Migrating with Myosin VI

Myosin VI

The recent discovery that the class VI myosin is minus end-directed (Schliwa, 1999; Wells et al., 1999) allows new mechanisms of actin-based motility to exist in cells. This will prompt reexamination of a broad range of cell movements previously difficult to explain by conventional force generating mechanisms. Myosins are a large family of molecular motor proteins divided into 15 or more classe...

Myosin VI: a multifunctional motor.

Myosin VI moves towards the minus end of actin filaments unlike all the other myosins so far studied, suggesting that it has unique properties and functions. Myosin VI is present in clathrin-coated pits and vesicles, in membrane ruffles and in the Golgi complex, indicating that it has a wide variety of functions in the cell. To investigate the cellular roles of myosin VI, we have identified a v...

Vi. the Spreading of Myosin

Model for processive movement of myosin V and myosin VI

Myosin V and myosin VI are two classes of two-headed molecular motors of the myosin superfamily that move processively along helical actin filaments in opposite directions. Here we present a hand-over-hand model for their processive movements. In the model, the moving direction of a dimeric molecular motor is automatically determined by the relative orientation between its two heads at free sta...

Porcine myosin-VI: characterization of a new mammalian unconventional myosin

We have cloned a new mammalian unconventional myosin, porcine myosin-VI from the proximal tubule cell line, LLC-PK1 (CL4). Porcine myosin-VI is highly homologous to Drosophila 95F myosin heavy chain, and together these two myosins comprise a sixth class of myosin motors. Myosin-VI exhibits ATP-sensitive actin-binding activities characteristic of myosins, and it is associated with a calmodulin l...