Myosin of the non-motile stereocilia located in the inner ear. It is thought to be functional as a monomer. Note that not all of these genes are active. Myosin light chains are distinct and have their own properties. They are not considered "myosins" but are components of the macromolecular complexes that make up the functional myosin enzymes. Paramyosin is a large, 93-115kDa muscle protein that has been described in a number of diverse invertebrate phyla. Invertebrate thick filaments are thought to be composed of an inner paramyosin core surrounded by myosin. The myosin interacts with actin, resulting in fibre contraction. Paramyosin
Myosin like a dynamic tether, retaining vesicles and organelles in the actin-rich periphery of cells. A recent single molecule in vitro reconstitution study on assembling actin filaments suggests that Myosin V travels farther on newly assembling (ADP-Pi rich) F-actin, while processive runlengths are shorter on older (ADP-rich) F-actin. Myosin VI is an unconventional myosin motor, which is primarily processive as a dimer, but also acts as a nonprocessive monomer. It walks along actin filaments, travelling towards the pointed end (- end) of the filaments. Myosin VI is thought to transport endocytic vesicles into the cell. Myosin VII is an unconventional myosin