Unconventional myosin-10 (MYO10)

Unconventional myosin-10 (MYO10) is an actin-based molecular motor protein distinguished from conventional myosins by its unique tail domain structure, including MyTH4 and FERM domains, and its ability to localize to the tips of filopodia—dynamic, actin-based cell surface protrusions involved in cell migration, adhesion, and signaling[1][2][3][6][7]. MYO10 is broadly expressed in diverse tissues, playing essential roles in embryonic development (notably neural tube closure, eye development, and limb patterning) as well as in adult cellular processes such as the formation of filopodia and invadopodia, phagocytosis, muscle cell fusion, spindle pole positioning during mitosis/meiosis, and regulation of cell-cell junction integrity in epithelia[2][3][4][5][6]. Pathologically, MYO10 is implicated in cancer invasion and metastasis, muscle regeneration failure, developmental malformations, and certain eye disorders[3][4][5][6]. Knockout studies in mice reveal that MYO10 is critical for normal development and tissue homeostasis, with loss-of-function resulting in semi-lethality and specific organ defects[4][5]. No direct pharmacological modulators or drugs are currently known, but MYO10 serves as a biomarker of invasive or aggressive cellular phenotypes in both cancer and muscle repair contexts[3][5].

Other names

Myosin XMyo10Unconventional myosin-XKIAA0799MyoXunconventional myosin-10