{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMYH10 encodes the nonmuscle myosin II‐B motor protein that plays a central role in actin–myosin contractility. Biochemical and kinetic studies have shown that MYH10’s motor domain has a high ADP affinity and a prolonged duty ratio, enabling sustained, force‐generating interactions with actin filaments. Furthermore, its filament assembly is tightly regulated by site‐specific phosphorylation events that modulate both its motor activity and the dynamic assembly–disassembly cycle, thereby ensuring proper control of contractile forces. These regulatory mechanisms have been elucidated through kinetic characterization and mutational analyses that underscore the precise modulation of MYH10 function."}, {"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 addition to its intrinsic motor properties, MYH10 is critical for establishing and maintaining cellular architecture during migration and mechanosensing. It participates in the formation and alignment of stress fibers and regulates cell polarity, thereby contributing to directional migration on substrates of varying stiffness. Domain‐specific cues—such as those in the tail region that govern filament assembly and subcellular distribution—further enable MYH10 to coordinate processes ranging from the organization of epithelial adherens junctions to the remodeling of the extracellular environment."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "22"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMYH10 is also indispensable for the successful completion of cell division. During cytokinesis, it contributes to the assembly and constriction of the contractile ring, cooperating with scaffolding proteins—such as anillin and survivin—to ensure proper furrow ingression and abscission. These interactions guarantee the spatial and temporal fidelity of cell division, and perturbation of MYH10’s filament assembly (or its regulatory binding interfaces) can lead to cytokinetic failure and abnormal cell morphology."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}, {"type": "fg_f", "ref": "10"}, {"type": "fg_f", "ref": "24"}, {"type": "fg_f", "ref": "17"}, {"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nDysregulation of MYH10 activity has been implicated in a variety of pathological contexts. Genetic alterations—including mosaic and missense mutations in MYH10—have been associated with neurodevelopmental disorders such as autism, while its aberrant persistence in platelets has been linked to hematologic dysfunction. Moreover, altered MYH10 expression and activity are found in several cancers (including glioma, ovarian, and hepatocellular carcinoma) and are thought to contribute to invasive behavior and chemoresistance. MYH10 is also a key determinant in the proper formation of primary cilia and in maintaining the integrity of the cardiovascular system, as evidenced by its altered roles in thoracic aortic aneurysm."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "27", "end_ref": "36"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Fei Wang, Mihaly Kovacs, Aihua Hu, et al. 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