The myosin family of motor proteins drive ATP-dependent actin-based motility in eukaryotic cells and contain a conserved amino-terminal motor domain. Myosin VI is an unconventional minus-end-directed myosin involved in the transport of vesicles and organelles within the cell, endocytosis, and organelle biogenesis. The movement of myosin VI and its cargo along actin filaments is unique among myosin family members in its mechanism, its tail domain structure allows it to take larger than predicted steps along the actin filament. Myosin VI has been shown to regulate the polarized delivery of proteins to specialized subcellular locations, including the delivery of EGFR to the leading edge of migrating cells, as well as the delivery of specialized axonal proteins in neurons. Myosin VI has also been shown to mediate activity of the tumor suppressor p53 during DNA damage.
