": "\nIn epithelial tissues, precise MYO5B‐dependent trafficking is critical for the establishment and maintenance of apical–basolateral polarity. Loss‐of‐function mutations in MYO5B disrupt the targeted delivery of apical proteins—such as the transferrin receptor, CFTR, and ATP7B—and this mis‐trafficking underlies the pathogenesis of microvillus inclusion disease (MVID) as well as abnormal bile canalicular formation and cholestasis. Disrupted recycling further compromises cell–cell junction integrity and general epithelial homeostasis, as evidenced by altered distribution of polarity markers in patients and experimental cell models. These findings highlight that proper MYO5B activity is indispensable for maintaining epithelial structure and function."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "20"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its canonical role in vesicle transport and epithelial polarity, emerging evidence links MYO5B dysfunction to a spectrum of human disorders. Genetic association studies have implicated MYO5B variants in neuropsychiatric conditions such as bipolar disorder and schizophrenia and even neurodevelopmental traits like dyslexia. In addition, altered MYO5B expression contributes to tumor biology in gastrointestinal and endometrial cancers, suggesting a tumor‐suppressor role, while MYO5B dysregulation has also been shown to affect nuclear functions, cell division orientation, and viral protein trafficking in coronavirus infections. Moreover, interactions with chaperones like UNC45A further modulate its function in complex tissue contexts. These multifaceted roles highlight MYO5B as a critical nexus in coordinating intracellular transport with cellular homeostasis and disease susceptibility."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "21", "end_ref": "33"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "L A Lapierre, R Kumar, C M Hales, et al. 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