{"type": "root", "children": [{"type": "p", "children": [{"type": "t", "text": "\nMyo10 is an unconventional, actin‐based motor protein that plays a central role in generating and regulating filopodia. Studies have shown that endogenous Myo10 is indispensable for filopodia formation—its knockdown leads to a dramatic loss of these fine, actin‐rich protrusions while overexpression robustly induces their formation even in cells that normally lack them."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": " In addition, Myo10 transports key actin regulatory proteins, such as Mena/VASP toward the filopodial tips"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "1"}]}, {"type": "t", "text": ", and its PH2 domain binds phosphatidylinositol (3,4,5)-trisphosphate to regulate its own trafficking and dynamic localization within these structures."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "3"}]}, {"type": "t", "text": " Structural studies further demonstrate that the MyTH4–FERM cassette of Myo10 mediates alternative cargo binding—including interactions with receptors like netrin DCC"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "4"}]}, {"type": "t", "text": "—and that during pathogen infection, Myo10 localizes along bacterially induced protrusions, thereby contributing to the extension of membrane processes that facilitate cell-to-cell spread."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "5"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nIn the context of cancer, upregulated Myo10 promotes cell migration, invasion, and metastasis. In mutant p53–driven breast cancer and through its role in invadopodia formation, Myo10 drives the targeted transport of integrins and other adhesion molecules to the protrusive tips, thereby enhancing extracellular matrix degradation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "6"}]}, {"type": "t", "text": " Its expression is tightly regulated by noncoding RNAs—microRNAs such as miR‑124, miR‑340, and miR‑129 suppress Myo10 to attenuate migration"}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "8", "end_ref": "10"}]}, {"type": "t", "text": "—while circular and long noncoding RNAs contribute to its upregulation in osteosarcoma and neuroblastoma."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "11"}]}, {"type": "t", "text": " Moreover, TGF‑β signaling in lung cancer and elevated Myo10 levels in cervical cancer, as well as in lesions of ductal carcinoma in situ and colorectal tumors, correlate with aggressive features and poor prognosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "13", "end_ref": "16"}]}, {"type": "t", "text": "\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nBeyond its functions in cell migration, Myo10 is critically involved in mitotic processes. By interfacing with regulatory proteins such as ADD1, Myo10 contributes to proper spindle assembly and the accurate positioning of centrosomes."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "17"}]}, {"type": "t", "text": " Its activity is modulated by phosphorylation events—exemplified by PCTAIRE-1–dependent phosphorylation of associated factors—and by regulated degradation during mitosis."}, {"type": "fg", "children": [{"type": "fg_fs", "start_ref": "18", "end_ref": "20"}]}, {"type": "t", "text": " These mitotic roles underscore Myo10’s importance in integrating actin and microtubule dynamics to maintain genomic stability.\n"}]}, {"type": "t", "text": "\n\n"}, {"type": "p", "children": [{"type": "t", "text": "\nMyo10 also fulfills diverse physiological roles beyond cancer and cell division. In the nervous system, distinct isoforms—including a headless variant expressed in the brain—regulate dendritic spine formation and synaptic maturation."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "21"}]}, {"type": "t", "text": " Furthermore, its translation is promoted by calmodulin-like proteins"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "23"}]}, {"type": "t", "text": ", an effect that contributes to efficient keratinocyte motility during wound healing"}, {"type": "fg", "children": [{"type": "fg_f", "ref": "24"}]}, {"type": "t", "text": "and to the formation of transzonal projections in ovarian granulosa cells that support oocyte development."}, {"type": "fg", "children": [{"type": "fg_f", "ref": "25"}]}, {"type": "t", "text": "\n"}]}, {"type": "rg", "children": [{"type": "r", "ref": 1, "children": [{"type": "t", "text": "Hiroshi Tokuo, Mitsuo Ikebe "}, {"type": "b", "children": [{"type": "t", "text": "Myosin X transports Mena/VASP to the tip of filopodia."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Biochem Biophys Res Commun (2004)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1016/j.bbrc.2004.04.167"}], "href": "https://doi.org/10.1016/j.bbrc.2004.04.167"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "15158464"}], "href": "https://pubmed.ncbi.nlm.nih.gov/15158464"}]}, {"type": "r", "ref": 2, "children": [{"type": "t", "text": "Aparna B Bohil, Brian W Robertson, Richard E Cheney "}, {"type": "b", "children": [{"type": "t", "text": "Myosin-X is a molecular motor that functions in filopodia formation."}]}, {"type": "t", "text": " "}, {"type": "i", "children": [{"type": "t", "text": "Proc Natl Acad Sci U S A (2006)"}]}, {"type": "t", "text": " DOI: "}, {"type": "a", "children": [{"type": "t", "text": "10.1073/pnas.0602443103"}], "href": "https://doi.org/10.1073/pnas.0602443103"}, {"type": "t", "text": " PMID: "}, {"type": "a", "children": [{"type": "t", "text": "16894163"}], "href": "https://pubmed.ncbi.nlm.nih.gov/16894163"}]}, {"type": "r", "ref": 3, "children": [{"type": "t", "text": "Laure Plantard, Antti Arjonen, John G Lock, et al. 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