"Myosin VI is an ATP hydrolysis coupled motor protein involved in many cellular functions including endocytosis, protein secretion and the maintenance of both the Golgi morphology and stereocilia . It is a unique myosin in that it moves to the minus end of an actin filament , while all other myosins move to the plus end . Recently, we proposed that myosin VI moves using three types of steps: large and small forward steps (minus end directed), and backward steps (plus end directed)   . "
[Show abstract][Hide abstract] ABSTRACT: Myosin VI is a processive myosin that has a unique stepping motion, which includes three kinds of steps: a large forward step, a small forward step and a backward step. Recently, we proposed the parallel lever arms model to explain the adjacent binding state, which is necessary for the unique motion. In this model, both lever arms are directed the same direction. However, experimental evidence has not refuted the possibility that the adjacent binding state emerges from myosin VI folding its lever arm extension (LAE). To clarify this issue, we constructed a myosin VI/V chimera that replaces the myosin VI LAE with the IQ3-6 domains of the myosin V lever arm, which cannot fold, and performed single molecule imaging. Our chimera showed the same stepping patterns as myosin VI, indicating the LAE is not responsible for the adjacent binding state.
"These newly discovered myosin-like molecules are referred to as unconventional myosins. There are about 20 classes of these molecules (Krendel and Mooseker, 2005; Hartman and Spudich, 2012). Redowicz and coworker (Karolczak et al., 2014) review the distribution and roles of one of these unconventional myosins, myosin VIA, in healthy and in diseased striated muscle cells. "
"Myosin Superfamily M yosins are actin-dependent molecular motors that utilize the energy of ATP hydrolysis to generate force. The many functions of myosins include cell contractility, cell signaling, endocytosis, vesicle trafficking and protein/ RNA localization [Krendel and Mooseker, 2005; Woolner and Bement, 2009; Hartman and Spudich, 2012]. All myosins share certain structural and functional features, particularly the presence of an actin-binding head domain, which is also responsible for myosin ATPase activity. "
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