{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMYO1C functions as a versatile, non‐conventional motor protein that responds to mechanical tension and organizes membranes at the cell surface. Under low piconewton forces, MYO1C dramatically increases its duty ratio, thereby serving as a molecular force sensor that adapts its motility to cellular tension. In addition, MYO1C is tightly associated with cholesterol‐rich lipid rafts where it drives the formation of recycling tubules and mediates the targeted delivery of raft‐associated cargo such as GPI‐linked proteins. These activities are critical for maintaining plasma membrane plasticity, facilitating cell migration, and modulating processes such as podocyte integrity, vesicular transport at the Golgi, and the initiation or termination of long‐range kinesin-driven runs. Moreover, MYO1C interacts directly with key adhesion proteins (e.g., Neph1 and nephrin) and with actin‐binding partners to regulate focal adhesion dynamics and cell motility."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "1", "end_ref": "8"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the nucleus, the MYO1C isoform NM1 participates in the regulation of gene transcription and chromatin remodeling. NM1 is a component of multiprotein assemblies such as the B‐WICH complex, where it cooperates with chromatin remodeling factors (WSTF, SNF2h) to facilitate RNA polymerase I and III transcription and proper rRNA synthesis. Its recruitment to chromatin is intricately regulated by actin interactions, calcium–calmodulin binding, and post‐translational modifications such as GSK3β‐mediated phosphorylation that stabilize NM1 and promote a permissive chromatin state. In addition, NM1 associates with nuclear export complexes and even interfaces with viral transcription regulators, thereby modulating both the spatial organization of ribonucleoprotein particles and the cell cycle."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "9", "end_ref": "17"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nClinical and structural studies have further highlighted the diverse roles of MYO1C in human disease. Mutations or dysregulated expression of MYO1C have been linked to sensorineural hearing loss and malocclusion, underscoring its importance in both cytoplasmic trafficking and nuclear functions. In cancer, MYO1C can act either as a tumor suppressor or as an oncogenic factor depending on the cellular context. For example, miRNA-mediated downregulation of MYO1C contributes to decreased proliferation and migration in gastric cancer, whereas stabilization of MYO1C by noncanonical ubiquitination facilitates actin remodeling and promotes metastasis in prostate cancer. In addition, truncated forms of MYO1C have emerged as potential biomarkers in autoimmune disorders and even severe COVID-19, and aberrant secretion of MYO1C via extracellular vesicles has been implicated in glioma invasion."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "28"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Joseph M Laakso, John H Lewis, Henry Shuman, et al. 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